WO2025217017A1

WO2025217017A1 - Compositions and methods for increasing phosphorous availability

Info

Publication number: WO2025217017A1
Application number: PCT/US2025/023378
Authority: WO
Inventors: Laurel Anne KLUBER; Svend Gunnar Kaasgaard; Lars Kobberoee Skov; Justin HYNICKA
Original assignee: Novonesis Plant Biosolutions AS; Novozymes AS
Current assignee: Novonesis Plant Biosolutions AS; Novozymes AS
Priority date: 2024-04-08
Filing date: 2025-04-07
Publication date: 2025-10-16
Anticipated expiration: 2026-10-08

Abstract

The present invention relates to cleaning compositions comprising polypeptides having peptidoglycan degradation activity, as well as use of the cleaning compositions for cleaning of an item such as a textile or a surface.

Description

COMPOSITIONS AND METHODS FOR INCREASING PHOSPHOROUS AVAILABILITY CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority to U.S. Provisional Patent Application No.63/631,142, filed April 8, 2024, and U.S. Provisional Patent Application 63/695,081, filed September 16, 2024, the disclosures of which are incorporated herein by reference in their entireties. BACKGROUND Phosphorous is vital to plant health and development but much of the phosphorous found in soil is inaccessible to plants because it sequestered and immobilized within mineral deposits and insoluble organic compounds, such as phytates. Global supplies of inexpensive, exogenous phosphorous are dwindling. REFERENCE TO SEQUENCE LISTING This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference. The name of the file containing the Sequence Listing is SQ.XML, which contains 617,645 bytes and which was created on April 7, 2025. SUMMARY OF THE CLAIMED INVENTION The present disclosure provides compositions and methods for catalyzing hydrolysis of phytic acids in plant growth media and fertilizers and other substrates, thereby releasing soluble forms of phosphorous and other minerals. Composition and methods of the present disclosure have many uses, including, but not limited to, increasing the availability of nutrients for plant uptake/accumulation/utilization, reducing the need for exogenous fertilizers, mitigating the effects of phytopathogenic pests and abiotic stressors, and improving plant health/growth/yield. DETAILED DESCRIPTION This description is not intended to be a detailed catalog of all the different ways in which the inventive concepts disclosed herein may be implemented or of all the features that may be added thereto. For example, features illustrated with respect to one embodiment may be incorporated into other embodiments and features illustrated with respect to a particular embodiment may be deleted from that embodiment. In addition, numerous variations and additions to the various embodiments suggested herein, which do not depart from the instant inventions, will be apparent to those skilled in the art in light of the instant disclosure. Hence, the following description is intended to illustrate some embodiments of the instant inventions and not to exhaustively specify all permutations, combinations and variations thereof. The terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting of the instant inventions. Unless otherwise defined, all terms (including technical and scientific terms) used herein have the same meaning as commonly understood by one of ordinary skill in the art to which the inventions belong. It will be further understood that terms, such as those defined in commonly used dictionaries, should be interpreted as having a meaning that is consistent with their meaning in the context of the specification and relevant art and should not be interpreted in an idealized or overly formal sense unless expressly so defined herein. For the sake of brevity and/or clarity, well-known functions or constructions may not be described in detail. As used herein, the singular forms "a," "an," and "the" are intended to include the plural forms as well, unless the context clearly indicates otherwise. As used herein, the terms "acaricide" and "acaricidal" refer to an agent or combination of agents the application of which is toxic to an acarid (i.e., kills an acarid, inhibits the growth of an acarid and/or inhibits the reproduction of an acarid). As used herein, "additive," when referring to effects of combinations within a composition means that the effects of the combinations are generally about the same as the sum of effects of the individual components of the combination alone. The combination of individual components producing this effect may be called an additive combination. As used herein, the term "agronomically acceptable carrier" refers to a substance or composition that can be used to deliver a plant-beneficial agent to a plant, plant part or plant growth medium (e.g., soil) without causing/having an unduly adverse effect on plant growth and/or yield. As used herein, the term "foliar-compatible carrier" refers to a material that can be foliarly applied to a plant or plant part without causing/having an unduly adverse effect on the plant, plant part, plant growth, plant health, or the like. As used herein, the term "seed-compatible carrier" refers to a material that can be applied to a seed without causing/having an unduly adverse effect on the seed, the plant that grows from the seed, seed germination, or the like. As used herein, the term "soil-compatible carrier" refers to a material that can be added to a soil without causing/having an unduly adverse effect on plant growth, soil structure, soil drainage, or the like. As used herein, the term "AlphaFold" refers to AlphaFold version 2 (AlphaFold2, AF2), a computational method for calculating the three-dimensional structure of a polypeptide from its amino acid sequence (Jumper et al., NATURE 596:583–9 (2021)). Three-dimensional structures of millions of polypeptides deposited in the UniProt database have been calculated and deposited in the AlphaFold Protein Structure Database, using the AlphaFold Monomer v2.0 algorithm (Varadi et al., NUCLEIC ACIDS RES. 50(D1):D439–44 (2021)). In the AlphaFold Protein Structure Database, the three- dimensional structure of a polypeptide can be obtained by searching for the UniProt accession number of the polypeptide. In addition to the many three-dimensional structures that are already publicly available, code is available for reproducing and calculating structures of new polypeptides at source code repositories such as Github.com under deepmind/alphafold/, using notebooks/AlphaFold.ipynb, which uses AlphaFold v2.3.1 or newer. Additionally, it can be found in Github.com under sokrypton/ColabFold using v1.5.2 or newer, using AlphaFold2.ipynb. For technical details, please see Jumper et al. (vide supra). AlphaFold 2 produces a per-residue estimate of its confidence on a scale from 0 to 100. This confidence measure is called pLDDT and corresponds to the model’s predicted score on the lDDT-Cα metric. It is stored in the B-factor fields of the mmCIF and PDB files available for download (although unlike a B-factor, higher pLDDT is better). Regions with pLDDT score of more than 90 are expected to be modelled to high accuracy. These should be suitable for any application that benefits from high accuracy (e.g., characterization of binding sites). Regions with a pLDDT score between 70 and 90 are expected to be modelled well, corresponding to a generally good backbone prediction. As used herein, the term "and/or" is intended to include any and all combinations of one or more of the associated listed items, as well as the lack of combinations when interpreted in the alternative ("or"). Thus, the phrase "A, B and/or C" is to be interpreted as "A, A and B, A and B and C, A and C, B, B and C, or C." As used herein, "antagonistic," when referring to effects of combinations within a composition means that the effects of the combinations are generally less than the sum of effects of the individual components of the combination alone. These compositions may be called antagonistic combinations. As used herein, the term "aqueous" refers to a composition that contains more than a trace amount of water (i.e., more than 0.5% water by weight, based upon the total weight of the composition). As used herein, the terms "associated with," in association with" and "associated therewith," when used in reference to a relationship between a composition of the present disclosure and a plant or plant part, refer to at least a juxtaposition or close proximity of the composition and the plant or plant part. Such a juxtaposition or close proximity may be achieved by contacting or applying the composition directly to the plant or plant part and/or by applying the composition to the plant growth medium (e.g., soil) in which the plant or plant part will be grown (or is currently being grown). According to some embodiments, the composition is applied as a coating to the outer surface of the plant or plant part. According to some embodiments, the composition is applied to soil at, near or surrounding the site in which the plant or plant part will be grown (or is currently being grown). As used herein, the term "biostimulant" refers to an agent or combination of agents the application of which enhances one or more metabolic and/or physiological processes of a plant or plant part (e.g., carbohydrate biosynthesis, ion uptake, nucleic acid uptake, nutrient delivery, photosynthesis and/or respiration). As used herein, the term "binding module" refers to the region of an enzyme that mediates binding to the enzyme to a substrate. As used herein, the term "catalytic domain" refers to the region of an enzyme containing the catalytic machinery of the enzyme. As used herein, the term "cDNA" refers to a DNA molecule that can be prepared by reverse transcription from a mature, spliced, mRNA molecule obtained from a eukaryotic or prokaryotic cell. cDNAs lack intron sequences that may be present in the corresponding genomic DNA. The initial, primary RNA transcript is a precursor to mRNA that is processed through a series of steps, including splicing, before appearing as mature spliced mRNA. As used herein, the term "coding sequence" refers to a polynucleotide that directly specifies the amino acid sequence of a polypeptide. The boundaries of the coding sequence are generally determined by an open reading frame, which begins with a start codon, such as ATG, GTG, or TTG, and ends with a stop codon, such as TAA, TAG, or TGA. The coding sequence may be a genomic DNA, cDNA, synthetic DNA, or a combination thereof. As used herein, the terms "colony forming unit" and "cfu" refer to a microbial cell/spore capable of propagating on or in a suitable growth medium or substrate (e.g., a soil) when conditions (e.g., temperature, moisture, nutrient availability, pH, etc.) are favorable for germination and/or microbial growth. As used herein, the term "consists essentially of," when used in reference to compositions and methods of the present disclosure, means that the compositions/methods may contain additional components/steps so long as the additional components/steps do not materially alter the composition/method. The term "materially alter," as applied to a composition/method of the present disclosure, refers to an increase or decrease in the effectiveness of the composition/method of at least 20%. For example, a component added to a composition of the present disclosure may be deemed to "materially alter" the composition if it increases or decreases the composition's ability to inhibit the growth of a target phytopathogen by at least 20%. As used herein, the term "control sequences" refers to nucleic acid sequences involved in regulation of expression of a polynucleotide in a specific organism or in vitro. Each control sequence may be native (i.e., from the same gene) or heterologous (i.e., from a different gene) to the polynucleotide encoding the polypeptide, and native or heterologous to each other. Such control sequences include, but are not limited to leader, polyadenylation, prepropeptide, propeptide, signal peptide, promoter, terminator, enhancer, and transcription or translation initiator and terminator sequences. At a minimum, the control sequences include a promoter, and transcriptional and translational stop signals. The control sequences may be provided with linkers for the purpose of introducing specific restriction sites facilitating ligation of the control sequences with the coding region of the polynucleotide encoding a polypeptide. As used herein, the term "derived from," when used in reference to a relationship between an organism and a protein and/or polynucleotide, means that the protein and/or polynucleotide is naturally occurring in said organism. As used herein, the term "diazotroph" refers to an organism capable of converting atmospheric nitrogen (N2) into a form that may be utilized by a plant or plant part (e.g., ammonia (NH₃), ammonium (NH₄+), etc.). As used herein, the term "dispersant" refers to an agent or combination of agents the application of which reduces the cohesiveness of like particles, the surface tension of a liquid, the interfacial tension between two liquids and/or the interfacial tension between or a liquid and a solid. As used herein, the terms "effective amount," "effective concentration" and "effective amount/concentration" refer to an amount or concentration that is sufficient to cause a desired effect (e.g.¸ enhanced crop yield). The absolute value of the amount/concentration that is sufficient to cause the desired effect may be affected by factors such as the type and magnitude of effect desired, the type, size and volume of material to which the composition will be applied, the type(s) of enzymes in the composition, the amount(s) of enzyme(s) in the composition, the stability of the enzyme(s) in the composition and the storage conditions (e.g., temperature, relative humidity, duration). Those skilled in the art will understand how to select an effective amount/concentration using routine dose-response experiments. In some examples, an effective amount of a substance when used alone may be different than an effective amount of the same substance when used as part of a combination. As used herein, the term "endogenous gene" refers to a gene consisting of an endogenous polynucleotide. As used herein, the term "endogenous polynucleotide" refers to a polynucleotide that is native to the referenced host cell. As used herein, the terms "enhanc[e/ed/ing] growth" and "enhanc[e/ed/ing] plant growth" refer to an improvement in one or more characteristics of plant growth and/or development as compared to one or more control plants (e.g., a plant germinated from an untreated seed or an untreated plant). Exemplary plant growth/development characteristics include, but are not limited to, biomass, carbohydrate biosynthesis, chlorophyll content, cold tolerance, drought tolerance, height, leaf canopy, leaf length, leaf mass, leaf number, leaf surface area, leaf volume, lodging resistance, nutrient uptake and/or accumulation (e.g., ammonium, boron, calcium, copper, iron, magnesium, manganese, nitrate, nitrogen, phosphorous, potassium, sodium, sulfur and/or zinc uptake/accumulation), rate(s) of photosynthesis, root area, root diameter, root length, root mass, root nodulation (e.g., nodule mass, nodule number, nodule volume), root number, root surface area, root volume, salt tolerance, seed germination, seedling emergence, shoot diameter, shoot length, shoot mass, shoot number, shoot surface area, shoot volume, spread, stand, stomatal conductance and survival rate. Unless otherwise indicated, references to enhanced plant growth are to be interpreted as meaning that microbial strains, inoculant compositions and methods of the present disclosure enhance plant growth by enhancing nutrient availability, improving soil characteristics, etc. and are not to be interpreted as suggesting that microbial strains, inoculant compositions and methods of the present disclosure act as plant growth regulators. As used herein, the terms "enhanc[e/ed/ing] yield" and "enhanc[e/ed/ing] plant yield" refer to an improvement in one or more characteristics of plant yield as compared to one or more control plants (e.g., a control plant germinated from an untreated seed). Exemplary plant yield characteristics include, but are not limited to, biomass; bushels per acre; grain weight per plot (GWTPP); nutritional content; percentage of plants in a given area (e.g., plot) that fail to produce grain; yield at standard moisture percentage (YSMP), such as grain yield at standard moisture percentage (GYSMP); yield per plot (YPP), such as grain weight per plot (GWTPP); and yield reduction (YRED). Unless otherwise indicated, references to enhanced plant yield are to be interpreted as meaning that microbial strains, inoculant compositions and methods of the present disclosure enhance plant yield by enhancing nutrient availability, improving soil characteristics, etc. and are not to be interpreted as suggesting that microbial strains, inoculant compositions and methods of the present disclosure act as plant growth regulators. As used herein, the term "expression" refers to any step involved in the production of a polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion. Expression can be measured—for example, to detect increased expression—by techniques known in the art, such as measuring levels of mRNA and/or translated polypeptide. As used herein, the term "expression vector" refers to a linear or circular DNA construct comprising a DNA sequence encoding a polypeptide, which coding sequence is operably linked to a suitable control sequence capable of effecting expression of the DNA in a suitable host. Such control sequences may include a promoter to effect transcription, an optional operator sequence to control transcription, a sequence encoding suitable ribosome binding sites on the mRNA, enhancers and sequences which control termination of transcription and translation. As used herein, the term "extension" refers to an addition of one or more amino acids to the amino and/or carboxyl terminus of a polypeptide. As used herein, the term "foliage" refers to those portions of a plant that normally grow above the ground, including, but not limited to, leaves, stalks, stems, flowers, fruiting bodies and fruits. As used herein, the terms "foliar application" and "foliarly applied" refer to the application of one or more active ingredients to the foliage of a plant (e.g., to the leaves of the plant). Application may be affected by any suitable means, including, but not limited to, spraying/fogging the plant with a composition comprising the active ingredient(s). In some embodiments, the active ingredient(s) is/are applied to the leaves, stems and/or stalk of the plant and not to the flowers, fruiting bodies or fruits of the plant. As used herein, the term "fragment" refers to a polypeptide having one or more amino acids absent from the amino and/or carboxyl terminus of the mature polypeptide. As used herein, the term "fusion protein" refers to a polypeptide in which one polypeptide is fused at the N-terminus and/or the C-terminus of a polypeptide of the present disclosure. A fusion protein is produced by fusing a polynucleotide encoding another polypeptide to a polynucleotide of the present disclosure, or by fusing two or more polynucleotides of the present disclosure together. Techniques for producing fusion proteins are known in the art and include ligating the coding sequences encoding the polypeptides so that they are in frame and that expression of the fusion protein is under control of the same promoter(s) and terminator. Fusion proteins may also be constructed using intein technology in which fusion proteins are created post-translationally (Cooper et al., 1993, EMBO J.12: 2575–83; Dawson et al., 1994, SCIENCE 266: 776–9). A fusion protein can further comprise a cleavage site between the two polypeptides. Upon secretion of the fusion protein, the site is cleaved releasing the two polypeptides. Examples of cleavage sites include, but are not limited to, the sites disclosed in Martin et al., 2003, J. IND. MICROBIOL. BIOTECHNOL. 3: 568–76; Svetina et al., 2000, J. BIOTECHNOL. 76: 245–51; Rasmussen-Wilson et al., 1997, APPL. ENVIRON. MICROBIOL. 63: 3488–93; Ward et al., 1995, BIOTECHNOL. 13: 498–503; Contreras et al., 1991, BIOTECHNOL. 9: 378–81; Eaton et al., 1986, BIOCHEM. 25: 505–12; Collins-Racie et al., 1995, BIOTECHNOL. 13: 982–7; Carter et al., 1989, PROTEINS: STRUCTURE, FUNCTION, AND GENETICS 6: 240–8; and Stevens, 2003, DRUG DISCOVERY WORLD 4: 35–48. As used herein, the term "heterologous," when used to describe the relationship between a polynucleotide or polypeptide and a host cell, refers to a polynucleotide or polypeptide that does not naturally occur in the host cell. For the purposes of the present disclosure, extraneous copies of polynucleotides that are otherwise native to the referenced host cell are deemed heterologous polynucleotides. As used herein, the term "heterologous," when used to describe the relationship between a polynucleotide or polypeptide and a control sequence (e.g., a promoter sequence), refers to a polynucleotide or polypeptide that is not naturally associated with the control sequence (i.e., the control sequence is from a gene other than the gene encoding the mature polypeptide). As used herein, the terms "host strain" and "host cell" refer to an organism into which an expression vector, phage, virus, or other DNA construct, including a polynucleotide encoding a polypeptide of interest (e.g., an amylase) has been introduced. Exemplary host strains are microorganism cells (e.g., bacteria, filamentous fungi, and yeast) and plant cells capable of expressing a protein of interest. The term "host cell" includes protoplasts created from cells. As used herein, the terms "inoculant" and "inoculum" refer to a composition comprising microbial cells and/or spores, said cells/spores being capable of propagating/germinating on or in a suitable growth medium or substrate (e.g., a soil) when conditions (e.g., temperature, moisture, nutrient availability, pH, etc.) are favorable for germination and/or microbial growth. As used herein, the terms "insecticide" and "insecticidal" refer to an agent or combination of agents the application of which is toxic to an insect (i.e., kills an insect, inhibits the growth of an insect and/or inhibits the reproduction of an insect). As used herein, the term "introduced," when used to describe the insertion of a nucleic acid sequence into a cell, encompasses "transfection", "transformation" or "transduction," as known in the art. As used herein, the term "isolated" refers to a polypeptide, nucleic acid, cell, or other specified material or component that has been separated from at least one other material or component, including but not limited to, other proteins, nucleic acids, cells, etc. An isolated polypeptide, nucleic acid, cell or other material is thus in a form that does not occur in nature. An isolated polypeptide includes, but is not limited to, a culture broth containing the secreted polypeptide expressed in a host cell. As used herein, the term "mature polypeptide" refers to a polypeptide in its mature form following N-terminal and/or C-terminal processing (e.g., removal of signal peptide). As used herein, the term "mature polypeptide coding sequence" refers to a polynucleotide that encodes a mature polypeptide. As used herein, the term "native" refers to a polynucleotide or polypeptide naturally occurring in a host cell. As used herein, the term "naturally occurring" refers to anything (e.g., proteins, amino acids, or nucleic acid sequences) that is found in nature. Conversely, the term "non-naturally occurring" refers to anything that is not found in nature (e.g., recombinant nucleic acids and protein sequences produced in a laboratory, modification of a wild-type sequence, formulations comprising one or more synthetic components, formulations comprising an artificial combination of otherwise naturally occurring components). As used herein, the terms "nematicide" and "nematicidal" refer to an agent or combination of agents the application of which is toxic to a nematode (i.e., kills a nematode, inhibits the growth of a nematode and/or inhibits the reproduction of a nematode). As used herein, the term "non-aqueous" refers to a composition that comprises no more than a trace amount of water (i.e., no more than 0.5% water by weight, based upon the total weight of the composition). As used herein, the term "nucleic acid" encompasses DNA, RNA, heteroduplexes, and synthetic molecules capable of encoding a variant. Nucleic acids may be single-stranded or double-stranded and may be chemically modified. The terms "nucleic acid" and "polynucleotide" are used interchangeably. Because the genetic code is degenerate, more than one codon may be used to encode a particular amino acid, and the present compositions and methods encompass nucleotide sequences that encode a particular amino acid sequence. Unless otherwise indicated, nucleic acid sequences are presented in 5'-to-3' orientation. As used herein, the term "nucleic acid construct" refers to a polynucleotide, either single- or double-stranded, which is isolated from a naturally occurring gene or is modified to contain segments of nucleic acids in a manner that would not otherwise exist in nature or which is synthetic, and which comprises one or more control sequences operably linked to the nucleic acid sequence. As used herein, the term "nutrient" refers to a compound or element useful for nourishing a plant (e.g., vitamins, macrominerals, micronutrients, trace minerals, organic acids, etc. that are necessary for plant growth and/or development). As used herein, the term "obtained from," when used in reference to a relationship between an organism and a protein, means that the protein is expressed in the organism, whether from a naturally occurring polynucleotide therein or from a heterologous polynucleotide that was introduced into the organism. As used herein, the term "operably linked" means that specified components are in a relationship (including but not limited to juxtaposition) permitting them to function in an intended manner. For example, a regulatory sequence is operably linked to a coding sequence such that expression of the coding sequence is under control of the regulatory sequence. As used herein, the terms "parent" and "parent phytase" refer to a polypeptide to which an alteration is made to produce a variant polypeptide having phytase activity. As used herein, the terms "pesticide" and "pesticidal" refer to agents or combinations of agents the application of which is toxic to a pest (i.e., kills a pest, inhibits the growth of a pest and/or inhibits the reproduction of a pest). Non-limiting examples of pesticides include acaricides, fungicides, herbicides, insecticides, and nematicides, etc. As used herein, the term "phosphate-solubilizing microorganism" refers to a microorganism capable of converting insoluble phosphate into a soluble form of phosphate that may be utilized by a plant or plant part (e.g., hydrogen phosphate (HPO4^-2), dihydrogen phosphate (H2PO4-), etc.). As used herein, the term "phytase activity" refers to hydrolysis of a phytate (inositol mono-, di-, tri-, tetra-, penta- and/or hexa-phosphate) to release inorganic phosphate. Phytase activity may be determined by the liberation of inorganic phosphate from Na-phytate solution, wherein one phytase activity unit is the amount of enzyme which liberates 1 µmol inorganic phosphate per min from a 0.0051 M Na-phytate solution in 0.25 M Na-acetate, pH 5.5 and at 37 °C (Engelen, et al., Simple and rapid determination of phytase activity, J. AOAC INT.77:760–4 (1994)). Examples of activity unit names are: FYT, FTU and U. Phytase activity may be determined using the assay as described in Example 2 ("Determination of Phytase Activity"). As used herein, the terms "phytate" and "phytic acid" refer collectively to myo-inositol hexaphosphate (also known as myo-inositol hexakisphosphate, IP6) and to the inositol phosphate products produced by the stepwise hydrolysis thereof (i.e., inositol pentaphosphate (IP5), inositol tetraphosphate (IP4), inositol triphosphate (IP3), inositol diphosphate (IP2), inositol monophosphate (IP1)). As used herein, the term "phytopathogenic pest" includes any organism or virus that negatively affects a plant, including, but not limited to, organisms and viruses that spread disease, damage host plants and/or compete for soil nutrients. The term "phytopathogenic pest" encompasses organisms and viruses that are known to associate with plants and to cause a detrimental effect on the plant's health and/or vigor. Phytopathogenic pests include, but are not limited to, arachnids (e.g., mites, ticks, spiders, etc.), bacteria, fungi, gastropods (e.g., slugs, snails, etc.), invasive plants (e.g., weeds), insects (e.g., white flies, thrips, weevils, etc.), nematodes (e.g., root-knot nematode, soybean cyst nematode, etc.), rodents and viruses (e.g., tobacco mosaic virus (TMV), tomato spotted wilt virus (TSWV), cauliflower mosaic virus (CaMV), etc.). As used herein, the term "plant" includes all plant populations, including, but not limited to, agricultural, floricultural, horticultural and silvicultural plants. The term "plant" encompasses plants obtained by conventional plant breeding and optimization methods (e.g., marker-assisted selection) and plants obtained by genetic engineering, including cultivars protectable and not protectable by plant breeders' rights. As used herein, the term "plant-beneficial" refers to a composition, method or use having at least one property/effect that is advantageous with respect to the cultivation of a plant in any field of agronomy, including, but not limited to, agriculture, floriculture, horticulture and silviculture. As used herein, the term "plant cell" refers to a cell of an intact plant, a cell taken from a plant, or a cell derived from a cell taken from a plant. Thus, the term "plant cell" includes cells within seeds, suspension cultures, embryos, meristematic regions, callus tissue, leaves, shoots, gametophytes, sporophytes, pollen and microspores. As used herein, the term "plant growth regulator" refers to an agent or combination of agents the application of which accelerates or retards the growth/maturation rate of a plant through direct physiological action on the plant or which otherwise alters the behavior of a plant through direct physiological action on the plant. "Plant growth regulator" shall not be interpreted to include any agent or combination of agents excluded from the definition of "plant regulator" that is set forth section 2(v) of the Federal Insecticide, Fungicide, and Rodenticide Act (7 U.S.C. § 136(v)). Thus, "plant growth regulator" does not encompass microorganisms applied to a plant, plant part or plant growth medium for the purpose of enhancing the availability and/or uptake of nutrients, nutrients necessary to normal plant growth, soil amendments applied for the purpose of improving soil characteristics favorable for plant growth or vitamin hormone products as defined by 40 C.F.R. § 152.6(f). As used herein, the term "plant part" refers to any part of a plant, including cells and tissues derived from plants. Thus, the term "plant part" may refer to any of plant components or organs (e.g., leaves, stems, roots, etc.), plant tissues, plant cells and seeds. Examples of plant parts, include, but are not limited to, anthers, embryos, flowers, fruits, fruiting bodies, leaves, ovules, pollen, rhizomes, roots, seeds, shoots, stems and tubers, as well as scions, rootstocks, protoplasts, calli and the like. As used herein, the term "plant propagation material" refers to a plant part from which a whole plant can be generated. Examples of plant propagation materials include, but are not limited to, cuttings (e.g., leaves, stems), rhizomes, seeds, tubers and cells/tissues that can be cultured into a whole plant. As used herein, the term "polynucleotide" encompasses DNA, RNA, heteroduplexes, and synthetic molecules capable of encoding a polypeptide. Polynucleotides may be single-stranded or double-stranded and may comprise chemical modifications. The terms "nucleic acid" and "polynucleotide" are used interchangeably. Because the genetic code is degenerate, more than one codon may be used to encode a particular amino acid, and the present compositions and methods encompass nucleotide sequences that encode a particular amino acid sequence. Unless otherwise indicated, nucleic acid sequences are presented in 5'-to-3' orientation. As used herein, the term "protein" is not meant to refer to a specific amino acid chain length and encompasses peptides, oligopeptides and polypeptides. It is to be understood that the term "protein" also encompasses two or more polypeptides combined to form an encoded product, as well as hybrid polypeptides and fusion proteins. As used herein, the term "purified" refers to a polynucleotide, protein or cell that is substantially free from other components as determined by analytical techniques well known in the art (e.g., a purified polynucleotide or protein may form a discrete band in an electrophoretic gel, chromatographic eluate, and/or a media subjected to density gradient centrifugation). A purified polynucleotide or protein is at least about 50% pure, usually at least about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, about 99.5%, about 99.6%, about 99.7%, about 99.8% or more pure (e.g., percent by weight or on a molar basis). In a related sense, a composition is enriched for a molecule when there is a substantial increase in the concentration of the molecule after application of a purification or enrichment technique. The term "enriched" refers to a compound, polynucleotide, protein, cell, nucleic acid, amino acid, or other specified material or component that is present in a composition at a relative or absolute concentration that is higher than a starting composition. ln one aspect, the term "purified" as used herein refers to the protein or cell being essentially free from components (especially insoluble components) from the production organism. In other aspects. the term "purified" refers to the protein being essentially free of insoluble components (especially insoluble components) from the native organism from which it is obtained. In one aspect, the protein is separated from some of the soluble components of the organism and culture medium from which it is recovered. The protein may be purified (i.e., separated) by one or more of the unit operations filtration, precipitation, or chromatography. Accordingly, the protein may be purified such that only minor amounts of other proteins, in particular, other proteins, are present. The term "purified" as used herein may refer to removal of other components, particularly other proteins and most particularly other enzymes present in the cell of origin of the protein. The protein may be "substantially pure", i.e., free from other components from the organism in which it is produced, e.g., a host organism for recombinantly produced protein. In one aspect, the protein is at least 40% pure by weight of the total protein material present in the preparation. In one aspect, the protein is at least 50%, 60%, 70%, 80% or 90% pure by weight of the total protein material present in the preparation. As used herein. a "substantially pure protein" may denote a protein preparation that contains at most 10%, preferably at most 8%, more preferably at most 6%, more preferably at most 5%, more preferably at most 4%, more preferably at most 3%, even more preferably at most 2%, most preferably at most 1%, and even most preferably at most 0.5% by weight of other protein material with which the protein is natively or recombinantly associated. It is, therefore, preferred that the substantially pure protein is at least 92% pure, preferably at least 94% pure, more preferably at least 95% pure, more preferably at least 96% pure, more preferably at least 97% pure, more preferably at least 98% pure, even more preferably at least 99% pure, most preferably at least 99.5% pure by weight of the total protein material present in the preparation. Proteins of the present disclosure are preferably in a substantially pure form (i.e., the preparations are essentially free of other protein material). This can be accomplished, for example by preparing the protein by well- known recombinant methods or by classical purification methods. As used herein, the term "recombinant" is used in its conventional meaning to refer to the manipulation, e.g., cutting and rejoining, of nucleic acid sequences to form constellations different from those found in nature. The term recombinant refers to a cell, nucleic acid, protein or vector that has been modified from its native state. Thus, for example, recombinant cells express genes that are not found within the native (non-recombinant) form of the cell, or express native genes at different levels or under different conditions than found in nature. The term "recombinant" is synonymous with "genetically modified" and "transgenic". As used herein, the terms "recover" and "recovery" refer to the removal of a protein from at least one fermentation broth component selected from the list of a cell, a nucleic acid, or other specified material, e.g., recovery of the protein from the whole fermentation broth, or from the cell-free fermentation broth, by protein crystal harvest, by filtration, e.g. depth filtration (by use of filter aids or packed filter medias, cloth filtration in chamber filters, rotary-drum filtration, drum filtration, rotary vacuum-drum filters, candle filters, horizontal leaf filters or similar, using sheed or pad filtration in framed or modular setups) or membrane filtration (using sheet filtration, module filtration, candle filtration, microfiltration, ultrafiltration in either cross flow, dynamic cross flow or dead end operation), or by centrifugation (using decanter centrifuges, disc stack centrifuges, hyrdo cyclones or similar), or by precipitating the protein and using relevant solid-liquid separation methods to harvest the protein from the broth media by use of classification separation by particle sizes. Recovery encompasses isolation and/or purification of the protein. As used herein, the term "sequence difference" refers to the percent of amino acid differences between a polypeptide and a reference polypeptide and is calculated as follows: (Different Residues x 100)/(Length of Reference Polypeptide) wherein he different residues comprise any substitution, deletion or insertion (e.g., an extension at the N-terminus and/or C-terminus) in the sequence. As used herein, the term "sequence identity" refers to the relatedness between two amino acid sequences or between two nucleotide sequences. For purposes of the present disclosure, the sequence identity between two amino acid sequences is determined as the output of "longest identity" using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol.48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet.16: 276-277), preferably version 6.6.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. In order for the Needle program to report the longest identity, the -nobrief option must be specified in the command line. The output of Needle labeled "longest identity" is calculated as follows: (Identical Residues x 100)/(Length of Alignment – Total Number of Gaps in Alignment). For purposes of the present disclosure, the sequence identity between two polynucleotide sequences is determined as the output of "longest identity" using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably version 6.6.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. In order for the Needle program to report the longest identity, the nobrief option must be specified in the command line. The output of Needle labeled "longest identity" is calculated as follows: (Identical Deoxyribonucleotides x 100)/(Length of Alignment – Total Number of Gaps in Alignment). As used herein, the term "signal peptide" refers to a sequence of amino acids attached to the N-terminal portion of a protein, which facilitates the secretion of the protein outside the cell. The mature form of an extracellular protein lacks the signal peptide, which is cleaved off during the secretion process. As used herein, the term "stabilizing agent" refers to an agent or combination of agents the application of which enhances the stability of an enzyme. As used herein, the term "structural similarity" refers to the relatedness between the three-dimensional structures of two polypeptides. A three-dimensional structure of any polypeptide may be obtained experimentally via, e.g., X-ray crystallography or calculated using in silico methods such as AlphaFold2 (vide supra). The structural similarity between three-dimensional structures may then be determined by the TM-score, which is calculated using the following general formula (Zhang & Skolnick, 2004, Proteins 57:702–710): T_M-score where LN is the length of the native structure, LT is the length of the aligned residues to the template structure, di is the distance between pair i of aligned residues and d₀ is a scale to normalize the match difference. ‘Max’ denotes the maximum value after optimal spatial superposition. For the purposes of the present disclosure, LN is the length of the reference polypeptide: T_{M score} A structural alignment of the three-dimensional structures of two polypeptides is necessary before the TM-score can be calculated. This is achieved via algorithms that optimize the structural overlap, and several methods are available, such as CEalign (Shindyalov and Bourne, 1998, Protein Eng., 11:739-747), DALI (Holm and Sander, 1995, Trends Biochem. Sci., 20:478-480), or TM-align (Zhang and Skolnick, 2005, Nucleic Acids Res.33(7):2302-2309). For the purposes of the present disclosure, TM-align is applied. For convenience, TM-score is integrated in the TM-align software, which is available from the author’s website (zhanggroup.org/TM-score/). The version of TM-align is preferably updated 2019-08-22 or later, and the TM-score between a reference and a query protein is determined by running this command: TMalign <query.pdb> <reference.pdb> -L <length of reference> where <query.pdb> is the name of the PDB file containing coordinates of the query polypeptide, <reference.pdb> is the name of the PDB file containing coordinates of the reference polypeptide. The TM-score is calculated and reported in the output, along with several other parameters from the alignment. The maximal TM-score is 1, e.g., 1.0, corresponding to identical three-dimensional structures. As used herein, the term "subsequence" refers to a polynucleotide having one or more nucleotides absent from the 5' and/or 3' end of a mature protein coding sequence. As used herein, the term "variant" refers to a protein comprising a man-made mutation, i.e., a substitution, insertion (including extension), and/or deletion (e.g., truncation), at one or more positions. A substitution means replacement of the amino acid occupying a position with a different amino acid; a deletion means removal of the amino acid occupying a position; and an insertion means adding 1-5 amino acids (e.g., 1-3 amino acids, in particular, 1 amino acid) adjacent to and immediately following the amino acid occupying a position. For purposes of the present disclosure, the polypeptides disclosed herein as SEQ ID NO: 1, SEQ ID NO: 2 and SEQ ID NO: 3 are used to identify corresponding amino acid positions in other polypeptides having phytase activity. The amino acid sequence of another polypeptide is aligned with the polypeptide disclosed in SEQ ID NO: 1 or SEQ ID NO: 2 or SEQ ID NO: 3, and based on the alignment, the amino acid position number corresponding to any amino acid residue in the polypeptide disclosed in SEQ ID NO: 1 or SEQ ID NO: 2 or SEQ ID NO: 3 is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol.48: 443–53) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet.16: 276–7), preferably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. In describing polypeptides of the present invention, the nomenclature described below is adapted for ease of reference. The accepted IUPAC single letter or three letter amino acid abbreviation is employed. For an amino acid substitution, the following nomenclature is used: Original amino acid, position, substituted amino acid. Accordingly, the substitution of threonine at position 226 with alanine is designated as “T226A”. Multiple mutations are separated by addition marks (“+”) or by commas, e.g., “G205R, S411F” or “G205R + S411F”, representing substitutions at positions 205 and 411 of glycine (G) with arginine (R) and serine (S) with phenylalanine (F), respectively. Because the amino acid residue at a given position varies from parent to parent, the amino acid to be substituted may be indicated with X, e.g., X226A. For an amino acid deletion, the following nomenclature is used: Original amino acid, position, *. Accordingly, the deletion of the amino acid at position 195 is designated as “X195*”. Multiple deletions are separated by addition marks (“+”) or by commas, e.g., “X195* + X411*” or “X195*, X411*”. For an amino acid insertion, the following nomenclature is used: Original amino acid, position, original amino acid, inserted amino acid. Accordingly, the insertion of lysine after the amino acid at position 195 is designated “X195XK”. An insertion of multiple amino acids is designated [Original amino acid, position, original amino acid, inserted amino acid #1, inserted amino acid #2; etc.]. For example, the insertion of lysine and alanine after the amino acid at position 195 is indicated as “X195XKA”. In such cases, the inserted amino acid residue(s) are numbered by the addition of lower case letters to the position number of the amino acid residue preceding the inserted amino acid residue(s). In the above example, the sequence would thus be: Alternatively, an insertion of an amino acid residue such as lysine after the amino acid at position 195 may be indicated by “195aK”, and the insertion of two or more additional amino acid residues such as lysine and alanine after the amino acid at position 195 may be indicated by “195aK, 195bA”. As used herein, the term "wild-type" in reference to an amino acid sequence or nucleic acid sequence means that the amino acid sequence or nucleic acid sequence is a native or naturally occurring sequence. While certain aspects of the present disclosure will hereinafter be described with reference to embodiments thereof, it will be understood by those of ordinary skill in the art that various changes in form and details may be made therein without departing from the spirit and scope of the present disclosure as defined by the claims. All publications, patent applications, patents and other references mentioned herein are incorporated by reference in their entirety, except insofar as they contradict any disclosure expressly set forth herein. The present disclosure provides proteins useful for a) enhancing plant growth environments; b) catalyzing hydrolysis of phytic acids in plant growth media and fertilizers; c) removing phosphate from myo-inositol hexakisphosphates in plant growth media and fertilizers; d) removing phosphate from myo-inositol pentakisphosphates in plant growth media and fertilizers; e) removing phosphate from myo-inositol tetrakisphosphates in plant growth media and fertilizers; f) removing phosphate from myo-inositol trisphosphates in plant growth media and fertilizers; g) removing phosphate from myo-inositol diphosphates in plant growth media and fertilizers; h) removing phosphate from myo-inositol monophosphates in plant growth media and fertilizers; i) producing/releasing soluble forms of phosphorous in plant growth media and fertilizers; j) producing/releasing soluble forms of minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in plant growth media and fertilizers; k) increasing nutrient availability in plant growth media and fertilizers (e.g., phosphorous, calcium, iron, magnesium, manganese, potassium, zinc availability); l) improving nutrient stability in plant growth media and fertilizers (e.g., stabilizing levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in plant growth media and fertilizers); m) increasing nutrient uptake in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; n) increasing nutrient accumulation in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; o) increasing nutrient utilization in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; p) enhancing plant growth; q) enhancing plant yield; r) reducing the amount(s) of exogenous fertilizer needed to achieve a desired result (e.g., the amount of exogenous phosphorous required to produce X bushels of corn); s) reducing nutrient washout/runoff from plant growth media (e.g., phosphorous washout/runoff from field soil); t) enhancing soil microbiomes; u) stimulating growth and/or proliferation of plant-beneficial microorganisms in plant growth media (e.g., growth and/or proliferation of plant-beneficial diazotrophs, phosphate-solubilizers and/or mycorrhizae); v) enhancing plant root nodulation; w) enhancing plant root mycorrhization; x) enhancing the abilities of plants and plant parts to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; y) reducing disease severity in plants and plant parts affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; z) reducing phytopathogen loads in plant growth media; aa) reducing detrimental effects of pesticide-induced phytotoxicity; bb) enhancing the abilities of plant and plant parts to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; cc) reducing disease severity in plants and plant parts affected by abiotic stresses, such as drought, salinity and extreme temperatures; dd) degrading organic materials in plant growth media and fertilizers; and/or ee) enhancing turnover of organic materials in plant growth media and fertilizers, as well as polynucleotides encoding such proteins, organisms expressing such proteins, formulations comprising such proteins, polynucleotides and organisms, and methods of using such proteins, polynucleotides, organisms and formulations in agriculture and other fields of endeavor. As those skilled in the art will appreciate, proteins, polynucleotides and organisms of the present disclosure may be used (and may be formulated for use) at any time(s) throughout agricultural, floricultural, horticultural, and silvicultural processes, such as prior to planting, at the time of planting, after planting, prior to germination, after germination, prior to seedling emergence, at the time of seedling emergence, after seedling emergence, prior to the vegetative stage, during the vegetative stage, after the vegetative stage, prior to the reproductive stage, during the reproductive stage, after the reproductive stage, prior to flowering, at the time of flowering, after flowering, prior to fruiting, at the time of fruiting, after fruiting, prior to ripening, at the time of ripening, after ripening, and/or prior to harvest. Accordingly, compositions of the present disclosure may be formulated for any suitable method of application, including, but not limited to, on-seed application and in-furrow application. In some embodiments, compositions of the present disclosure are formulated as fertilizers or fertilizer additives. Those skilled in the art will further appreciate that proteins, polynucleotides, organisms and formulations of the present disclosure may be used in combination to achieve the desire outcome(s). The present disclosure thus extends to formulations comprising two or more proteins of the present disclosure, to hybrid proteins comprising two or more distinct catalytic domains, to fusion proteins comprising two or more enzymatic polypeptides, etc. Although certain combinations will be described in detail below, it is to be understood that the present disclosure is not limited to those combinations but extends to all possible combinations of proteins, polynucleotides, organisms and formulations described herein. The present disclosure encompasses proteins exhibiting one or more phytase activities belonging to EC 3.1.3 (e.g., EC 3.1.3.8, EC 3.1.3.26, EC 3.1.3.72) and having: a) a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of any one or more of SEQ ID NOs: 1–3 and 7–480, wherein the three-dimensional structure is determined using AlphaFold; and/or b) at least 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to any one or more of SEQ ID NOs: 1–3 and 7–480; and/or c) at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to any one or more of SEQ ID NOs: 1–3 and 7–480, as well as polynucleotides encoding such proteins, organisms expressing such proteins, formulations comprising such proteins, polynucleotides and organisms, and methods of using such proteins, polynucleotides, organisms and formulations in agriculture and other fields of endeavor. In preferred embodiments, proteins of the present disclosure exhibit phytase activity belonging to EC 3.1.3.26 and are selected from the group consisting of: a) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 1, wherein the three-dimensional structure is determined using AlphaFold; b) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 2, wherein the three-dimensional structure is determined using AlphaFold; c) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 3, wherein the three-dimensional structure is determined using AlphaFold; d) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 1; e) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 2; f) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 3; g) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 1; h) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 2; i) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 3; j) polypeptides derived from any one of SEQ ID NO(s): 1–3 and 7–480 by substitution, deletion, or insertion of one or more amino acids; k) polypeptides derived from the polypeptide of any one of a) through j) wherein the N- and/or C-terminal end has been extended by the addition of one or more amino acids; and l) fragments of the polypeptides of any one of a) through k). In some embodiments, proteins of the present disclosure are wild-type polypeptides. In some embodiments, proteins of the present disclosure are fragments/mutants/variants of wild-type polypeptides. In some embodiments, proteins of the present disclosure exhibit phytase activity belonging to 3.1.3.26 and comprise, consist essentially of or consist of the amino acid sequence of any one of SEQ ID NO(s): 1–3, 7–19, 21–35, 37– 46, 48–50, 52–107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162–177, 179–253, 255–261, 263–271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416–480 or an enzymatically active fragment thereof, said fragment optionally comprising at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 82, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.5, 99 or 99.5% of the amino acids found in the original protein. In some embodiments, proteins of the present disclosure are variants of SEQ ID NO: 1 having a) a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 1, wherein the three-dimensional structure is determined using AlphaFold; and/or b) at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 1; and/or c) at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4. 85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 1, optionally comprising one or more of the following: 16S, 82T, 97Y, 170W, 172K, 235T, 311A, 337V, using SEQ ID NO: 1 for numbering. In some embodiments, the phytase variant comprises 16S, 82T, 97Y, 170W, 172K, 235T, 311A and 337V. In some embodiments, proteins of the present disclosure are variants of SEQ ID NO: 2 having a) a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 2, wherein the three-dimensional structure is determined using AlphaFold; and/or b) at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 2; and/or c) at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4. 85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 2, optionally comprising one or more of the following: 31C, 52C, 99C, 141C, 177C, 199C, using SEQ ID NO: 2 for numbering. In some embodiments, the phytase variant comprises 31C, 52C, 99C, 141C, 177C and 199C, resulting in the formation of disulfide bridges between positions 52 and 99, 31 and 177, and 141 and 199. See WO 2022/034211. In some embodiments, the phytase variant further comprises a substitution at one or more of positions 57, 73, 121, 134, 155, 203, 207, and 273—for example, 57Y, 73P, 121P, 134Q, 155F, 203L, 207T, 273L— using SEQ ID NO: 2 for numbering. See WO 2022/034211. In some embodiments, proteins of the present disclosure are variants of SEQ ID NO: 3 having a) a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 3, wherein the three-dimensional structure is determined using AlphaFold; and/or b) at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 3; and/or c) at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4. 85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 3. In some embodiments, proteins of the present disclosure are variants of one of SEQ ID NOs: 7–480 having about/at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to said parent. In some embodiments, proteins of the present disclosure comprise, consist essentially of or consist of one of SEQ ID NO(s): 1–3, 7–19, 21–35, 37–46, 48–50, 52–107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162–177, 179–253, 255–261, 263–271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416–480 or an enzymatically active fragment thereof with an N-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), a C-terminal extension of one or more amino acids (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more amino acids), one or more substitutions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more substitutions), one or more insertions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more insertions), and/or one or more deletions (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more deletions). The amino acid changes may be of a minor nature, that is conservative amino acid substitutions or insertions that do not significantly affect the folding and/or activity of the protein; small deletions, typically of 1-30 amino acids; small amino- or carboxyl-terminal extensions, such as an amino-terminal methionine residue; a small linker peptide of up to 20-25 residues; or a small extension that facilitates purification by changing net charge or another function, such as a poly-histidine tract, an antigenic epitope or a binding module. Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site- directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the resultant molecules are evaluated for catalytic activity to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem.271: 4699-4708. The active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labeling, in conjunction with mutation of putative contact site amino acids. See, for example, de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol.224: 899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identity of essential amino acids can also be inferred from an alignment with a related polypeptide, and/or be inferred from sequence homology and conserved catalytic machinery with a related polypeptide or within a polypeptide or protein family with polypeptides/proteins descending from a common ancestor, typically having similar three-dimensional structures, functions, and significant sequence similarity. Additionally, or alternatively, protein structure prediction tools can be used for protein structure modelling to identify essential amino acids and/or active sites of polypeptides. See, for example, Jumper et al., 2021, "Highly accurate protein structure prediction with AlphaFold", Nature 596: 583-589. Single or multiple amino acid substitutions, deletions, and/or insertions can be made and tested using known methods of mutagenesis, recombination, and/or shuffling, followed by a relevant screening procedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95/17413; or WO 95/22625. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991, Biochemistry 30: 10832-10837; US 5,223,409; WO 92/06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner et al., 1988, DNA 7: 127). Mutagenesis/shuffling methods can be combined with high-throughput, automated screening methods to detect activity of cloned, mutagenized polypeptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17: 893-896). Mutagenized DNA molecules that encode active polypeptides can be recovered from the host cells and rapidly sequenced using standard methods in the art. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide. In some embodiments, proteins of the present disclosure comprise, consist essentially of or consist of a catalytic domain, a binding module and a linker between said catalytic domain and said binder module. The present disclosure extends to proteins capable of exhibiting two, three, four, five or more distinct catalytic activities, including, but not limited to, proteins that inherently exhibit two or more distinct catalytic activities and fusion proteins comprising two or more polypeptides that exhibit distinct catalytic activities. In some embodiments, proteins of the present disclosure are hybrid proteins. In some embodiments, proteins of the present disclosure comprise two or more catalytic domains. In some embodiments, proteins of the present disclosure comprise two or more binding modules. In some embodiments, proteins of the present disclosure are fusion proteins comprising a first polypeptide having a first enzymatic activity and a second polypeptide having a second enzymatic activity. For example, in some embodiments, the protein is a fusion protein comprising a first polypeptide and a second polypeptide, said second polypeptide being distinct from said first polypeptide, wherein said first polypeptide exhibits phytase activity and is selected from the group consisting of: a) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 1, wherein the three-dimensional structure is determined using AlphaFold; b) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 2, wherein the three-dimensional structure is determined using AlphaFold; c) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 3, wherein the three-dimensional structure is determined using AlphaFold; d) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 1; e) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 2; f) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 3; g) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 1; h) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 2; i) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 3; j) polypeptides derived from any one of SEQ ID NO(s): 1–3 and 7–480 by substitution, deletion, or insertion of one or more amino acids; k) polypeptides derived from the polypeptide of any one of a) through j) wherein the N- and/or C-terminal end has been extended by the addition of one or more amino acids; and l) fragments of the polypeptides of any one of a) through k), and, optionally, wherein said second polypeptide exhibits phytase activity and is selected from the group consisting of: m) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 1, wherein the three-dimensional structure is determined using AlphaFold; n) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 2, wherein the three-dimensional structure is determined using AlphaFold; o) polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 3, wherein the three-dimensional structure is determined using AlphaFold; p) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 1; q) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 2; r) polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 3; s) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 1; t) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 2; u) polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 3; v) polypeptides derived from any one of SEQ ID NO(s): 1–3 and 7–480 by substitution, deletion, or insertion of one or more amino acids; w) polypeptides derived from the polypeptide of any one of m) through v) wherein the N- and/or C-terminal end has been extended by the addition of one or more amino acids; and x) fragments of the polypeptides of any one of m) through w). In some embodiments, proteins of the present disclosure are encoded by a polynucleotide having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to one or more of SEQ ID NO(s): 4–6 or the cDNA thereof. In preferred embodiments, proteins of the present disclosure are encoded by a polynucleotide that comprises, consists essentially of or consists of one of SEQ ID NO(s): 4–6 or the cDNA thereof. Proteins of the present disclosure may be derived from microorganisms of any genus. In some embodiments, the protein is derived from and/or obtained from a Gram-negative bacterium, such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Citrobacter (e.g., C. amalonaticus, C. braakii, C. freundii, C. gillenii, C. werkmanii), Cronobacter (e.g., C. sakazakii, C. turicensis), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Kosakonia (e.g., K. sacchari), Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella or Ureaplasma. In some embodiments, the protein is derived from a Gram-positive bacterium, such as Alkalihalobacillus (e.g., A. akibai, A. clausii), Bacillus (e.g., B. agaradhaerens, B. alkalophilus, B. amyloliquefaciens, B. brevis, B. circulans, B. clausii, B. coagulans, B. deramificans, B. firmus, B. lautus, B. lentus, B. licheniformis, B. megaterium, B. pumilus, B. stearothermophilus, B. subtilis, B. thuringiensis), Clostridium, Effusibacillus (e.g., E. pohliae), Enterococcus, Geobacillus (e.g., G. stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., L. lenta), Neobacillus (e.g., N. novalis), Nocardiopsis, Oceanobacillus (e.g., O. barbara), Staphylococcus, Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, and S. equi subsp. Zooepidemicus) or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sutcliffiella (e.g., S. halmapala). In some embodiments, the protein is derived from a fungus, such as Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. caregiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis subrufa, C. subvermispora), Chaetomium (e.g., C. erraticum, C. globosum), Chrysosporium (e.g., C. inops, C. keratinophilum, C. lucknowense, C. merdarium, C. pannicola, C. queenslandicum, C. tropicum, C. zonatum), Colletotrichum (e.g., C. graminicola), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (e.g., C. hirsutus), Cryphonectria (e.g., C. parasitica), Cryptococcus, Evansstolkia (e.g., E. leycettana), Filibasidium, Fusarium (e.g., F. bactridioides, F. cerealis, F. crookwellense, F. culmorum, F. graminearum, F. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum), Peniophora (e.g., P. lycii), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Podospora (e.g., P. anserina), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. versicolor), Trichoderma (e.g., T. atroviride, T. harzianum, T. koningii, T. longibrachiatum, T. reesei, T. viride), Trichophaea (e.g., T. saccata), or Urnula (e.g., U. criterium). In some embodiments, the protein is derived from a yeast, such as Candida, Hansenula, Komagataella (e.g., K. phaffii), Kluyveromyces (e.g., Kluyveromyces lactis), Pichia (e.g., P. pastoris), Saccharomyces (e.g., S. carlsbergensis, S. cerevisiae, S. diastaticus, S. douglasii, S. kluyveri, S. norbensis, S. oviformis), Schizosaccharomyces, or Yarrowia (e.g., Yarrowia lipolytica). In some preferred embodiments, proteins of the present disclosure are derived from Citrobacter, Escherichia, Kosakonia, Peniophora or Podospora. For example, in some embodiments, the protein is a native Citrobacter, Escherichia, Kosakonia, Peniophora or Podospora acid phytase or is a fragment/mutant/variant of a native Citrobacter, Escherichia, Kosakonia, Peniophora or Podospora acid phytase. It will be understood that for the aforementioned species, the disclosure encompasses both the perfect and imperfect states, and other taxonomic equivalents, e.g., anamorphs, regardless of the species name by which they are known. Those skilled in the art will readily recognize the identity of appropriate equivalents. The proteins may be identified and derived from other sources including microorganisms isolated from nature (e.g., soil, composts, water, etc.) or DNA samples obtained directly from natural materials (e.g., soil, composts, water, etc.) using the above-mentioned probes. Techniques for isolating microorganisms and DNA directly from natural habitats are well known in the art. A polynucleotide encoding the protein may then be obtained by similarly screening a genomic DNA or cDNA library of another microorganism or mixed DNA sample. Once a polynucleotide encoding a protein has been detected with the probe(s), the polynucleotide can be isolated or cloned by utilizing techniques that are known to those of ordinary skill in the art (see, e.g., Davis et al., 2012, Basic Methods in Molecular Biology, Elsevier). Proteins of the present disclosure may likewise be derived from plants of any genus. In some embodiments, the protein is derived from a plant selected from the families Amaranthaceae (e.g., chard, spinach, sugar beet, quinoa), Asteraceae (e.g., artichoke, asters, chamomile, chicory, chrysanthemums, dahlias, daisies, echinacea, goldenrod, guayule, lettuce, marigolds, safflower, sunflowers, zinnias), Brassicaceae (e.g., arugula, broccoli, bok choy, Brussels sprouts, cabbage, cauliflower, canola, collard greens, daikon, garden cress, horseradish, kale, mustard, radish, rapeseed, rutabaga, turnip, wasabi, watercress, Arabidopsis thaliana), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, pumpkin, squash (e.g., acorn squash, butternut squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentils, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch), Malvaceae (e.g., cacao, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, lawn grass (e.g., Bahia grass, Bermudagrass, bluegrass, Buffalograss, Centipede grass, Fescue, or Zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugar cane, triticale, wheat and other cereal crops, Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almonds, apples, apricots, blackberry, blueberry, cherries, peaches, plums, quinces, raspberries, roses, strawberries), Rutaceae (e.g., curry, grapefruit, lemon, lime, kumquat, mandarin, orange), Solanaceae (e.g., bell peppers, chili peppers, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape). Those skilled in the art will understand how to identify, isolate, characterize, produce and recover proteins having phytase activities belonging to EC 3.1.3. See, e.g., CN 102311964, CN 110484521, CN 110724676, CN 115725649, DE 102020131856, EP 1092764, EP 3257381, EP 969089, RU 2706086, US 2005/0108791, US 2009/0158452, WO 2003/066847, WO 2006/037327, WO 2006/037328, WO 2006/038062, WO 2006/038128, WO 2006/063588, WO 2007/112739, WO 2009/074650, WO 2011/117396, WO 2012/110776, WO 2015/197871, WO 2017/001701, WO 2020/131691, WO 2021/102238, WO 2021/133658, WO 2021/173974, WO 2022/034211, WO 2024/056643, WO 2024/121327, WO 98/28409. Proteins of the present disclosure may be produced/obtained using any suitable method(s), including, but not limited to, shake flask cultivation and large-scale fermentation (including continuous, batch, fed-batch, solid-state and/or microcarrier-based fermentation) methods. The present disclosure extends to methods of producing a protein of the present disclosure, comprising (a) cultivating a cell, which in its wild-type form produces the protein, under conditions conducive for production of the protein; and optionally, (b) recovering the protein. The present disclosure also extends to methods of producing a protein of the present disclosure, comprising (a) cultivating a recombinant host cell of the present disclosure under conditions conducive for production of the protein; and optionally, (b) recovering the protein. In some embodiments, the protein is produced by and obtained from a Gram-negative bacterium, such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Citrobacter (e.g., C. amalonaticus, C. braakii, C. freundii, C. gillenii, C. werkmanii), Cronobacter (e.g., C. sakazakii, C. turicensis), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Kosakonia (e.g., K. sacchari), Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella or Ureaplasma. In some embodiments, the protein is produced by and obtained from a Gram-positive bacterium, such as Alkalihalobacillus (e.g., A. akibai, A. clausii), Bacillus (e.g., B. agaradhaerens, B. alkalophilus, B. amyloliquefaciens, B. brevis, B. circulans, B. clausii, B. coagulans, B. deramificans, B. firmus, B. lautus, B. lentus, B. licheniformis, B. megaterium, B. pumilus, B. stearothermophilus, B. subtilis, B. thuringiensis), Clostridium, Effusibacillus (e.g., E. pohliae), Enterococcus, Geobacillus (e.g., G. stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., L. lenta), Neobacillus (e.g., N. novalis), Nocardiopsis, Oceanobacillus (e.g., O. barbara), Staphylococcus, Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, and S. equi subsp. Zooepidemicus) or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sutcliffiella (e.g., S. halmapala). In some embodiments, the protein is produced by and obtained from a fungal cell, such as Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. caregiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis subrufa, C. subvermispora), Chaetomium (e.g., C. erraticum, C. globosum), Chrysosporium (e.g., C. inops, C. keratinophilum, C. lucknowense, C. merdarium, C. pannicola, C. queenslandicum, C. tropicum, C. zonatum), Colletotrichum (e.g., C. graminicola), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (e.g., C. hirsutus), Cryphonectria (e.g., C. parasitica), Cryptococcus, Evansstolkia (e.g., E. leycettana), Filibasidium, Fusarium (e.g., F. bactridioides, F. cerealis, F. crookwellense, F. culmorum, F. graminearum, F. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum Peniophora (e.g., P. lycii), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Podospora (e.g., P. anserina), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. versicolor), Trichoderma (e.g., T. atroviride, T. harzianum, T. koningii, T. longibrachiatum, T. reesei, T. viride), Trichophaea (e.g., T. saccata), or Urnula (e.g., U. criterium). In some embodiments, the protein is produced by and obtained from a yeast cell, such as Candida, Hansenula, Komagataella (e.g., K. phaffii), Kluyveromyces (e.g., K. lactis), Pichia (e.g., P. pastoris), Saccharomyces (e.g., S. carlsbergensis, S. cerevisiae, S. diastaticus, S. douglasii, S. kluyveri, S. norbensis, S. oviformis), Schizosaccharomyces, or Yarrowia (e.g., Y. lipolytica). In some embodiments, the protein is produced by and obtained from a plant cell selected from the families Amaranthaceae (e.g., chard, spinach, sugar beet, quinoa), Asteraceae (e.g., artichoke, asters, chamomile, chicory, chrysanthemums, dahlias, daisies, echinacea, goldenrod, guayule, lettuce, marigolds, safflower, sunflowers, zinnias), Brassicaceae (e.g., arugula, broccoli, bok choy, Brussels sprouts, cabbage, cauliflower, canola, collard greens, daikon, garden cress, horseradish, kale, mustard, radish, rapeseed, rutabaga, turnip, wasabi, watercress, Arabidopsis thaliana), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, pumpkin, squash (e.g., acorn squash, butternut squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentils, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch), Malvaceae (e.g., cacao, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, lawn grass (e.g., Bahia grass, Bermudagrass, bluegrass, Buffalograss, Centipede grass, Fescue, or Zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugar cane, triticale, wheat and other cereal crops, Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almonds, apples, apricots, blackberry, blueberry, cherries, peaches, plums, quinces, raspberries, roses, strawberries), Rutaceae (e.g., curry, grapefruit, lemon, lime, kumquat, mandarin, orange), Solanaceae (e.g., bell peppers, chili peppers, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape). Cells may be cultivated in a nutrient medium suitable for production of the protein using methods known in the art. For example, the cell may be cultivated by shake flask cultivation, or small-scale or large-scale fermentation (including continuous, batch, fed-batch, or solid-state, and/or microcarrier-based fermentations) in laboratory or industrial fermentors in a suitable medium and under conditions allowing the protein to be expressed and/or isolated. Suitable media are available from commercial suppliers or may be prepared according to published compositions (e.g., in catalogues of the American Type Culture Collection). If the protein is secreted into the nutrient medium, the protein can be recovered directly from the medium. If the protein is not secreted, it can be recovered from cell lysates. The protein may be detected using methods known in the art that are specific for the protein, including, but not limited to, the use of specific antibodies, formation of an enzyme product, disappearance of an enzyme substrate, or an assay determining the relative or specific activity of the protein. The protein may be recovered from the medium using methods known in the art, including, but not limited to, collection, centrifugation, filtration, extraction, spray-drying, evaporation, or precipitation. In one aspect, a whole fermentation broth comprising the protein is recovered. In another aspect, a cell-free fermentation broth comprising the protein is recovered. In some embodiments, the protein is secreted extracellularly. In some embodiments, the protein is isolated. In some embodiments, the protein is purified. The protein may be purified by a variety of procedures known in the art to obtain substantially pure proteins and/or protein fragments (see, e.g., Wingfield, 2015, Current Protocols in Protein Science; 80(1): 6.1.1-6.1.35; Labrou, 2014, Protein Downstream Processing, 1129: 3-10). In an alternative aspect, the protein is not recovered. The present disclosure also provides cells that naturally express native proteins of the present disclosure and cells that have been engineered to express heterologous proteins of the present disclosure (e.g., recombinant host cells comprising a polynucleotide of the present disclosure operably linked to one or more control sequences that direct the production of a protein of the present disclosure), as well as tools and methods for producing such recombinant host cells, including polynucleotides encoding proteins of the present disclosure and nucleic acid constructs comprising such polynucleotides. In some embodiments, the cell is a Gram-negative bacterium, such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Citrobacter (e.g., C. amalonaticus, C. braakii, C. freundii, C. gillenii, C. werkmanii), Cronobacter (e.g., C. sakazakii, C. turicensis), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Kosakonia (e.g., K. sacchari), Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella or Ureaplasma. In some embodiments, the cell is a Gram-positive bacterium, such as Alkalihalobacillus (e.g., A. akibai, A. clausii), Bacillus (e.g., B. agaradhaerens, B. alkalophilus, B. amyloliquefaciens, B. brevis, B. circulans, B. clausii, B. coagulans, B. deramificans, B. firmus, B. lautus, B. lentus, B. licheniformis, B. megaterium, B. pumilus, B. stearothermophilus, B. subtilis, B. thuringiensis), Clostridium, Effusibacillus (e.g., E. pohliae), Enterococcus, Geobacillus (e.g., G. stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., L. lenta), Neobacillus (e.g., N. novalis), Nocardiopsis, Oceanobacillus (e.g., O. barbara), Staphylococcus, Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, and S. equi subsp. Zooepidemicus) or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sutcliffiella (e.g., S. halmapala). In some embodiments, the cell is a fungal cell, such as Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. caregiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis subrufa, C. subvermispora), Chaetomium (e.g., C. erraticum, C. globosum), Chrysosporium (e.g., C. inops, C. keratinophilum, C. lucknowense, C. merdarium, C. pannicola, C. queenslandicum, C. tropicum, C. zonatum), Colletotrichum (e.g., C. graminicola), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (e.g., C. hirsutus), Cryphonectria (e.g., C. parasitica), Cryptococcus, Evansstolkia (e.g., E. leycettana), Filibasidium, Fusarium (e.g., F. bactridioides, F. cerealis, F. crookwellense, F. culmorum, F. graminearum, F. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum), Peniophora (e.g., P. lycii), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Podospora (e.g., P. anserina), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. versicolor), Trichoderma (e.g., T. atroviride, T. harzianum, T. koningii, T. longibrachiatum, T. reesei, T. viride), Trichophaea (e.g., T. saccata), or Urnula (e.g., U. criterium). In some embodiments, the cell is a yeast cell, such as Candida, Hansenula, Komagataella (e.g., K. phaffii), Kluyveromyces (e.g., Kluyveromyces lactis), Pichia (e.g., P. pastoris), Saccharomyces (e.g., S. carlsbergensis, S. cerevisiae, S. diastaticus, S. douglasii, S. kluyveri, S. norbensis, S. oviformis), Schizosaccharomyces, or Yarrowia (e.g., Yarrowia lipolytica). In some embodiments, the cell is a plant cell, optionally a plant cell selected from the families Amaranthaceae (e.g., chard, spinach, sugar beet, quinoa), Asteraceae (e.g., artichoke, asters, chamomile, chicory, chrysanthemums, dahlias, daisies, echinacea, goldenrod, guayule, lettuce, marigolds, safflower, sunflowers, zinnias), Brassicaceae (e.g., arugula, broccoli, bok choy, Brussels sprouts, cabbage, cauliflower, canola, collard greens, daikon, garden cress, horseradish, kale, mustard, radish, rapeseed, rutabaga, turnip, wasabi, watercress, Arabidopsis thaliana), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, pumpkin, squash (e.g., acorn squash, butternut squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentils, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch), Malvaceae (e.g., cacao, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, lawn grass (e.g., Bahia grass, Bermudagrass, bluegrass, Buffalograss, Centipede grass, Fescue, or Zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugar cane, triticale, wheat and other cereal crops, Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almonds, apples, apricots, blackberry, blueberry, cherries, peaches, plums, quinces, raspberries, roses, strawberries), Rutaceae (e.g., curry, grapefruit, lemon, lime, kumquat, mandarin, orange), Solanaceae (e.g., bell peppers, chili peppers, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape). In preferred embodiments, cells of the present disclosure express or more of the proteins described above. In some embodiments, cells of the present disclosure comprise a homologous or heterologous nucleic acid sequence that is at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% identical to one or more of the nucleic acid sequences set forth herein as SEQ ID NO(s): 4–6 or the cDNA sequence thereof. In preferred embodiments, cells of the present disclosure comprise a polynucleotide that comprises, consists essentially of or consists of the nucleic acid sequence of any one of SEQ ID NO(s): 4–6 or a cDNA sequence thereof. Also included within the scope of the present disclosure are the progeny of such cells. The present disclosure thus encompasses plants and plant parts expressing one or more proteins of the present disclosure, including plants and plant parts that have been engineered to (over)express one or more proteins of the present disclosure, as well as methods producing proteins of the present disclosure comprising cultivating a (transgenic) plant or a plant part comprising a polynucleotide that encodes the protein under conditions conducive for production of the protein, and, optionally, recovering the protein. In alternative embodiments, such plants may be used as is to enhance one or more food/feed characteristics (e.g., improve nutritional value, palatability and/or rheological properties, destroy an antinutritive factor, etc.). In preferred embodiments, plants and plant parts of the present disclosure express one or more of the proteins described above. In some embodiments, plants and plant parts of the present disclosure comprise a homologous or heterologous nucleic acid sequence that is at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% identical to one or more of the nucleic acid sequences set forth herein as SEQ ID NO(s): 4–6 or the cDNA sequence thereof. In preferred embodiments, plants and plant parts of the present disclosure comprise a polynucleotide that comprises, consists essentially of or consists of the nucleic acid sequence of any one of SEQ ID NO(s): 4–6 or a cDNA sequence thereof. Also included within the scope of the present disclosure are the progeny of such plants and plant parts. The present disclosure extends to tools and methods for producing recombinant host cells that express one or more proteins of the present disclosure, including polynucleotides encoding proteins of the present disclosure and nucleic acid constructs comprising such polynucleotides. The present disclosure provides polynucleotides encoding proteins of the present disclosure, including, but not limited to, nucleic acid constructs and recombinant expression vectors that encode one or more enzymes of the present disclosure, as well as methods of producing such polynucleotides. The polynucleotide may be a genomic DNA, a cDNA, a synthetic DNA, a synthetic RNA, a mRNA, or a combination thereof. The polynucleotide may be cloned from any suitable genus, species or strain. In some embodiments, the protein is cloned from a Gram-negative bacterium, such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Citrobacter (e.g., C. amalonaticus, C. braakii, C. freundii, C. gillenii, C. werkmanii), Cronobacter (e.g., C. sakazakii, C. turicensis), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Kosakonia (e.g., K. sacchari), Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella or Ureaplasma. In some embodiments, the polynucleotide is cloned from a Gram-positive bacterium, such as Alkalihalobacillus (e.g., A. akibai, A. clausii), Bacillus (e.g., B. agaradhaerens, B. alkalophilus, B. amyloliquefaciens, B. brevis, B. circulans, B. clausii, B. coagulans, B. deramificans, B. firmus, B. lautus, B. lentus, B. licheniformis, B. megaterium, B. pumilus, B. stearothermophilus, B. subtilis, B. thuringiensis), Clostridium, Effusibacillus (e.g., E. pohliae), Enterococcus, Geobacillus (e.g., G. stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., L. lenta), Neobacillus (e.g., N. novalis), Nocardiopsis, Oceanobacillus (e.g., O. barbara), Staphylococcus, Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, and S. equi subsp. Zooepidemicus) or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sutcliffiella (e.g., S. halmapala). In some embodiments, the polynucleotide is cloned from a fungus, such as Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. caregiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis subrufa, C. subvermispora), Chaetomium (e.g., C. erraticum, C. globosum), Chrysosporium (e.g., C. inops, C. keratinophilum, C. lucknowense, C. merdarium, C. pannicola, C. queenslandicum, C. tropicum, C. zonatum), Colletotrichum (e.g., C. graminicola), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (e.g., C. hirsutus), Cryphonectria (e.g., C. parasitica), Cryptococcus, Evansstolkia (e.g., E. leycettana), Filibasidium, Fusarium (e.g., F. bactridioides, F. cerealis, F. crookwellense, F. culmorum, F. graminearum, F. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum), Peniophora (e.g., P. lycii), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Podospora (e.g., P. anserina), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. versicolor), Trichoderma (e.g., T. atroviride, T. harzianum, T. koningii, T. longibrachiatum, T. reesei, T. viride), Trichophaea (e.g., T. saccata), or Urnula (e.g., U. criterium). In some embodiments, the polynucleotide is cloned from a yeast, such as Candida, Hansenula, Komagataella (e.g., K. phaffii), Kluyveromyces (e.g., K. lactis), Pichia (e.g., P. pastoris), Saccharomyces (e.g., S. carlsbergensis, S. cerevisiae, S. diastaticus, S. douglasii, S. kluyveri, S. norbensis, S. oviformis), Schizosaccharomyces, or Yarrowia (e.g., Y. lipolytica). In some embodiments, the polynucleotide is cloned from a plant cell selected from the families Amaranthaceae (e.g., chard, spinach, sugar beet, quinoa), Asteraceae (e.g., artichoke, asters, chamomile, chicory, chrysanthemums, dahlias, daisies, echinacea, goldenrod, guayule, lettuce, marigolds, safflower, sunflowers, zinnias), Brassicaceae (e.g., arugula, broccoli, bok choy, Brussels sprouts, cabbage, cauliflower, canola, collard greens, daikon, garden cress, horseradish, kale, mustard, radish, rapeseed, rutabaga, turnip, wasabi, watercress, Arabidopsis thaliana), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, pumpkin, squash (e.g., acorn squash, butternut squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentils, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch), Malvaceae (e.g., cacao, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, lawn grass (e.g., Bahia grass, Bermudagrass, bluegrass, Buffalograss, Centipede grass, Fescue, or Zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugar cane, triticale, wheat and other cereal crops, Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almonds, apples, apricots, blackberry, blueberry, cherries, peaches, plums, quinces, raspberries, roses, strawberries), Rutaceae (e.g., curry, grapefruit, lemon, lime, kumquat, mandarin, orange), Solanaceae (e.g., bell peppers, chili peppers, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape). In preferred embodiments, polynucleotides of the present disclosure encode one or more of the proteins described above. Polynucleotides of the present disclosure may be mutated by introduction of nucleotide substitutions that do not result in a change in the amino acid sequence of the protein, but which correspond to the codon usage of the host organism intended for production of the enzyme, or by introduction of nucleotide substitutions that may give rise to a different amino acid sequence. For a general description of nucleotide substitution, see, e.g., Ford et al., 1991, Protein Expression and Purification 2: 95-107. In an aspect, the polynucleotide is isolated. In another aspect, the polynucleotide is purified. The present disclosure also provides nucleic acid constructs comprising a polynucleotide of the present disclosure, wherein the polynucleotide is operably linked to one or more control sequences that direct the expression of the coding sequence in a suitable host cell under conditions compatible with the control sequences. The polynucleotide may be manipulated in a variety of ways to provide for expression of the protein. Manipulation of the polynucleotide prior to its insertion into a vector may be desirable or necessary depending on the expression vector. Techniques for modifying polynucleotides utilizing recombinant DNA methods are well known in the art. The control sequence may be a promoter, a polynucleotide that is recognized by a host cell for expression of a polynucleotide encoding a protein of the present disclosure. The promoter contains transcriptional control sequences that mediate the expression of the protein. The promoter may be any polynucleotide that shows transcriptional activity in the host cell including mutant, truncated, and hybrid promoters, and may be obtained from genes encoding extracellular or intracellular proteins either homologous or heterologous to the host cell. Examples of suitable promoters for directing transcription of the polynucleotide of the present disclosure in a bacterial host cell are described in Sambrook et al., 1989, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Lab., NY, Davis et al., 2012, supra, and Song et al., 2016, PLOS One 11(7): e0158447. Examples of suitable promoters for directing transcription of the polynucleotide of the present disclosure in a filamentous fungal host cell are promoters obtained from Aspergillus, Fusarium, Rhizomucor and Trichoderma cells, such as the promoters described in Mukherjee et al., 2013, "Trichoderma: Biology and Applications", and by Schmoll and Dattenböck, 2016, "Gene Expression Systems in Fungi: Advancements and Applications", Fungal Biology. For expression in a yeast host, examples of useful promoters are described by Smolke et al., 2018, "Synthetic Biology: Parts, Devices and Applications" (Chapter 6: Constitutive and Regulated Promoters in Yeast: How to Design and Make Use of Promoters in S. cerevisiae), and by Schmoll and Dattenböck, 2016, "Gene Expression Systems in Fungi: Advancements and Applications", Fungal Biology. The control sequence may also be a transcription terminator, which is recognized by a host cell to terminate transcription. The terminator is operably linked to the 3’-terminus of the polynucleotide encoding the protein. Any terminator that is functional in the host cell may be used in the present disclosure. Preferred terminators for bacterial host cells may be obtained from the genes for Bacillus clausii alkaline protease (aprH), Bacillus licheniformis alpha-amylase (amyL), and Escherichia coli ribosomal RNA (rrnB). Preferred terminators for filamentous fungal host cells may be obtained from Aspergillus or Trichoderma species, such as obtained from the genes for Aspergillus niger glucoamylase, Trichoderma reesei beta-glucosidase, Trichoderma reesei cellobiohydrolase I, and Trichoderma reesei endoglucanase I, such as the terminators described in Mukherjee et al., 2013, "Trichoderma: Biology and Applications", and by Schmoll and Dattenböck, 2016, "Gene Expression Systems in Fungi: Advancements and Applications", Fungal Biology. Preferred terminators for yeast host cells may be obtained from the genes for Saccharomyces cerevisiae enolase, Saccharomyces cerevisiae cytochrome C (CYC1), and Saccharomyces cerevisiae glyceraldehyde-3-phosphate dehydrogenase. Other useful terminators for yeast host cells are described by Romanos et al., 1992, Yeast 8: 423-488. The control sequence may also be an mRNA stabilizer region downstream of a promoter and upstream of the coding sequence of a gene which increases expression of the gene. Examples of suitable mRNA stabilizer regions are obtained from a Bacillus thuringiensis cryIIIA gene (WO 94/25612) and a Bacillus subtilis SP82 gene (Hue et al., 1995, J. Bacteriol.177: 3465-3471). Examples of mRNA stabilizer regions for fungal cells are described in Geisberg et al., 2014, Cell 156(4): 812- 824, and in Morozov et al., 2006, Eukaryotic Cell 5(11): 1838-1846. The control sequence may also be a leader, a non-translated region of an mRNA that is important for translation by the host cell. The leader is operably linked to the 5’-terminus of the polynucleotide encoding the protein. Any leader that is functional in the host cell may be used. Suitable leaders for bacterial host cells are described by Hambraeus et al., 2000, Microbiology 146(12): 3051- 3059, and by Kaberdin and Bläsi, 2006, FEMS Microbiol. Rev.30(6): 967-979. Preferred leaders for filamentous fungal host cells may be obtained from the genes for Aspergillus oryzae TAKA amylase and Aspergillus nidulans triose phosphate isomerase. Suitable leaders for yeast host cells may be obtained from the genes for Saccharomyces cerevisiae enolase (ENO-1), Saccharomyces cerevisiae 3-phosphoglycerate kinase, Saccharomyces cerevisiae alpha-factor, and Saccharomyces cerevisiae alcohol dehydrogenase/glyceraldehyde-3-phosphate dehydrogenase (ADH2/GAP). The control sequence may also be a polyadenylation sequence, a sequence operably linked to the 3’-terminus of the polynucleotide which, when transcribed, is recognized by the host cell as a signal to add polyadenosine residues to transcribed mRNA. Any polyadenylation sequence that is functional in the host cell may be used. Preferred polyadenylation sequences for filamentous fungal host cells are obtained from the genes for Aspergillus nidulans anthranilate synthase, Aspergillus niger glucoamylase, Aspergillus niger alpha-glucosidase, Aspergillus oryzae TAKA amylase, and Fusarium oxysporum trypsin-like protease. Useful polyadenylation sequences for yeast host cells are described by Guo and Sherman, 1995, Mol. Cellular Biol.15: 5983-5990. The control sequence may also be a signal peptide coding region that encodes a signal peptide linked to the N-terminus of a protein and directs the protein into the cell’s secretory pathway. The 5’-end of the coding sequence of the polynucleotide may inherently contain a signal peptide coding sequence naturally linked in translation reading frame with the segment of the coding sequence that encodes the protein. Alternatively, the 5’-end of the coding sequence may contain a signal peptide coding sequence that is heterologous to the coding sequence. A heterologous signal peptide coding sequence may be required where the coding sequence does not naturally contain a signal peptide coding sequence. Alternatively, a heterologous signal peptide coding sequence may simply replace the natural signal peptide coding sequence to enhance secretion of the protein. Any signal peptide coding sequence that directs the expressed protein into the secretory pathway of a host cell may be used. Effective signal peptide coding sequences for bacterial host cells are the signal peptide coding sequences obtained from the genes for Bacillus NCIB 11837 maltogenic amylase, Bacillus licheniformis subtilisin, Bacillus licheniformis beta- lactamase, Bacillus stearothermophilus alpha-amylase, Bacillus stearothermophilus neutral proteases (nprT, nprS, nprM), and Bacillus subtilis prsA. Further signal peptides are described by Freudl, 2018, Microbial Cell Factories 17: 52. Effective signal peptide coding sequences for filamentous fungal host cells are the signal peptide coding sequences obtained from the genes for Aspergillus niger neutral amylase, Aspergillus niger glucoamylase, Aspergillus oryzae TAKA amylase, Humicola insolens cellulase, Humicola insolens endoglucanase V, Humicola lanuginosa lipase, and Rhizomucor miehei aspartic proteinase, such as the signal peptide described by Xu et al., 2018, Biotechnology Letters 40: 949-955 Useful signal peptides for yeast host cells are obtained from the genes for Saccharomyces cerevisiae alpha-factor and Saccharomyces cerevisiae invertase. Other useful signal peptide coding sequences are described by Romanos et al., 1992, supra. The control sequence may also be a propeptide coding sequence that encodes a propeptide positioned at the N-terminus of a protein. The resultant protein is known as a proenzyme or proprotein (or a zymogen in some cases). A proprotein is generally inactive and can be converted to an active protein by catalytic or autocatalytic cleavage of the propeptide from the proprotein. The propeptide coding sequence may be obtained from the genes for Bacillus subtilis alkaline protease (aprE), Bacillus subtilis neutral protease (nprT), Myceliophthora thermophila laccase (WO 95/33836), Rhizomucor miehei aspartic proteinase, and Saccharomyces cerevisiae alpha-factor. Where both signal peptide and propeptide sequences are present, the propeptide sequence is positioned next to the N-terminus of a protein and the signal peptide sequence is positioned next to the N-terminus of the propeptide sequence. Additionally or alternatively, when both signal peptide and propeptide sequences are present, the protein may comprise only a part of the signal peptide sequence and/or only a part of the propeptide sequence. Alternatively, the final or isolated protein may comprise a mixture of mature proteins and proteins which comprise, either partly or in full length, a propeptide sequence and/or a signal peptide sequence. It may also be desirable to add regulatory sequences that regulate expression of the protein relative to the growth of the host cell. Examples of regulatory sequences are those that cause expression of the gene to be turned on or off in response to a chemical or physical stimulus, including the presence of a regulatory compound. Regulatory sequences in prokaryotic systems include the lac, tac, and trp operator systems. In yeast, the ADH2 system or GAL1 system may be used. In filamentous fungi, the Aspergillus niger glucoamylase promoter, Aspergillus oryzae TAKA alpha-amylase promoter, and Aspergillus oryzae glucoamylase promoter, Trichoderma reesei cellobiohydrolase I promoter, and Trichoderma reesei cellobiohydrolase II promoter may be used. Other examples of regulatory sequences are those that allow for gene amplification. In fungal systems, these regulatory sequences include the dihydrofolate reductase gene that is amplified in the presence of methotrexate, and the metallothionein genes that are amplified with heavy metals. The control sequence may also be a transcription factor, a polynucleotide encoding a polynucleotide-specific DNA-binding protein that controls the rate of the transcription of genetic information from DNA to mRNA by binding to a specific polynucleotide sequence. The transcription factor may function alone and/or together with one or more other proteins or transcription factors in a complex by promoting or blocking the recruitment of RNA polymerase. Transcription factors are characterized by comprising at least one DNA-binding domain which often attaches to a specific DNA sequence adjacent to the genetic elements which are regulated by the transcription factor. The transcription factor may regulate the expression of a protein of interest either directly, i.e., by activating the transcription of the gene encoding the protein of interest by binding to its promoter, or indirectly, i.e., by activating the transcription of a further transcription factor which regulates the transcription of the gene encoding the protein of interest, such as by binding to the promoter of the further transcription factor. Suitable transcription factors for fungal host cells are described in WO 2017/144177. Suitable transcription factors for prokaryotic host cells are described in Seshasayee et al., 2011, Subcellular Biochemistry 52: 7-23, as well in Balleza et al., 2009, FEMS Microbiol. Rev.33(1): 133-151. The present disclosure also provides recombinant expression vectors comprising a polynucleotide of the present disclosure, a promoter, and transcriptional and translational stop signals. The various nucleotide and control sequences may be joined together to produce a recombinant expression vector that may include one or more convenient restriction sites to allow for insertion or substitution of the polynucleotide encoding the protein at such sites. Alternatively, the polynucleotide may be expressed by inserting the polynucleotide or a nucleic acid construct comprising the polynucleotide into an appropriate vector for expression. In creating the expression vector, the coding sequence is located in the vector so that the coding sequence is operably linked with the appropriate control sequences for expression. The recombinant expression vector may be any vector (e.g., a plasmid or virus) that can be conveniently subjected to recombinant DNA procedures and can bring about expression of the polynucleotide. The choice of the vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced. The vector may be a linear or closed circular plasmid. The vector may be an autonomously replicating vector, i.e., a vector that exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g., a plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector may contain any means for assuring self-replication. Alternatively, the vector may be one that, when introduced into the host cell, is integrated into the genome and replicated together with the chromosome(s) into which it has been integrated. Furthermore, a single vector or plasmid or two or more vectors or plasmids that together contain the total DNA to be introduced into the genome of the host cell, or a transposon, may be used. The vector preferably contains one or more selectable markers that permit easy selection of transformed, transfected, transduced, or the like cells. A selectable marker is a gene the product of which provides for biocide or viral resistance, resistance to heavy metals, prototrophy to auxotrophs, and the like. The vector preferably contains at least one element that permits integration of the vector into the host cell's genome or autonomous replication of the vector in the cell independent of the genome. For integration into the host cell genome, the vector may rely on the polynucleotide’s sequence encoding the protein or any other element of the vector for integration into the genome by homologous recombination, such as homology- directed repair (HDR), or non-homologous recombination, such as non-homologous end-joining (NHEJ). For autonomous replication, the vector may further comprise an origin of replication enabling the vector to replicate autonomously in the host cell in question. The origin of replication may be any plasmid replicator mediating autonomous replication that functions in a cell. The term "origin of replication" or "plasmid replicator" means a polynucleotide that enables a plasmid or vector to replicate in vivo. More than one copy of a polynucleotide of the present disclosure may be inserted into a host cell to increase production of a protein. For example, 2 or 3 or 4 or 5 or more copies are inserted into a host cell. An increase in the copy number of the polynucleotide can be obtained by integrating at least one additional copy of the sequence into the host cell genome or by including an amplifiable selectable marker gene with the polynucleotide where cells containing amplified copies of the selectable marker gene, and thereby additional copies of the polynucleotide, can be selected for by cultivating the cells in the presence of the appropriate selectable agent. The present disclosure also provides methods for producing recombinant host cells comprising a polynucleotide of the present disclosure operably linked to one or more control sequences that direct the production of a protein of the present disclosure. A construct or vector comprising a polynucleotide is introduced into a host cell so that the construct or vector is maintained as a chromosomal integrant or as a self-replicating extra-chromosomal vector as described earlier. The choice of a host cell will to a large extent depend upon the gene encoding the protein and its source. The protein can be native or heterologous to the recombinant host cell. Also, at least one of the one or more control sequences can be heterologous to the polynucleotide encoding the protein. The recombinant host cell may comprise a single copy, or at least two copies, e.g., three, four, five, or more copies of the polynucleotide of the present disclosure. The host cell may be any cell useful in the recombinant production of a protein of the present disclosure, including, not limited to, prokaryotic cells, fungal cells and plant cells, as described above. In an aspect, the host cell is isolated. In another aspect, the host cell is purified. In some embodiments, the host cell is a Gram-negative bacterium, such as Campylobacter, Chryseobacterium (e.g., C. viscerum), Citrobacter (e.g., C. amalonaticus, C. braakii, C. freundii, C. gillenii, C. werkmanii), Cronobacter (e.g., C. sakazakii, C. turicensis), Dicytoglomus (e.g., D. thermophilum), Escherichia (e.g., E. coli), Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Kosakonia (e.g., K. sacchari), Lysobacter (e.g., L. gummosus), Neisseria, Pseudomonas, Salmonella or Ureaplasma. In some embodiments, the host cell is a Gram-positive bacterium, such as Alkalihalobacillus (e.g., A. akibai, A. clausii), Bacillus (e.g., B. agaradhaerens, B. alkalophilus, B. amyloliquefaciens, B. brevis, B. circulans, B. clausii, B. coagulans, B. deramificans, B. firmus, B. lautus, B. lentus, B. licheniformis, B. megaterium, B. pumilus, B. stearothermophilus, B. subtilis, B. thuringiensis), Clostridium, Effusibacillus (e.g., E. pohliae), Enterococcus, Geobacillus (e.g., G. stearothermophilus), Lactobacillus, Lactococcus, Lederbergia (e.g., L. lenta), Neobacillus (e.g., N. novalis), Nocardiopsis, Oceanobacillus (e.g., O. barbara), Staphylococcus, Streptococcus (e.g., S. equisimilis, S. pyogenes, S. uberis, and S. equi subsp. Zooepidemicus) or Streptomyces (e.g., S. achromogenes, S. avermitilis, S. coelicolor, S. griseus, S. lividans), Sutcliffiella (e.g., S. halmapala). Methods for introducing DNA into prokaryotic host cells are well-known in the art, and any suitable method can be used including but not limited to protoplast transformation, competent cell transformation, electroporation, conjugation, transduction, with DNA introduced as linearized or as circular polynucleotide. Persons skilled in the art will be readily able to identify a suitable method for introducing DNA into a given prokaryotic cell depending, e.g., on the genus. Methods for introducing DNA into prokaryotic host cells are for example described in Heinze et al., 2018, BMC Microbiology 18:56, Burke et al., 2001, Proc. Natl. Acad. Sci. USA 98: 6289-6294, Choi et al., 2006, J. Microbiol. Methods 64: 391-397, and Donald et al., 2013, J. Bacteriol.195(11): 2612-2620. In some embodiments, the host cell is a fungal cell, such as Acremonium, Acrophialophora (e.g., A. fusispora), Aspergillus (e.g., A. aculeatus, A. awamori, A. chevalieri, A. foetidus, A. fumigatus, A. japonicus, A. nidulans, A. niger, A. niveoglaucus, A. oryzae, A. tubingensis), Aureobasidium, Bjerkandera (e.g., B. adusta, B. fumosa), Ceriporiopsis (e.g., C. aneirina, C. caregiea, C. gilvescens, C. pannocinta, C. rivulosa, Ceriporiopsis subrufa, C. subvermispora), Chaetomium (e.g., C. erraticum, C. globosum), Chrysosporium (e.g., C. inops, C. keratinophilum, C. lucknowense, C. merdarium, C. pannicola, C. queenslandicum, C. tropicum, C. zonatum), Colletotrichum (e.g., C. graminicola), Coprinopsis (e.g., C. cinereus), Coprinus (e.g., C. cinereus), Coriolus (e.g., C. hirsutus), Cryphonectria (e.g., C. parasitica), Cryptococcus, Evansstolkia (e.g., E. leycettana), Filibasidium, Fusarium (e.g., F. bactridioides, F. cerealis, F. crookwellense, F. culmorum, F. graminearum, F. graminum, F. heterosporum, F. longipes, F. negundi, F. oxysporum, F. reticulatum, F. roseum, F. sambucinum, F. sarcochroum, F. solani, F. sporotrichioides, F. sulphureum, F. torulosum, F. trichothecioides, F. venenatum), Humicola (e.g., H. insolens, H. lanuginosa), Magnaporthe, Microdochium (e.g., M. nivale), Mucor (e.g., M. miehei), Myceliophthora (e.g., M. thermophila), Neocallimastix, Neurospora (e.g., Neurospora crassa), Ostropa (e.g., O. barbara), Paecilomyces, Penicillium (e.g., P. emersonii, P. purpurogenum, P. thomii, P. viridicatum), Peniophora (e.g., P. lycii), Phanerochaete (e.g., P. chrysosporium), Phlebia (e.g., Phlebia radiata), Piromyces, Pleurotus (e.g., Pleurotus eryngii), Podospora (e.g., P. anserina), Pseudoplectania (e.g., P. vogesiaca), Schizophyllum, Sodiomyces (e.g., S. alcalophilus), Stenocarpella (e.g., S. maydis), Talaromyces (e.g., T. bacillisporus, T. emersonii, T. pinophilus), Thermoascus (e.g., T. aurantiacus), Themochaetoides (e.g., T. thermophila), Thermomyces (e.g., T. lanuginosus), Thermothielavioides (e.g., T. terrestris), Thermothelomyces (e.g., T. thermophilus), Thielavia (e.g., T. terrestris), Tolypocladium, Trametes (e.g., T. hirsuta, T. villosa, T. versicolor), Trichoderma (e.g., T. atroviride, T. harzianum, T. koningii, T. longibrachiatum, T. reesei, T. viride), Trichophaea (e.g., T. saccata), or Urnula (e.g., U. criterium). In some embodiments, the host cell is a yeast cell, such as Candida, Hansenula, Komagataella (e.g., K. phaffii), Kluyveromyces (e.g., Kluyveromyces lactis), Pichia (e.g., P. pastoris), Saccharomyces (e.g., S. carlsbergensis, S. cerevisiae, S. diastaticus, S. douglasii, S. kluyveri, S. norbensis, S. oviformis), Schizosaccharomyces, or Yarrowia (e.g., Yarrowia lipolytica). Fungal cells may be transformed by a process involving protoplast-mediated transformation, Agrobacterium- mediated transformation, electroporation, biolistic method and shock-wave-mediated transformation as reviewed by Li et al., 2017, Microbial Cell Factories 16: 168 and procedures described in EP 238023, Yelton et al., 1984, Proc. Natl. Acad. Sci. USA 81: 1470-1474, Christensen et al., 1988, Bio/Technology 6: 1419-1422, and Lubertozzi and Keasling, 2009, Biotechn. Advances 27: 53-75. However, any method known in the art for introducing DNA into a fungal host cell can be used, and the DNA can be introduced as linearized or as circular polynucleotide. In some embodiments, the host cell is a plant cell, optionally a plant cell selected from the families Amaranthaceae (e.g., chard, spinach, sugar beet, quinoa), Asteraceae (e.g., artichoke, asters, chamomile, chicory, chrysanthemums, dahlias, daisies, echinacea, goldenrod, guayule, lettuce, marigolds, safflower, sunflowers, zinnias), Brassicaceae (e.g., arugula, broccoli, bok choy, Brussels sprouts, cabbage, cauliflower, canola, collard greens, daikon, garden cress, horseradish, kale, mustard, radish, rapeseed, rutabaga, turnip, wasabi, watercress, Arabidopsis thaliana), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, pumpkin, squash (e.g., acorn squash, butternut squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentils, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch), Malvaceae (e.g., cacao, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, lawn grass (e.g., Bahia grass, Bermudagrass, bluegrass, Buffalograss, Centipede grass, Fescue, or Zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugar cane, triticale, wheat and other cereal crops, Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almonds, apples, apricots, blackberry, blueberry, cherries, peaches, plums, quinces, raspberries, roses, strawberries), Rutaceae (e.g., curry, grapefruit, lemon, lime, kumquat, mandarin, orange), Solanaceae (e.g., bell peppers, chili peppers, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape). Transgenic plants and plant cells expressing the protein may be constructed in accordance with methods known in the art. In short, the plant or plant cell is constructed by incorporating one or more expression constructs encoding the protein into the plant host genome or chloroplast genome and propagating the resulting modified plant or plant cell into a transgenic plant or plant cell. In an embodiment, a plant cell does not belong to plant varieties. The expression construct is conveniently a nucleic acid construct that comprises a polynucleotide encoding a protein, wherein the polynucleotide is operably linked with appropriate regulatory sequences required for expression of the polynucleotide in the plant or plant part of choice. Furthermore, the expression construct may comprise a selectable marker useful for identifying plant cells into which the expression construct has been integrated and DNA sequences necessary for introduction of the construct into the plant in question (the latter depends on the DNA introduction method to be used). The choice of regulatory sequences, such as promoter and terminator sequences and optionally signal or transit sequences, is determined, for example, on the basis of when, where, and how the protein is desired to be expressed (Sticklen, 2008, Nature Reviews 9: 433-443). For instance, the expression of the gene encoding a protein may be constitutive or inducible, or may be developmental, stage or tissue specific, and the gene product may be targeted to a specific tissue or plant part such as seeds or leaves. Regulatory sequences are, for example, described by Tague et al., 1988, Plant Physiology 86: 506. For constitutive expression, the 35S-CaMV, the maize ubiquitin 1, or the rice actin 1 promoter may be used (Franck et al., 1980, Cell 21: 285-294; Christensen et al., 1992, Plant Mol. Biol.18: 675-689; Zhang et al., 1991, Plant Cell 3: 1155-1165). Organ-specific promoters may be, for example, a promoter from storage sink tissues such as seeds, potato tubers, and fruits (Edwards and Coruzzi, 1990, Ann. Rev. Genet. 24: 275-303), or from metabolic sink tissues such as meristems (Ito et al., 1994, Plant Mol. Biol.24: 863-878), a seed specific promoter such as the glutelin, prolamin, globulin, or albumin promoter from rice (Wu et al., 1998, Plant Cell Physiol.39: 885-889), a Vicia faba promoter from the legumin B4 and the unknown seed protein gene from Vicia faba (Conrad et al., 1998, J. Plant Physiol. 152: 708-711), a promoter from a seed oil body protein (Chen et al., 1998, Plant Cell Physiol.39: 935-941), the storage protein napA promoter from Brassica napus, or any other seed specific promoter known in the art, e.g., as described in WO 91/14772. Furthermore, the promoter may be a leaf specific promoter such as the rbcs promoter from rice or tomato (Kyozuka et al., 1993, Plant Physiol. 102: 991-1000), the chlorella virus adenine methyltransferase gene promoter (Mitra and Higgins, 1994, Plant Mol. Biol.26: 85-93), the aldP gene promoter from rice (Kagaya et al., 1995, Mol. Gen. Genet. 248: 668-674), or a wound inducible promoter such as the potato pin2 promoter (Xu et al., 1993, Plant Mol. Biol.22: 573-588). Likewise, the promoter may be induced by abiotic treatments such as temperature, drought, or alterations in salinity or induced by exogenously applied substances that activate the promoter, e.g., ethanol, oestrogens, plant hormones such as ethylene, abscisic acid, and gibberellic acid, and heavy metals. A promoter enhancer element may also be used to achieve higher expression of a protein in the plant. For instance, the promoter enhancer element may be an intron that is placed between the promoter and the polynucleotide encoding a protein. For instance, Xu et al., 1993, supra, disclose the use of the first intron of the rice actin 1 gene to enhance expression. The selectable marker gene and any other parts of the expression construct may be chosen from those available in the art. The nucleic acid construct is incorporated into the plant genome according to conventional techniques known in the art, including Agrobacterium-mediated transformation, virus-mediated transformation, microinjection, particle bombardment, biolistic transformation, and electroporation (Gasser et al., 1990, Science 244: 1293; Potrykus, 1990, Bio/Technology 8: 535; Shimamoto et al., 1989, Nature 338: 274). Agrobacterium tumefaciens-mediated gene transfer is a method for generating transgenic dicots (for a review, see Hooykas and Schilperoort, 1992, Plant Mol. Biol.19: 15-38) and for transforming monocots, although other transformation methods may be used for these plants. A method for generating transgenic monocots is particle bombardment (microscopic gold or tungsten particles coated with the transforming DNA) of embryonic calli or developing embryos (Christou, 1992, Plant J. 2: 275-281; Shimamoto, 1994, Curr. Opin. Biotechnol. 5: 158-162; Vasil et al., 1992, Bio/Technology 10: 667- 674). An alternative method for transformation of monocots is based on protoplast transformation as described by Omirulleh et al., 1993, Plant Mol. Biol.21: 415-428. Additional transformation methods include those described in U.S. Patent Nos. 6,395,966 and 7,151,204 (both of which are herein incorporated by reference in their entirety). Following transformation, the transformants having incorporated the expression construct are selected and regenerated into whole plants according to methods well known in the art. Often the transformation procedure is designed for the selective elimination of selection genes either during regeneration or in the following generations by using, for example, co-transformation with two separate T-DNA constructs or site-specific excision of the selection gene by a specific recombinase. In addition to direct transformation of a particular plant genotype with a construct of the present disclosure, transgenic plants may be made by crossing a plant having the construct to a second plant lacking the construct. For example, a construct encoding a protein can be introduced into a particular plant variety by crossing, without the need for ever directly transforming a plant of that given variety. Therefore, the present disclosure encompasses not only a plant directly regenerated from cells which have been transformed in accordance with the present disclosure, but also the progeny of such plants. As used herein, progeny may refer to the offspring of any generation of a parent plant prepared in accordance with the present disclosure. Such progeny may include a DNA construct prepared in accordance with the present disclosure. Crossing results in the introduction of a transgene into a plant line by cross pollinating a starting line with a donor plant line. Non-limiting examples of such steps are described in U.S. Patent No.7,151,204. Plants may be generated through a process of backcross conversion. For example, plants include plants referred to as a backcross converted genotype, line, inbred, or hybrid. Genetic markers may be used to assist in the introgression of one or more transgenes of the disclosure from one genetic background into another. Marker assisted selection offers advantages relative to conventional breeding in that it can be used to avoid errors caused by phenotypic variations. Further, genetic markers may provide data regarding the relative degree of elite germplasm in the individual progeny of a particular cross. For example, when a plant with a desired trait which otherwise has a non-agronomically desirable genetic background is crossed to an elite parent, genetic markers may be used to select progeny which not only possess the trait of interest, but also have a relatively large proportion of the desired germplasm. In this way, the number of generations required to introgress one or more traits into a particular genetic background is minimized. The present disclosure encompasses methods of producing a mutant of a parent cell, which comprises disrupting or deleting a polynucleotide, or a portion thereof, encoding a protein of the present disclosure, which results in the mutant cell producing less of the protein than the parent cell when cultivated under the same conditions. The mutant cell may be constructed by reducing or eliminating expression of the polynucleotide using methods well known in the art, for example, one or more nucleotide insertions, one or more gene disruptions, one or more nucleotide replacements, or one or more nucleotide deletions. The polynucleotide to be modified or inactivated may be, for example, the coding region or a part thereof essential for activity, or a regulatory or control element required for expression of the coding region, e.g., a functional part of a promoter sequence, and/or a regulatory or control element required for the transcription or translation of the polynucleotide. Other control sequences for possible modification include, but are not limited to, a leader, polyadenylation sequence, propeptide sequence, signal peptide sequence, transcription terminator, and transcriptional activator. Modification or inactivation of the polynucleotide may be performed by subjecting the parent cell to mutagenesis and selecting for mutant cells in which expression of the polynucleotide has been reduced or eliminated. The mutagenesis, which may be specific or random, may be performed, for example, by use of a suitable physical or chemical mutagenizing agent, by use of a suitable oligonucleotide, or by subjecting the DNA sequence to PCR generated mutagenesis. Furthermore, the mutagenesis may be performed by use of any combination of these mutagenizing agents. Examples of a physical or chemical mutagenizing agent include ultraviolet (UV) irradiation, hydroxylamine, N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), O-methyl hydroxylamine, nitrous acid, ethyl methane sulphonate (EMS), sodium bisulphite, formic acid, and nucleotide analogues (see J. L. Bose, Springer Protocols 2016, Methods in Molecular Biology, The Genetic Manipulation of Staphylococci). Additionally, or alternatively, nucleotides may be inserted or removed so as to result in the introduction of a stop codon, the removal of the start codon, or a change in the open reading frame. Such modification or inactivation may be accomplished by site-directed mutagenesis or PCR generated mutagenesis in accordance with methods known in the art, or by targeted gene editing using one or more nucleases, e.g., zinc-finger nucleases or CRISPR-associated nucleases. Additionally, or alternatively, the modification or inactivation may be achieved by gene silencing, genetic repression, genetic activation, and/or post-translational mutagenesis, e.g., by methods employing non-coding RNA, RNAi, siRNA, miRNA, ribozymes, catalytically inactive nucleases, CRISPRi, nucleotide methylation, and/or histone acetylation. The modification may be transient and/or reversible, irreversible and/or stable, or the modification may be dependent on chemical inducers or dependent on cultivation conditions, such as the cultivation temperature. The modification may be performed in vivo, i.e., directly on the cell expressing the polynucleotide to be modified, or the modification be performed in vitro. An example of a convenient way to eliminate or reduce expression of a polynucleotide is based on techniques of gene replacement, gene deletion, or gene disruption. For example, in the gene disruption method, a nucleic acid sequence corresponding to the endogenous polynucleotide is mutagenized in vitro to produce a defective nucleic acid sequence that is then transformed into the parent cell to produce a defective gene. By homologous recombination, the defective nucleic acid sequence replaces the endogenous polynucleotide. It may be desirable that the defective polynucleotide also encodes a marker that may be used for selection of transformants in which the polynucleotide has been modified or destroyed. In an aspect, the polynucleotide is disrupted with a selectable marker such as those described herein. The present disclosure further relates to a mutant cell of a parent cell that comprises a disruption or deletion of a polynucleotide encoding a protein or a control sequence thereof or a silenced gene encoding the protein, which results in the mutant cell producing less of the protein or no protein compared to the parent cell. Protein-deficient mutant cells are useful as host cells for expression of native and heterologous proteins. Therefore, the present disclosure further relates to methods of producing a native or heterologous protein, comprising (a) cultivating a protein-deficient mutant cell under conditions conducive for production of a desired protein (e.g., a protein of the present disclosure); and (b) recovering the desired protein. The term "heterologous proteins" means proteins that are not native to the host cell, e.g., a variant of a native protein. The host cell may comprise more than one copy of a polynucleotide encoding a desired native or heterologous protein. In some embodiments, the present disclosure relates to a protein product essentially free from [enzyme] activity that is produced by a method of the present disclosure. Proteins, polynucleotides and organisms of the present disclosure may be incorporated into any suitable formulation(s), including, but not limited to, formulations comprising one or more seed-compatible carriers, soil- compatible carriers, foliar-compatible carriers, preharvest carriers, and/or postharvest carriers. Selection of appropriate carrier materials will depend on the intended application(s) and the protein(s) to be included in the formulation, as well as any other components that may be present in and/or added to the formulation. In some embodiments, the carrier is a liquid, a gel, a slurry, or a solid. In some embodiments, the carrier consists essentially of or consists of one or more stabilizing agents. The present disclosure encompasses granules/particles comprising one or more proteins of the disclosure. In an embodiment, the granule comprises a core, and optionally one or more coatings (outer layers) surrounding the core. The core may have a diameter, measured as equivalent spherical diameter (volume based average particle size), of 20-2000 µm, particularly 50-1500 µm, 100-1500 µm or 250-1200 µm. The core diameter, measured as equivalent spherical diameter, can be determined using laser diffraction, such as using a Malvern Mastersizer and/or the method described under ISO13320 (2020). In an embodiment, the core comprises one or more proteins of the present disclosure. The core may include additional materials such as fillers, fiber materials (cellulose or synthetic fibers), stabilizing agents, solubilizing agents, suspension agents, viscosity regulating agents, light spheres, plasticizers, salts, lubricants and fragrances. The core may include a binder, such as synthetic polymer, wax, fat, or carbohydrate. The core may include a salt of a multivalent cation, a reducing agent, an antioxidant, a peroxide decomposing catalyst and/or an acidic buffer component, typically as a homogenous blend. The core may include an inert particle with the protein absorbed into it, or applied onto the surface, e.g., by fluid bed coating. The core may have a diameter of 20-2000 µm, particularly 50-1500 µm, 100-1500 µm or 250-1200 µm. The core may be surrounded by at least one coating, e.g., to improve the storage stability, to reduce dust formation during handling, or for coloring the granule. The optional coating(s) may include a salt coating, or other suitable coating materials, such as polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). The coating may be applied in an amount of at least 0.1% by weight of the core, e.g., at least 0.5%, at least 1%, at least 5%, at least 10%, or at least 15%. The amount may be at most 100%, 70%, 50%, 40% or 30%. The coating is preferably at least 0.1 µm thick, particularly at least 0.5 µm, at least 1 µm or at least 5 µm. In some embodiments, the thickness of the coating is below 100 µm, such as below 60 µm, or below 40 µm. The coating should encapsulate the core unit by forming a substantially continuous layer. A substantially continuous layer is to be understood as a coating having few or no holes, so that the core unit has few or no uncoated areas. The layer or coating should, in particular, be homogeneous in thickness. The coating can further contain other materials as known in the art, e.g., fillers, antisticking agents, pigments, dyes, plasticizers and/or binders, such as titanium dioxide, kaolin, calcium carbonate or talc. A salt coating may comprise at least 60% by weight of a salt, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% or at least 99% by weight. To provide acceptable protection, the salt coating is preferably at least 0.1 µm thick, e.g., at least 0.5 µm, at least 1 µm, at least 2 µm, at least 4 µm, at least 5 µm, or at least 8 µm. In a particular embodiment, the thickness of the salt coating is below 100 µm, such as below 60 µm, or below 40 µm. The salt may be added from a salt solution where the salt is completely dissolved or from a salt suspension wherein the fine particles are less than 50 µm, such as less than 10 µm or less than 5 μm. The salt coating may comprise a single salt or a mixture of two or more salts. The salt may be water soluble, in particular, having a solubility at least 0.1 g in 100 g of water at 20°C, preferably at least 0.5 g per 100 g water, e.g., at least 1 g per 100 g water, e.g., at least 5 g per 100 g water. The salt may be an inorganic salt, e.g., salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids (less than 10 carbon atoms, e.g., 6 or less carbon atoms) such as citrate, malonate or acetate. Examples of cations in these salts are alkali or earth alkali metal ions, the ammonium ion or metal ions of the first transition series, such as sodium, potassium, magnesium, calcium, zinc or aluminum. Examples of anions include chloride, bromide, iodide, sulfate, sulfite, bisulfite, thiosulfate, phosphate, monobasic phosphate, dibasic phosphate, hypophosphite, dihydrogen pyrophosphate, tetraborate, borate, carbonate, bicarbonate, metasilicate, citrate, malate, maleate, malonate, succinate, lactate, formate, acetate, butyrate, propionate, benzoate, tartrate, ascorbate or gluconate. In particular, alkali- or earth alkali metal salts of sulfate, sulfite, phosphate, phosphonate, nitrate, chloride or carbonate or salts of simple organic acids such as citrate, malonate or acetate may be used. The salt in the coating may have a constant humidity at 20°C above 60%, particularly above 70%, above 80% or above 85%, or it may be another hydrate form of such a salt (e.g., anhydrate). The salt coating may be as described in WO 00/01793 or WO 2006/034710. Specific examples of suitable salts are NaCl (CH_20°C=76%), Na₂CO₃ (CH_20°C=92%), NaNO₃ (CH_20°C=73%), Na₂HPO₄ (CH_20°C=95%), Na₃PO₄ (CH_25°C=92%), NH₄Cl (CH_20°C = 79.5%), (NH₄)₂HPO₄ (CH_20°C = 93,0%), NH₄H₂PO₄ (CH20°C = 93.1%), (NH4)2SO4 (CH20°C=81.1%), KCl (CH20°C=85%), K2HPO4 (CH20°C=92%), KH2PO4 (CH20°C=96.5%), KNO₃ (CH_20°C=93.5%), Na₂SO₄ (CH_20°C=93%), K₂SO₄ (CH_20°C=98%), KHSO₄ (CH_20°C=86%), MgSO₄ (CH_20°C=90%), ZnSO4 (CH20°C=90%) and sodium citrate (CH25°C=86%). Other examples include NaH2PO4, (NH4)H2PO4, CuSO4, Mg(NO3)2 and magnesium acetate. The salt may be in anhydrous form, or it may be a hydrated salt, i.e., a crystalline salt hydrate with bound water(s) of crystallization, such as described in WO 99/32595. Specific examples include anhydrous sodium sulfate (Na2SO4), anhydrous magnesium sulfate (MgSO₄), magnesium sulfate heptahydrate (MgSO₄ ^.7H₂O), zinc sulfate heptahydrate (ZnSO₄ ^.7H₂O), sodium phosphate dibasic heptahydrate (Na₂HPO₄ ^.7H₂O), magnesium nitrate hexahydrate (Mg(NO3)2(6H2O)), sodium citrate dihydrate and magnesium acetate tetrahydrate. Preferably the salt is applied as a solution of the salt, e.g., using a fluid bed. The coating materials can be waxy coating materials and film-forming coating materials. Examples of waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591. The granule may optionally have one or more additional coatings. Examples of suitable coating materials are polyethylene glycol (PEG), methyl hydroxy-propyl cellulose (MHPC) and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are described in WO 93/07263 and WO 97/23606. The core can be prepared by granulating a blend of the ingredients, e.g., by a method comprising granulation techniques such as crystallization, precipitation, pan-coating, fluid bed coating, fluid bed agglomeration, rotary atomization, extrusion, prilling, spheronization, size reduction methods, drum granulation, and/or high shear granulation. Methods for preparing the core can be found in the Handbook of Powder Technology; Particle size enlargement by C. E. Capes; Vol.1; 1980; Elsevier. Preparation methods include known feed and granule formulation technologies, e.g., (a) Spray dried products, wherein a liquid protein-containing solution is atomized in a spray drying tower to form small droplets which during their way down the drying tower dry to form a protein-containing particulate material. Exceedingly small particles can be produced this way (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; Vol.71; pages 140-142; Marcel Dekker). (b) Layered products, wherein the protein is coated as a layer around a pre-formed inert core particle, wherein a protein-containing solution is atomized, typically in a fluid bed apparatus wherein the pre-formed core particles are fluidized, and the protein-containing solution adheres to the core particles and dries up to leave a layer of dry protein on the surface of the core particle. Particles of a desired size can be obtained this way if a useful core particle of the desired size can be found. This type of product is described in, e.g., WO 97/23606. (c) Absorbed core particles, wherein rather than coating the protein as a layer around the core, the protein is absorbed onto and/or into the surface of the core. Such a process is described in WO 97/39116. (d) Extrusion or pelletized products, wherein a protein-containing paste is pressed to pellets or under pressure is extruded through a small opening and cut into particles which are subsequently dried. Such particles usually have a considerable size because of the material in which the extrusion opening is made (usually a plate with bore holes) sets a limit on the allowable pressure drop over the extrusion opening. Also, extremely high extrusion pressures when using a small opening increase heat generation in the protein paste, which is harmful to the protein (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; Vol.71; pages 140-142; Marcel Dekker). (e) Prilled products, wherein a protein-containing powder is suspended in molten wax and the suspension is sprayed, e.g., through a rotating disk atomizer, into a cooling chamber where the droplets quickly solidify (Michael S. Showell (editor); Powdered detergents; Surfactant Science Series; 1998; Vol. 71; pages 140-142; Marcel Dekker). The product obtained is one wherein the protein is uniformly distributed throughout an inert material instead of being concentrated on its surface. US 4,016,040 and US 4,713,245 describe this technique. (f) Mixer granulation products, wherein a protein-containing liquid is added to a dry powder composition of conventional granulating components. The liquid and the powder in a suitable proportion are mixed and as the moisture of the liquid is absorbed in the dry powder, the components of the dry powder will start to adhere and agglomerate and particles will build up, forming granulates comprising the protein. Such a process is described in US 4,106,991, EP 170360, EP 304332, EP 304331, WO 90/09440 and WO 90/09428. In a particular aspect of this process, various high-shear mixers can be used as granulators. Granulates consisting of protein, fillers and binders etc. are mixed with cellulose fibers to reinforce the particles to produce a so-called T-granulate. Reinforced particles are more robust and release less enzymatic dust. (g) Size reduction, wherein the cores are produced by milling or crushing of larger particles, pellets, tablets, briquettes etc. containing the protein. The wanted core particle fraction is obtained by sieving the milled or crushed product. Over and undersized particles can be recycled. Size reduction is described in Martin Rhodes (editor); Principles of Powder Technology; 1990; Chapter 10; John Wiley & Sons. (h) Fluid bed granulation. Fluid bed granulation involves suspending particulates in an air stream and spraying a liquid onto the fluidized particles via nozzles. Particles hit by spray droplets get wetted and become tacky. The tacky particles collide with other particles and adhere to them to form a granule. (i) The cores may be subjected to drying, such as in a fluid bed drier. Other known methods for drying granules in the feed or enzyme industry can be used by the skilled person. The drying preferably takes place at a product temperature of from 25 to 90°C. For some proteins, it is important the cores comprising the protein contain a low amount of water before coating with the salt. If water sensitive proteins are coated with a salt before excessive water is removed, the excessive water will be trapped within the core and may affect the activity of the protein negatively. After drying, the cores preferably contain 0.1-10% w/w water. Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and US 4,661,452 and may optionally be coated by methods known in the art. The granulate may further comprise one or more additional enzymes, e.g., hydrolase, isomerase, ligase, lyase, oxidoreductase, and transferase. The one or more additional enzymes are preferably selected from the group consisting of acetylxylan esterase, acylglycerol lipase, amylase, alpha-amylase, beta-amylase, arabinofuranosidase, cellobiohydrolases, cellulase, feruloyl esterase, galactanase, alpha-galactosidase, beta-galactosidase, beta-glucanase, beta-glucosidase, lysophospholipase, lysozyme, alpha-mannosidase, beta-mannosidase (mannanase), nitrogenase, phosphatase, phospholipase A1, phospholipase A2, phospholipase D, phytase, protease, pullulanase, pectin esterase, triacylglycerol lipase, xylanase, beta-xylosidase or any combination thereof. Each enzyme will then be present in more granules securing a more uniform distribution of the enzymes, and also reduces the physical segregation of different enzymes due to different particle sizes. Methods for producing multi-enzyme co-granulates is disclosed in the ip.com disclosure IPCOM000200739D. Another example of formulation of proteins by the use of co-granulates is disclosed in WO 2013/188331. The present disclosure also relates to protected proteins prepared according to the method(s) disclosed in EP 238216. The present disclosure likewise encompasses liquid formulations comprising one or more proteins of the disclosure. The formulation may comprise one or more stabilizing agents (examples of which include polyols such as propylene glycol or glycerol, sugar or sugar alcohol, lactic acid, reversible protease inhibitor, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid). In some embodiments, filler(s) or carrier material(s) are included to increase the volume of such formulation. Suitable filler or carrier materials include, but are not limited to, various salts of sulfate, carbonate and silicate as well as talc, clay and the like. Suitable filler or carrier materials for liquid formulation include, but are not limited to, water or low molecular weight primary and secondary alcohols including polyols and diols. Examples of such alcohols include, but are not limited to, methanol, ethanol, propanol and isopropanol. In some embodiments, the formulation contain from about 5% to about 90% of such materials. In an aspect, the liquid formulation comprises 20-80% w/w of polyol. In one embodiment, the liquid formulation comprises 0.001-2% w/w preservative. In another embodiment, the disclosure relates to liquid formulations comprising: (A) 0.001-25% w/w of one or more proteins of the present disclosure; (B) 20-80% w/w of polyol; (C) optionally 0.001-2% w/w preservative; and (D) water. In another embodiment, the disclosure relates to liquid formulations comprising: (A) 0.001-25% w/w one or more proteins of the present disclosure; (B) 0.001-2% w/w preservative; (C) optionally 20-80% w/w of polyol; and (D) water. In another embodiment, the liquid formulation comprises one or more formulating agents, such as a formulating agent selected from the group consisting of polyol, sodium chloride, sodium benzoate, potassium sorbate, sodium sulfate, potassium sulfate, magnesium sulfate, sodium thiosulfate, calcium carbonate, sodium citrate, dextrin, glucose, sucrose, sorbitol, lactose, starch, PVA, acetate and phosphate, preferably selected from the group consisting of sodium sulfate, dextrin, cellulose, sodium thiosulfate, kaolin and calcium carbonate. In one embodiment, the polyols is selected from the group consisting of glycerol, sorbitol, propylene glycol (MPG), ethylene glycol, diethylene glycol, triethylene glycol, 1,2- propylene glycol or 1,3-propylene glycol, dipropylene glycol, polyethylene glycol (PEG) having an average molecular weight below about 600 and polypropylene glycol (PPG) having an average molecular weight below about 600, more preferably selected from the group consisting of glycerol, sorbitol and propylene glycol (MPG) or any combination thereof. In another embodiment, the liquid formulation comprises 20-80% polyol (i.e., total amount of polyol), e.g., 25- 75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol. In one embodiment, the liquid formulation comprises 20- 80% polyol, e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol, wherein the polyol is selected from the group consisting of glycerol, sorbitol, propylene glycol (MPG), ethylene glycol, diethylene glycol, triethylene glycol, 1,2-propylene glycol or 1,3-propylene glycol, dipropylene glycol, polyethylene glycol (PEG) having an average molecular weight below about 600 and polypropylene glycol (PPG) having an average molecular weight below about 600. In one embodiment, the liquid formulation comprises 20-80% polyol (i.e., total amount of polyol), e.g., 25-75% polyol, 30-70% polyol, 35-65% polyol, or 40-60% polyol, wherein the polyol is selected from the group consisting of glycerol, sorbitol and propylene glycol (MPG). In another embodiment, the preservative is selected from the group consisting of sodium sorbate, potassium sorbate, sodium benzoate and potassium benzoate or any combination thereof. In one embodiment, the liquid formulation comprises 0.02-1.5% w/w preservative, e.g., 0.05-1% w/w preservative or 0.1-0.5% w/w preservative. In one embodiment, the liquid formulation comprises 0.001-2% w/w preservative (i.e., total amount of preservative), e.g., 0.02-1.5% w/w preservative, 0.05-1% w/w preservative, or 0.1-0.5% w/w preservative, wherein the preservative is selected from the group consisting of sodium sorbate, potassium sorbate, sodium benzoate and potassium benzoate or any combination thereof. It is to be understood that formulations of the present disclosure may comprise combinations of enzymes, including, but not limited to combinations of enzymes expressly disclosed herein and combinations with enzymes that are not expressly disclosed herein. In some embodiments, formulations of the present disclosure comprise 2, 3, 4, 5, 6, 7, 8, 9, 10 or more proteins of the present disclosure. For example, in some embodiments, formulations of the present disclosure comprise 2, 3, 4, 5, 6, 7, 8, 9, 10 or more of the polypeptides set forth herein as SEQ ID NO(s): 1–3, 7–19, 21–35, 37–46, 48–50, 52–107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162–177, 179–253, 255–261, 263–271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416–480 or a functional fragment/mutant/variant thereof. In some embodiments, formulations of the present disclosure comprise two or more distinct phosphatases and/or phytases. In some embodiments, formulations of the present disclosure comprise at least one phosphatase (e.g., an acid phosphatase belonging to EC 3.1.3.2 or a functional fragment/mutant/variant thereof) and at least one phytase (e.g., any one of SEQ ID NOs: 1–3, 7–19, 21–35, 37–46, 48–50, 52–107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162–177, 179–253, 255–261, 263–271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416–480 or a functional fragment/mutant/variant thereof). In some embodiments, formulations of the present disclosure comprise a fermentation broth that comprises 2, 3, 4, 5, 6, 7, 8, 9, 10 or more enzymes. In some embodiments, formulations of the present disclosure comprise a fermentation broth that comprises 2, 3, 4, 5, 6, 7, 8, 9, 10 or more proteins of the present disclosure (2, 3, 4, 5, 6, 7, 8, 9, 10 or more of SEQ ID NOs: 1–3, 7–19, 21–35, 37–46, 48–50, 52–107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162–177, 179–253, 255–261, 263–271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416–480 or functional fragments/mutants/variants thereof). Formulations of the present disclosure may comprise myriad components, including, but not limited to, adhesives, anti-freezing agents, anti-settling agents, biostimulants, chemical actives, dispersants, drying agents, effect pigments, emulsifiers, growth media, microbial extracts, nutrients, pest attractants and feeding stimulants, pH control components, plant-beneficial microorganisms, plant signal molecules, preservatives, rain fasteners, rhealogical agents, safeners, seed flowability agents, stabilizing agents, UV protectants and wetting agents. Examples of adhesives that may be included in formulations of the present disclosure include, but not are not limited to, acrylics (e.g., polyvinyl acetate copolymer emulsions, polyvinyl chloride acrylic copolymer emulsions), disaccharides (e.g. maltose, sucrose, trehalose), gums (e.g., cellulose gum, guar gum, gum arabic, gum combretum, xantham gum), maltodextrins (e.g., maltodextrins (each and/or collectively) having a DEV of about 10 to about 20), microcapsules (e.g., polydopamine microcapsules), monosaccharides, nanocomposites (e.g., mesoporous silica nanoparticles), oils (e.g., mineral oil, olive oil, peanut oil, soybean oil and/or sunflower oil), oligosaccharides, polysaccharides, sol-gel polymers, and combinations thereof. See generally, e.g., POWERBLOX™ (Dow, Midland, MI, USA), such as POWERBLOX™ ADJ-65 and POWERBLOX™ ADJ-65; EP 0245970; US 5,496,568; WO 2008/144024; WO 2009/135049; WO 2011/126832; WO 2017/083049; WO 2020/225276; WO 2021/055316; WO 2022/096688; WO 2022/096691; WO 2022/096692; WO 2022/096693; WO 2022/096694; WO 2022/096695; WO 2022/096696. Examples of suitable anti-freezing agents include, but not are not limited to, ethylene glycol, glycerin, propylene glycol, urea, and combinations thereof. Examples of suitable anti-settling agents include, but not are not limited to, polyvinyl acetate, polyvinyl alcohols with different degrees of hydrolysis, polyvinylpyrrolidones, polyacrylates, acrylate-, polyol- or polyester-based paint system binders which are soluble or dispersible in water, moreover copolymers of two or more monomers such as acrylic acid, methacrylic acid, itaconic acid, maleic acid, fumaric acid, maleic anhydride, vinylpyrrolidone, ethylenically unsaturated monomers such as ethylene, butadiene, isoprene, chloroprene, styrene, divinylbenzene, ot-methylstyrene or p-methylstyrene, further vinyl halides such as vinyl chloride and vinylidene chloride, additionally vinyl esters such as vinyl acetate, vinyl propionate or vinyl stearate, moreover vinyl methyl ketone or esters of acrylic acid or methacrylic acid with monohydric alcohols or polyols such as methyl acrylate, methyl methacrylate, ethyl acrylate, ethylene methacrylate, lauryl acrylate, lauryl methacrylate, decyl acrylate, N,N-dimethylamino-ethyl methacrylate, 2-hydroxyethyl methacrylate, 2-hydroxypropyl methacrylate or glycidyl methacrylate, furthermore diethyl esters or monoesters of unsaturated dicarboxylic acids, furthermore (meth)acrylamido-N-methylol methyl ether, amides or nitriles such as acrylamide, methacrylamide, N- methylol(meth)acrylamide, acrylonitrile, methacrylonitrile, and also N-substituted maleiraides and ethers such as vinyl butyl ether, vinyl isobutyl ether or vinyl phenyl ether, and combinations thereof. Examples of suitable biostimulants include, but not are not limited to, alginates, carrageenans, chitosans, fulvic acids, glycine, humic acids, humins, inorganic compounds, laminarins, protein hydrosylates, seaweed extracts (e.g., Ascophyllum nodosum extracts, Ecklonia maxima extracts, etc.), and combinations thereof. See generally, e.g., Rouphael and Colla, Editorial: Biostimulants in Agriculture, FRONT. PLANT SCI.11 (2020), CN 114190406, US 2012/0129695, US 2022/0009851, US 2024/0298650, WO 2022/023389, WO 2023/214389, WO 2023/286928, WO 2024/201362, WO 2024/218232, WO 2024/234111, WO 2025/017538. In some embodiments, formulations of the present disclosure comprise one or more humic acids (e.g., one or more leonardite humic acids, lignite humic acids, peat humic acids and water-extracted humic acids). In some embodiments, formulations of the present disclosure comprise ammonium humate, boron humate, potassium humate and/or sodium humate. In some embodiments, one or more of ammonium humate, boron humate, potassium humate and sodium humate is/are excluded from formulations of the present disclosure. Nonlimiting examples of humic acids that may be useful in embodiments of the present disclosure include MDL Number MFCD00147177 (CAS Number 1415-93-6), MDL Number MFCD00135560 (CAS Number 68131-04-4), MDL Number MFCS22495372 (CAS Number 68514-28-3), CAS Number 93924-35-7, and CAS Number 308067-45-0. In some embodiments, formulations of the present disclosure comprise one or more fulvic acids (e.g., one or more leonardite fulvic acids, lignite fulvic acids, peat fulvic acids and/or water-extracted fulvic acids). In some embodiments, formulations of the present disclosure comprise ammonium fulvate, boron fulvate, potassium fulvate and/or sodium fulvate. In some embodiments, one or more of ammonium fulvate, boron fulvate, potassium fulvate and sodium fulvate is/are excluded from formulations of the present disclosure. Nonlimiting examples of fulvic acids that may be useful in embodiments of the present disclosure include MDL Number MFCD09838488 (CAS Number 479-66-3). Examples of chemical actives that may be included in formulations of the present disclosure include, but not are not limited to, acaracides and miticides (e.g., carvacrol, sanguinarine, azobenzene, benzoximate, benzyl benzoate, bromopropylate, chlorbenside, chlorfenethol, chlorfenson, chlorfensulphide, chlorobenzilate, chloropropylate, cyflumetofen, DDT, dicofol, diphenyl sulfone, dofenapyn, fenson, fentrifanil, fluorbenside, genit, hexachlorophene, phenproxide, proclonol, tetradifon, tetrasul, benomyl, carbanolate, carbaryl, carbofuran, methiocarb, metolcarb, promacyl, propoxur, aldicarb, butocarboxim, oxamyl, thiocarboxime, thiofanox, bifenazate, binapacryl, dinex, dinobuton, dinocap-4, dinocap-6, dinocton, dinopenton, dinosulfon, dinoterbon, DNOC, amitraz, chlordimeform, chloromebuform, formetanate, formparanate, medimeform, semiamitraz, afoxolaner, fluralaner, sarolaner, tetranactin ◦avermectin acaricides, abamectin, doramectin, eprinomectin, ivermectin, selamectin, milbemectin, milbemycin oxime, moxidectin,, clofentezine, cyromazine, diflovidazin, dofenapyn, fluazuron, flubenzimine, flucycloxuron, flufenoxuron, hexythiazox, bromocyclen, camphechlor, DDT, dienochlor, endosulfan, lindane, chlorfenvinphos, crotoxyphos, dichlorvos, heptenophos, mevinphos, monocrotophos, naled, TEPP, tetrachlorvinphos, amidithion, amiton, azinphos-ethyl, azinphos-methyl, azothoate, benoxafos, bromophos, bromophos-ethyl, carbophenothion, chlorpyrifos, chlorthiophos, coumaphos, cyanthoate, demeton-O, demeton-S, demeton- O-methyl, demeton-S-methyl, demeton-S-methylsulphon, dialifos, diazinon, dimethoate, dioxathion, disulfoton, endothion, ethion, ethoate-methyl, formothion, malathion, mecarbam, methacrifos, omethoate, oxydeprofos, oxydisulfoton, parathion, phenkapton, phorate, phosalone, phosmet, phostin, phoxim, pirimiphos-methyl, prothidathion, prothoate, pyrimitate, quinalphos, quintiofos, sophamide, sulfotep, thiometon, triazophos, trifenofos, vamidothion, trichlorfon, isocarbophos, methamidophos, propetamphos, dimefox, mipafox, schradan,, azocyclotin, cyhexatin, fenbutatin oxide, phostin, dichlofluanid, dialifos, phosmet, cyenopyrafen, fenpyroximate, pyflubumide, tebufenpyrad, acetoprole, fipronil, vaniliprole,, acrinathrin, bifenthrin, brofluthrinate, cyhalothrin, alpha-cypermethrin, fenpropathrin, fenvalerate, flucythrinate, flumethrin, tau-fluvalinate, permethrin, halfenprox,, pyrimidifen, chlorfenapyr, sanguinarine, chinomethionat, thioquinox, bifujunzhi, fluacrypyrim, flufenoxystrobin, pyriminostrobin,, aramite, propargite, spirodiclofen, clofentezine, diflovidazin, flubenzimine, hexythiazox, fenothiocarb, chloromethiuron, diafenthiuron, acequinocyl, amidoflumet, arsenous oxide, clenpirin, closantel, crotamiton, cycloprate, cymiazole, disulfiram, etoxazole, fenazaflor, fenazaquin, fluenetil, mesulfen, MNAF, nifluridide, nikkomycins, pyridaben, sulfiram, sulfluramid, sulfur, thuringiensin, triarathene, and combinations thereof); fungicides (e.g., strobilurins, such as azoxystrobin, coumethoxystrobin, coumoxystrobin, dimoxystrobin, enestroburin, fluoxastrobin, kresoxim-methyl, metominostrobin, orysastrobin, picoxystrobin, pyraclostrobin, pyrametostrobin, pyraoxystrobin, pyribencarb, trifloxystrobin, 2-[2-(2,5-dimethyl-phenoxymethyl)- phenyl]-3-methoxy-acrylic acid methyl ester and 2-(2-(3-(2,6-dichlorophenyl)-1-methyl-allylideneaminooxymethyl)- phenyl)-2-methoxyimino-N-methyl-acetamide; carboxamides, such as carboxanilides (e.g., benalaxyl, benalaxyl-M, benodanil, bixafen, boscalid, carboxin, fenfuram, fenhexamid, flutolanil, fluxapyroxad, furametpyr, isopyrazam, isotianil, kiralaxyl, mepronil, metalaxyl, metalaxyl-M (mefenoxam), ofurace, oxadixyl, oxycarboxin, penflufen, penthiopyrad, sedaxane, tecloftalam, thifluzamide, tiadinil, 2-amino-4-methyl-thiazole-5-carboxanilide, N-(4'- trifluoromethylthiobiphenyl-2-yl)-3-difluoromethyl-1-methyl-1H-pyra- zole-4-carboxamide, N-(2-(1,3,3-trimethylbutyl)- phenyl)-1,3-dimethyl-5-fluoro-1H-pyrazole-4-carboxamide), carboxylic morpholides (e.g., dimethomorph, flumorph, pyrimorph), benzoic acid amides (e.g., flumetover, fluopicolide, fluopyram, zoxamide), carpropamid, dicyclomet, mandiproamid, oxytetracyclin, silthiofam and N-(6-methoxy-pyridin-3-yl) cyclopropanecarboxylic acid amide; azoles, such as triazoles (e.g., azaconazole, bitertanol, bromuconazole, cyproconazole, difenoconazole, diniconazole, diniconazole-M, epoxiconazole, fenbuconazole, fluquinconazole, flusilazole, flutriafol, hexaconazole, imibenconazole, ipconazole, metconazole, myclobutanil, oxpoconazole, paclobutrazole, penconazole, propiconazole, prothioconazole, simeconazole, tebuconazole, tetraconazole, triadimefon, triadimenol, triticonazole, uniconazole) and imidazoles (e.g., cyazofamid, imazalil, pefurazoate, prochloraz, triflumizol); heterocyclic compounds, such as pyridines (e.g., fluazinam, pyrifenox (cf.D1b), 3-[5-(4-chloro-phenyl)-2,3-dimethyl-isoxazolidin-3-yl]-pyridine, 3-[5-(4-methyl-phenyl)-2,3-dimethyl- isoxazolidin-3-yl]-pyridine), pyrimidines (e.g., bupirimate, cyprodinil, diflumetorim, fenarimol, ferimzone, mepanipyrim, nitrapyrin, nuarimol, pyrimethanil), piperazines (e.g., triforine), pirroles (e.g., fenpiclonil, fludioxonil), morpholines (e.g., aldimorph, dodemorph, dodemorph-acetate, fenpropimorph, tridemorph), piperidines (e.g., fenpropidin), dicarboximides (e.g., fluoroimid, iprodione, procymidone, vinclozolin), non-aromatic 5-membered heterocycles (e.g., famoxadone, fenamidone, flutianil, octhilinone, probenazole, 5-amino-2-isopropyl-3-oxo-4-ortho-tolyl-2,3-dihydro-pyrazole-1- carbothioic acid S-allyl ester), acibenzolar-S-methyl, ametoctradin, amisulbrom, anilazin, blasticidin-S, captafol, captan, chinomethionat, dazomet, debacarb, diclomezine, difenzoquat, difenzoquat-methylsulfate, fenoxanil, Folpet, oxolinic acid, piperalin, proquinazid, pyroquilon, quinoxyfen, triazoxide, tricyclazole, 2-butoxy-6-iodo-3-propylchromen-4-one, 5- chloro-1-(4,6-dimethoxy-pyrimidin-2-yl)-2-methyl-1H-benzoimidazole and 5-chloro-7-(4-methylpiperidin-1-yl)-6-(2,4,6- trifluorophenyl)-[1,2,4]triazolo-[1,5-a]pyrimidine; benzimidazoles, such as carbendazim; and other active substances, such as guanidines (e.g., guanidine, dodine, dodine free base, guazatine, guazatine-acetate, iminoctadine), iminoctadine-triacetate and iminoctadine-tris(albesilate); antibiotics (e.g., kasugamycin, kasugamycin hydrochloride-hydrate, streptomycin, polyoxine and validamycin A); nitrophenyl derivates (e.g., binapacryl, dicloran, dinobuton, dinocap, nitrothal-isopropyl, tecnazen); organometal compounds (e.g., fentin salts, such as fentin-acetate, fentin chloride, fentin hydroxide); sulfur- containing heterocyclyl compounds (e.g., dithianon, isoprothiolane); organophosphorus compounds (e.g., edifenphos, fosetyl, fosetyl-aluminum, iprobenfos, phosphorus acid and its salts, pyrazophos, tolclofos-methyl); organochlorine compounds (e.g., chlorothalonil, dichlofluanid, dichlorophen, flusulfamide, hexachlorobenzene, pencycuron, pentachlorphenole and its salts, phthalide, quintozene, thiophanate-methyl, thiophanate, tolylfluanid, N-(4-chloro-2-nitro- phenyl)-N-ethyl-4-methyl-benzenesulfonamide), inorganic active substances (e.g., Bordeaux mixture, copper acetate, copper hydroxide, copper oxychloride, basic copper sulfate, phosphite salt, sulfur, zinc sulfate), natamycin, and combinations thereof); gastropodicides (e.g., methiocarb, metaldehyde, carbaryl, spinosad, copper sulfate in combination with lime, boric acid, iron phosphate, and combinations thereof); herbicides (e.g., 2,4-dichlorophenoxyacetic acid (2,4-D), 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), ametryn, amicarbazone, aminocyclopyrachlor, acetochlor, acifluorfen, alachlor, atrazine, azafenidin, bentazon, benzofenap, bifenox, bromacil, bromoxynil, butachlor, butafenacil, butroxydim, carfentrazone-ethyl, chlorimuron, chlorotoluro, clethodim, clodinafop, clomazone, cyanazine, cycloxydim, cyhalofop, desmedipham, desmetryn, dicamba, diclofop, dimefuron, diuron, dithiopyr, fenoxaprop, fluazifop, fluazifop-P, fluometuron, flufenpyr-ethyl, flumiclorac-pentyl, flumioxazin, fluoroglycofen, fluthiacet- methyl, fomesafe, fomesafen, glyphosate, glufosinate, haloxyfop, hexazinone, imazamox, imazaquin, imazethapyr, ioxynil, isoproturon, isoxaflutole, lactofen, linuron, mecoprop, mecoprop-P, mesotrion, metamitron, metazochlor, methibenzuron, metolachlor (and S-metolachlor ), metoxuron, metribuzin, monolinuron, oxadiargyl, oxadiazon, oxyfluorfen, phenmedipham, pretilachlor, profoxydim, prometon, prometry, propachlor, propanil, propaquizafop, propisochlor, pyraflufen-ethyl, pyrazon, pyrazolynate, pyrazoxyfen, pyridate, quizalofop, quizalofop-P (e.g., quizalofop-ethyl, quizalofop-P-ethyl, clodinafop-propargyl, cyhalofop-butyl, diclofop- methyl, fenoxaprop-P-ethyl, fluazifop-P-butyl, haloxyfop-methyl, haloxyfop-R-methyl), saflufenacil, sethoxydim, siduron, simazine, simetryn, sulcotrione, sulfentrazone, tebuthiuron, tembotrione, tepraloxydim, terbacil, terbumeton, terbuthylazine, thaxtomin (e.g., the thaxtomins described in US Patent No.7,989,393), thenylchlor, tralkoxydim, triclopyr, trietazine, tropramezone, salts and esters thereof; racemic mixtures and resolved isomers thereof and combinations thereof); and insecticides and nematicides (e.g., antibiotic insecticides such as allosamidin and thuringiensin; macrocyclic lactone insecticides such as spinosad, spinetoram, and other spinosyns including the 21-butenyl spinosyns and their derivatives; avermectin insecticides such as abamectin, doramectin, emamectin, eprinomectin, ivermectin and selamectin; milbemycin insecticides such as lepimectin, milbemectin, milbemycin oxime and moxidectin; arsenical insecticides such as calcium arsenate, copper acetoarsenite, copper arsenate, lead arsenate, potassium arsenite and sodium arsenite; other biological insecticides, plant incorporated protectant insecticides such as Cry1Ab, Cry1Ac, Cry1F, Cry1A.105, Cry2Ab2, Cry3A, mir Cry3A, Cry3Bb1, Cry34, Cry35, and VIP3A; botanical insecticides such as anabasine, azadirachtin, d-limonene, nicotine, pyrethrins, cinerins, cinerin I, cinerin II, jasmolin I, jasmolin II, pyrethrin I, pyrethrin II, quassia, rotenone, ryania and sabadilla; carbamate insecticides such as bendiocarb and carbaryl; benzofuranyl methylcarbamate insecticides such as benfuracarb, carbofuran, carbosulfan, decarbofuran and furathiocarb; dimethylcarbamate insecticides dimitan, dimetilan, hyquincarb and pirimicarb; oxime carbamate insecticides such as alanycarb, aldicarb, aldoxycarb, butocarboxim, butoxycarboxim, methomyl, nitrilacarb, oxamyl, tazimcarb, thiocarboxime, thiodicarb and thiofanox; phenyl methylcarbamate insecticides such as allyxycarb, aminocarb, bufencarb, butacarb, carbanolate, cloethocarb, dicresyl, dioxacarb, EMPC, ethiofencarb, fenethacarb, fenobucarb, isoprocarb, methiocarb, metolcarb, mexacarbate, promacyl, promecarb, propoxur, trimethacarb, XMC and xylylcarb; dinitrophenol insecticides such as dinex, dinoprop, dinosam and DNOC; fluorine insecticides such as barium hexafluorosilicate, cryolite, sodium fluoride, sodium hexafluorosilicate and sulfluramid; formamidine insecticides such as amitraz, chlordimeform, formetanate and formparanate; fumigant insecticides such as acrylonitrile, carbon disulfide, carbon tetrachloride, chloroform, chloropicrin, para-dichlorobenzene, 1,2-dichloropropane, ethyl formate, ethylene dibromide, ethylene dichloride, ethylene oxide, hydrogen cyanide, iodomethane, methyl bromide, methylchloroform, methylene chloride, naphthalene, phosphine, sulfuryl fluoride and tetrachloroethane; inorganic insecticides such as borax, calcium polysulfide, copper oleate, mercurous chloride, potassium thiocyanate and sodium thiocyanate; chitin synthesis inhibitors such as bistrifluoron, buprofezin, chlorfluazuron, cyromazine, diflubenzuron, flucycloxuron, flufenoxuron, hexaflumuron, lufenuron, novaluron, noviflumuron, penfluoron, teflubenzuron and triflumuron; juvenile hormone mimics such as epofenonane, fenoxycarb, hydroprene, kinoprene, methoprene, pyriproxyfen and triprene; juvenile hormones such as juvenile hormone I, juvenile hormone II and juvenile hormone III; moulting hormone agonists such as chromafenozide, halofenozide, methoxyfenozide and tebufenozide; moulting hormones such as .alpha.-ecdysone and ecdysterone; moulting inhibitors such as diofenolan; precocenes such as precocene I, precocene II and precocene III; unclassified insect growth regulators such as dicyclanil; nereistoxin analogue insecticides such as bensultap, cartap, thiocyclam and thiosultap; nicotinoid insecticides such as flonicamid; nitroguanidine insecticides such as clothianidin, dinotefuran, imidacloprid and thiamethoxam; nitromethylene insecticides such as nitenpyram and nithiazine; pyridylmethylamine insecticides such as acetamiprid, imidacloprid, nitenpyram and thiacloprid; organochlorine insecticides such as bromo-DDT, camphechlor, DDT, pp'-DDT, ethyl-DDD, HCH, gamma-HCH, lindane, methoxychlor, pentachlorophenol and TDE; cyclodiene insecticides such as aldrin, bromocyclen, chlorbicyclen, chlordane, chlordecone, dieldrin, dilor, endosulfan, endrin, HEOD, heptachlor, HHDN, isobenzan, isodrin, kelevan and mirex; organophosphate insecticides such as bromfenvinfos, chlorfenvinphos, crotoxyphos, dichlorvos, dicrotophos, dimethylvinphos, fospirate, heptenophos, methocrotophos, mevinphos, monocrotophos, naled, naftalofos, phosphamidon, propaphos, TEPP and tetrachlorvinphos; organothiophosphate insecticides such as dioxabenzofos, fosmethilan and phenthoate; aliphatic organothiophosphate insecticides such as acethion, amiton, cadusafos, chlorethoxyfos, chlormephos, demephion, demephion-O, demephion-S, demeton, demeton-O, demeton-S, demeton-methyl, demeton-O-methyl, demeton- S-methyl, demeton-S-methylsulphon, disulfoton, ethion, ethoprophos, IPSP, isothioate, malathion, methacrifos, oxydemeton-methyl, oxydeprofos, oxydisulfoton, phorate, sulfotep, terbufos and thiometon; aliphatic amide organothiophosphate insecticides such as amidithion, cyanthoate, dimethoate, ethoate-methyl, formothion, mecarbam, omethoate, prothoate, sophamide and vamidothion; oxime organothiophosphate insecticides such as chlorphoxim, phoxim and phoxim-methyl; heterocyclic organothiophosphate insecticides such as azamethiphos, coumaphos, coumithoate, dioxathion, endothion, menazon, morphothion, phosalone, pyraclofos, pyridaphenthion and quinothion; benzothiopyran organothiophosphate insecticides such as dithicrofos and thicrofos; benzotriazine organothiophosphate insecticides such as azinphos-ethyl and azinphos-methyl; isoindole organothiophosphate insecticides such as dialifos and phosmet; isoxazole organothiophosphate insecticides such as isoxathion and zolaprofos; pyrazolopyrimidine organothiophosphate insecticides such as chlorprazophos and pyrazophos; pyridine organothiophosphate insecticides such as chlorpyrifos and chlorpyrifos- methyl; pyrimidine organothiophosphate insecticides such as butathiofos, diazinon, etrimfos, lirimfos, pirimiphos-ethyl, pirimiphos-methyl, primidophos, pyrimitate and tebupirimfos; quinoxaline organothiophosphate insecticides such as quinalphos and quinalphos-methyl; thiadiazole organothiophosphate insecticides such as athidathion, lythidathion, methidathion and prothidathion; triazole organothiophosphate insecticides such as isazofos and triazophos; phenyl organothiophosphate insecticides such as azothoate, bromophos, bromophos-ethyl, carbophenothion, chlorthiophos, cyanophos, cythioate, dicapthon, dichlofenthion, etaphos, famphur, fenchlorphos, fenitrothion fensulfothion, fenthion, fenthion-ethyl, heterophos, jodfenphos, mesulfenfos, parathion, parathion-methyl, phenkapton, phosnichlor, profenofos, prothiofos, sulprofos, temephos, trichlormetaphos-3 and trifenofos; phosphonate insecticides such as butonate and trichlorfon; phosphonothioate insecticides such as mecarphon; phenyl ethylphosphonothioate insecticides such as fonofos and trichloronat; phenyl phenylphosphonothioate insecticides such as cyanofenphos, EPN and leptophos; phosphoramidate insecticides such as crufomate, fenamiphos, fosthietan, imicyafos, mephosfolan, phosfolan and pirimetaphos; phosphoramidothioate insecticides such as acephate, isocarbophos, isofenphos, methamidophos and propetamphos; phosphorodiamide insecticides such as dimefox, mazidox, mipafox and schradan; oxadiazine insecticides such as indoxacarb; phthalimide insecticides such as dialifos, phosmet and tetramethrin; pyrazole insecticides such as acetoprole, ethiprole, fipronil, pyrafluprole, pyriprole, tebufenpyrad, tolfenpyrad and vaniliprole; pyrethroid ester insecticides such as acrinathrin, allethrin, bioallethrin, barthrin, bifenthrin, bioethanomethrin, cyclethrin, cycloprothrin, cyfluthrin, beta- cyfluthrin, cyhalothrin, gamma-cyhalothrin, lambda-cyhalothrin, cypermethrin, alpha-cypermethrin, beta-cypermethrin, theta-cypermethrin, zeta-cypermethrin, cyphenothrin, deltamethrin, dimefluthrin, dimethrin, empenthrin, fenfluthrin, fenpirithrin, fenpropathrin, fenvalerate, esfenvalerate, flucythrinate, fluvalinate, tau-fluvalinate, furethrin, imiprothrin, metofluthrin, permethrin, biopermethrin, transpermethrin, phenothrin, prallethrin, profluthrin, pyresmethrin, resmethrin, biopermethrin, cismethrin, tefluthrin, terallethrin, tetramethrin, tralomethrin and transfluthrin; pyrethroid ether insecticides such as etofenprox, flufenprox, halfenprox, protrifenbute and silafluofen; pyrimidinamine insecticides such as flufenerim and pyrimidifen; pyrrole insecticides such as chlorfenapyr; tetronic acid insecticides such as spirodiclofen, spiromesifen and spirotetramat; thiourea insecticides such as diafenthiuron; urea insecticides such as flucofuron and sulcofuron; and unclassified insecticides such as AKD-3088, chlorantraniliprole, closantel, crotamiton, cyflumetofen, E2Y45, EXD, fenazaflor, fenazaquin, fenoxacrim, fenpyroximate, FKI-1033, flubendiamide, HGW86, hydramethylnon, IKI-2002, isoprothiolane, malonoben, metaflumizone, metoxadiazone, nifluridide, NNI-9850, NNI-0101, pymetrozine, pyridaben, pyridalyl, pyrifluquinazon, Qcide, rafoxanide, Rynaxypyr.TM., SYJ-159, triarathene and triazamate, and combinations thereof). Non-limiting examples of commercially available chemical actives include products sold under the tradenames ABACUS®, ACROBAT®, ACRONIS®, ADHERE®, ADMIRAL®, AGCELENCE®, AGMUSA®, ALLEGRO®, ALITE 27®, ALTREVIN®, AMP®, AMPLEXUS®, AMPLO®, ARMEZON®, ARESENAL®, ASSIST®, ATECTRA®, ATIVUM®, AUMENAX®, AURA®, BASAGRAN®, BELLIS®, BEYOND®, BLAVITY®, BLITZ®, BOMVORO®, BRIO®, CABRIO®, CARAMBA®, CADRE®, CANTUS®, CAPACITY®, CARAMBA®, CAURIFIX®, CEPTIVA®, CEYVA®, CHOPPER®, CLARITY®, CLEARFIELD®, CLEARPATH®, CLEARSOL®, COLLIS®, COMET®, CONTAIN®, CONVEY®, COPEO®, CREDENZ®, CUPRODUL®, CYCOCEL®, DASH®, DELAN®, DISTINCT®, DORMEX®, DUETT®, DURAVEL®, ENDURA®, ENGENIA®, ENTIGRIS®, EXTREME®, F 500®, FACET®, FASTAC®, FENDONA®, FIBERMAX®, FINALE®, FORUM®, GELFIX®, GESTUS®, GLYTOL®, GRANOURO®, GREEN LAWNGER®, HEADLINE®, HEAT®, HERBADOX®, HI-LIGHT®, HICOAT®, HIDROCUP®, HISTICK®, ILEVO®, IMUNIT®, INITIUM®, INTERFIELD®, KIFIX®, KIXOR®, KUMULUS®, LACTOSILO®, LAWNGER®, LIBERTY®, LIBERTYLINK®, LIDERO®, LUPRO-GRAIN®, MEES®, MERIVON®, MUNEO®, NEALTA®, NEPAXIR®, NEWPATH®, NEXICOR®, NODULATOR®, NOMOLT®, OBVIUS®, ONDUTY®, ONLY®, OPERA®, OPTILL®, ORKESTRA®, ORQUESTA®, OUTLOOK®, PENDULUM®, PIRATE®, PIVOT®, PIX®, PLATEAU®, POAST®, POLYACER®, POLYRAM®, PONCHO®, PREMIS®, PRIAXOR®, PRISTINE®, PROVISIA®, PROVYSOL®, PROWL®, PURSUTI®, RAK®, RAPTOR®, REGENT®, RELENYA®, RELY®, RENESTRA®, REVYSOL®, REVYTEK®, RHIZO-FLO®, SEFINA®, SELTIMA®, SEPIRET®, SERIFEL®, SHARPEN®, SISTEMA®, SISTIVA®, SOYTECH®, SPHAEREX®, SPOT®, STAMINA®, STANDAK®, STATUS®, STORM®, STROBY®, SUNFIRE®, SYSTIVA®, TACAZO®, TAJ®, TERAXXA®, TREEVIX®, TUIT®, TUTOR®, TWINLINK®, VABORO®, VALEOS®, VARISTO®, VAULT®, VELTYMA®, VERDICT®, VERISMO®, VERSATILIS®, VERSYS®, VIVANDO®, VOTIVO®, XANTHION®, XEMIUM®, ZAMPOR®, ZIDUA® and ZYNION® from BASF (Ludwigshafen, Germany); CORVUS®, POWERMAX®, DELARO®, PROSARO®, BAYTHROID®, SIVANTO®, FINISH®, GINSTAR®, ACCELERON®, RAXIL®, AERIS®, EVERGOL®, TRILEX®, ALLEGIANCE®, BUTEO, EMESTO®, GAUCHO® and THIRAM® from Bayer Crop Science (Creve Coeur, MO, USA); AGREE®, AGRIPHAGE™, AGSIL®, ANCORA, AZATIN®, BOTANIGARD®, BOTEGHA®, BUG-N-SLUGGO®, CARB-O-NATOR®, CRYMAX®, CUEVA®, CYD-X®, DEFGUARD®, DELIVER®, DES-X®, DOUBLE NICKEL®, FIREFIGHTER™, GEMSTAR®, GROTTO®, HOMEPLATE®, JAVELIN®, KALMOR®, KOCIDE®, LIFEGARD®, MADEX®, MELOCON®, MYCOTROL®, NEEMIX®, OSO™, PFR-97™, SEDUCE™, SIL-MATRIX®, SLUGGO®, SOILGARD®, THURICIDE®, TRIACT®, TRIATHLON® and TRILOGY® from Certis (Columbia, MD); ABUNDIT®, ACCENT®, AFFORIA®, APROACH®, BASIS®, BEXFOND®, BLACKHAWK®, CANOPY®, CINCH®, CLINHER®, CURTAIL®, CURZATE®, DELEGATE®, RAINSHIELD®, DITHANE®, FEXAPAN®, VAPORGRIP®, LANNATE®, TANOS®, DURANGO®, DMA®, ELEVORE®, EMBED®, ENABLE®, ENLIST DUO®, ENLIST ONE®, ENLITE®, ENTRUST®, ENVIVE®, EVERPLEX®, FONTELIS®, FULTIME®, GOLDSKY®, GRANDSTAND®, GRANITE®, GRASP®, HEARKEN®, INDAR®, NXTGEN®, INSTINCT®, INTREPID 2F®, INTREPID EDGE®, KERB®, KEYSTONE®, KYBER®, LEADOFF®, LOYANT®, MATRIX®, N-SERVE®, NOVIXID®, OPENSKY®, PERFECTMATCH®, PINDAR®, PIXXARO®, POWERFLEX®, QUELEX®, RADIANT®, RALLY®, REALM®, REBELEX®, RESICORE®, RESOLVE®, REVULIN®, REZUVANT®, RIDGEBACK®, SEQUOIA®, SIMPLICITY®, SONIC®, STARANE®, STEADFAST®, STINGER®, STRONGARM®, SUCCESS®, SURESTART®, SURPASS®, SURVEIL®, SYNCHRONY®, TARZEC®, TRANSFORM®, TRELLIS®, TRIVENCE®, UTRISHA®, VERTISAN®, VYDATE®, WIDEARMATCH®, WIDEMATCH® and ZEST® from Corteva Agroscience (Indianapolis, IN, USA); BIO- SAVE® from Decco U.S. Post-Harvest, Inc. (Monrovia, CA, USA); ACCUDO®, AFFINITY®, AGILITY®, AIM®, ALLY®, ALTACOR®, ANTHEM®, ATHENA®, AUTHORITY®, AVAUNT®, BELEAF®, BRIGADE®, CADET®, CAPTURE®, CARBINE®, COMMAND®, CORAGEN®, DISPLAY®, ELEVEST®, ETHOS®, EXIREL®, EXPRESS®, FINESSE®, FIRSTSHOT®, FURAGRO®, GLADIATOR®, HARMONY®, HERO®, LUCENTO®, MARVEL®, MUSTANG®, OBEY®, PANOFLEX®, PRESENCE®, PREVATHON®, QUARTZO®, RHYME®, ROVRAL®, SEAMAC®, SHARK®, SOLIDA®, SPARTAN®, STEWARD®, TEMITRY®, TERRA®, TOPGUARD®, UPBEET®, VANTACOR®, VERIMARK®, XYWAY®, ZEUS® and ZIRONAR® from FMC Corporation (Philadelphia, PA, USA); PENTIA®, ABAMEX®, AGRI TIN®, CHAMP®, CHIPTOX®, GIN OUT®, KAISO®, MEPEX®, NUPRID®, RAPPORT®, TERMINATE®, THISTROL®, ULTRA FLOURISH®, GOAL®, GOALTENDER®, GRAPPLE®, TUSCANY®, CHAMPION++, AGRI-MYCIN®, PHOSTROL®, BLIGHTBAN®, CHEETAH®, MYCOSHIELD®, RITEWAY®, TAZER®, MYSTIC®, CUPROXAT® and TYPY® from Nufarm Limited (Victoria, Australia); BIOSPECTRA®, PACRITE®, EFOG®, SHIELD-BRITE®, FUNGAFLOR®, PENBOTEC, and SOPP from Pace International (Wapato, WA, USA); ACTARA®, ACTELLIC®, ACTIGARD®, ACURON™, ADVION®, AFLAGUARD®, AGRIPRO®, ALTO®, ALUMNI®, AMISTAR®, APIRO®, APRON®, AVICTA®, AWARD®, AXIAL™, AXORIS®, BANNER®, BANVEL®, BARRICADE®, BEACON®, BICEP II MAGNUM®, BION®, BONZI®, BOUNDARY®, BOXER®, BRAVO®, C. C. BENOIST®, CADENCE®, CALARIS®, CALLISTO®, CAMIX®, CAPTORA®, CASPER®, CELEST®, CHAIRMAN®, CHESS®, CITATION®, CLARIVA®, COLZOR®, CRUISER®, CULTAR®, CURACON®, DACONIL®, DISCOVER®, DIVIDEND®, DUAL®, DUAXO®, DURIVO®, DYNASTY®, EDDUS®, ELATIS®, ELUMIS®, ENDEAVOR®, ENVOKE®, EPERON®, EPIVO®, ERIJAN®, FARMORE®, FLAGSHIP®, FLEX®, FLEXSTAR®, FLORIPRO SERVICES®, FOLIO®, FORCE®, FORTENZA®, FUSIFLEX®, FUSILADE®, GESAGARD®, GESAPAX®, GESAPRIM®, GOLD®, GOLDEN HARVEST®, GRADUATE®, GRADUATEA+®, GRAMOXONE®, HALEX®, HERITAGE®, HILLESHOG®, HORIZON®, HYVIDO®, INSEGAR®, ISABION®, KARATE ZEON®, LENTAGRAN®, LISTEGO®, LOGRAN®, LUMAX®, MAAG®, MATCH®, MAXIM®, MAXX®, MENTOR®, MERTECT®, MILAGRO®, MINECTO®, MIRAVIS®, MODDUS®, NEMATHORIN®, NK®, ORDRAM®, ORONDIS®, PALISADE®, PEAK®, PEGASUS®, PIRIMOR®, POLO®, PREFIX®, PRIMO®, PROCLAIM®, QUANTIS®, REFLECT®, REFLEX®, REGLONE®, RESOLVA®, REVUS®, RIFIT®, ROGERS®, S&G®, SAKALIA®, SALTRO®, SCHOLAR®, SCIMITAR®, SCORE®, SEGURIS®, SEQUESTRENE®, SETOFF®, SOFIT®, SOLVIGO®, STADIUM®, SUPREN®, SWITCH®, SYMETRA®, SYNGENTA®, TAEGRO®, TAVIUM®, TERVIGO®, TILT®, TIMOREX®, TOPIK®, TOPREX®, TRIGARD®, TRIMMIT®, TOUCHDOWN®, UNIX®, VAYANTIS®, VERTIMAC®, VIBRANCE®, WEATHER STIK®, from Syngenta Crop Protection (Basel, Switzerland); and ASULOX®, BALISTIK®, BEETUP®, BELLMAC®, BETASANA®, BETTIX®, BUGUIS®, CENTURION®, CLIOPHAR®, COLZAMID®, CORZAL®, DEFIANT®, DEVRINOL®, MINSTREL®, AFFIX®, AXIDOR®, BUZZ®, MIMIX®, DIOZINOS®, DIPROSPERO®, EVITO®, MANZATE®, MICROTHIOL®, NAUTILE®, PENNCOZEB®, PROMESS®, PROPLANT®, PROXANIL®, PYRUS®, SACRON®, SYLLIT®, TEBUZOL®, THIOPRON®, TOKYO®, UNIZEB®, VACCIPLANT®, VIDEO®, ZOXIS®, CYTHRIN®, DIMILIN®, FORESTER®, FUMICYP®, TALISMA®, B-NINE®, FAZOR®, GYRO®, HIMALAYA®, ICENI®, TRINEXIS®, IODUS®, AUDIT®, BASAGRAN®, BATLIUM®, BOYCOTT®, BROADLOOM®, COYOTE®, COLLIDE®, DUET®, ETHOTRON®, EVEREST®, IMIFLEX®, LIFELINE®, METRICOR®, MOCCASIN®, MOTIF®, PRE-PARE®, SATELLITE®, SHADOW®, SHUTDOWN®, STAM®, SUPERWHAM! ®, SUPREMACY®, TRICOR®, TRIZENTA®, CUPROFIX®, DEXTER®, ELEVATE®, ELIXIR®, FORTIX®, FROGHORN®, METEOR®, MICROTHI®, ORANIL®, PH-D®, PROCURE®, RANCOVA®, TEPERA®, TERRAGUARD®, TERRAMASTER®, TERRAZOLE®, TOPSIN®, TRIONIC®, ZIRAM®, ZOLERA®, ADIOS®, GOLDWING®, OFF-SHOOT-T®, PACZOL®, ROYAL®, ROYALTAC®, ACENTHRIN®, ACEPHATE®, ACRAMITE®, ADEPT®, ARGYLE®, ASSAIL®, BANTER®, BIFENTURE®, BIOMITE®, COMITE®, DIMILIN®, ENKOUNTER®, INTRUDER®, KANEMITE®, LAMBDA-CY®, MICROMITE®, OMITE®, PEDESTAL®, PERM-UP®, RIMON®, STRAFER®, TURNSTYLE®, UP-CYDE®, VENDEX®, VIGILANT®, ZYLO®, ATTENDANT®, BEAN GUARD®, ALLEGIANCE®, BELMONT®, ENHANCE®, GRAINGUARD®, MESH®, PRO-GRO®, RANCONA®, STARTUP®, THIRAM®, VITAFLO®, VITAVAX®, MAGNAPHOS®, WEEVIL-CIDE®, AQUASTRIKE®, AQUATHOL®, PEGASUS, GOLIATH, POACONSTRICTOR, RAVEN, T-BIRD, UP-END®, UP-START®, ETHEPHON PEGASUS, GOLIATH, POACONSTRICTOR, RAVEN, T-BIRD, UP-END®, UP-START®, ZEBA® and FLORAMITE® from UPL Limited (Mumbai, Maharashtra, India). Examples of dispersants that may be included in formulations of the present disclosure include, but not are not limited to, anionic surfactants, cationic surfactants, non-ionic surfactants, and combinations thereof. See generally, e.g., EP 0245970; US 5,496,568; WO 2008/144024; WO 2009/135049; WO 2011/126832; WO 2017/083049; WO 2020/225276; WO 2021/055316; WO 2022/096688; WO 2022/096691; WO 2022/096692; WO 2022/096693; WO 2022/096694; WO 2022/096695; WO 2022/096696. In some embodiments, formulations of the present disclosure comprise one or more anionic surfactants. For example, in some embodiments, formulations of the present disclosure comprise one or more anionic surfactants selected from the group consisting of alkyl carboxylates (e.g., sodium stearate), alkyl sulfates (e.g., alkyl lauryl sulfate, sodium lauryl sulfate), alkyl ether sulfates, alkyl amido ether sulfates, alkyl aryl polyether sulfates, alkyl aryl sulfates, alkyl aryl sulfonates, alkyl sulfonates, alkyl amide sulfonates, alkyl aryl sulfonates, alkyl benzene sulfonates, alkyl diphenyloxide sulfonate, alpha-olefin sulfonates, alkyl naphthalene sulfonates, paraffin sulfonates, alkyl sulfosuccinates, alkyl ether sulfosuccinates, alkylamide sulfosuccinates, alkyl sulfosuccinamates, alkyl sulfoacetates, alkyl phosphates, alkyl ether phosphates, acyl sarconsinates, acyl isethionates, N-acyl taurates, N-acyl-N-alkyltaurates, benzene sulfonates, cumene sulfonates, dioctyl sodium sulfosuccinate, ethoxylated sulfosuccinates, lignin sulfonates, linear alkylbenzene sulfonates, monoglyceride sulfates, perfluorobutanesulfonate, perfluorooctanesulfonate, phosphate ester, styrene acrylic polymers, toluene sulfonates and xylene sulfonates. In some embodiments, formulations of the present disclosure comprise one or more cationic surfactants. For example, in some embodiments, formulations of the present disclosure comprise one or more cationic surfactants selected from the group consisting of alkyltrimethylammonium salts (e.g., cetyl trimethylammonium bromide, cetyl trimethylammonium chloride), cetylpyridinium chloride, benzalkonium chloride, benzethonium chloride, 5-Bromo-5-nitro- 1,3-dioxane, dimethyldioctadecylammonium chloride, cetrimonium bromide, dioctadecyldimethylammonium bromide and/or octenidine dihydrochloride. In some embodiments, formulations of the present disclosure comprise one or more nonionic surfactants. For example, in some embodiments, formulations of the present disclosure comprise one or more nonionic surfactants selected from the group consisting of alcohol ethoxylates (e.g., TERGITOL™ 15-S surfactants (The Dow Chemical Company, Midland, MI), such as TERGITOL™15-S-9, alkanolamides, alkanolamine condensates, carboxylic acid esters, cetostearyl alcohol, cetyl alcohol, cocamide DEA, dodecyldimethylamine oxides, ethanolamides, ethoxylates of glycerol ester and glycol esters, ethylene oxide polymers, ethylene oxide-propylene oxide copolymers, glucoside alkyl ethers, glycerol alkyl ethers, glycerol esters, glycol alkyl ethers (e.g., polyoxyethylene glycol alkyl ethers, polyoxypropylene glycol alkyl ethers), glycol alkylphenol ethers (e.g., polyoxyethylene glycol alkylphenol ethers,), glycol esters, monolaurin, pentaethylene glycol monododecyl ethers, poloxamer, polyamines, polyglycerol polyricinoleate, polysorbate, polyoxyethylenated fatty acids, polyoxyethylenated mercaptans, polyoxyethylenated polyoxyproylene glycols, polyoxyethylene glycol sorbitan alkyl esters, polyethylene glycol-polypropylene glycol copolymers, polyoxyethylene glycol octylphenol ethers, polyvinyl pynolidones, sugar-based alkyl polyglycosides, sulfoanylamides, sorbitan fatty acid alcohol ethoxylates, sorbitan fatty acid ester ethoxylates, sorbitan fatty acid ester and/or tertiary acetylenic glycols. In some embodiments, formulations of the present disclosure comprise one or more zwitterionic surfactants. For example, in some embodiments, formulations of the present disclosure comprise one or more zwitterionic surfactants selected from the group consisting of 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, cocamidopropyl betaine, cocamidopropyl hydroxysultaine, phosphatidylserine, phosphatidylethanolamine, phosphatidylcholine and/or one or more sphingomyelins. In some embodiments, formulations of the present disclosure comprise one or more soaps and/or organosilicone surfactants. Non-limiting examples of commercially available dispersants include products sold under the tradenames ATLOX™ (e.g., 4916, 4991; Croda International PLC, Edison, NJ), ATLOX METASPERSE™ (Croda International PLC, Edison, NJ), BIO-SOFT® (e.g., N series, such as N1-3, N1-7, N1-5, N1-9, N23-3, N2.3-6.5, N25-3, N25-7, N25-9, N91- 2.5, N91-6, N91-8; Stepan Company, Northfield, IL), MAKON® nonionic surfactants (e.g., DA-4, DA-6 and DA-9; Stepan Company, Northfield, IL), MORWET® powders (Akzo Nobel Surface Chemistry LLC, Chicago, IL), MULTIWET™ surfactants (e.g., MO-85P-PW-(AP); Croda International PLC, Edison, NJ), SAFER® soaps (Woodstream Corporation, Inc., Lancaster, PA), SILWET® surfactants (Momentive Performance Materials, Inc., Niskayuna, NY), SPAN™ surfactants (e.g., 20, 40, 60, 65, 80 and 85; Croda Inc., Edison NJ), TAMOL™ dispersants (The Dow Chemical Company, Midland, MI ), TERGITOL™ surfactants (e.g., TMN-6 and TMN-100X; The Dow Chemical Company, Midland, MI), TERSPERSE surfactants (e.g., 2001, 2020, 2100, 2105, 2158, 2700, 4894 and 4896; Hunstman Corp., The Woodlands, TX), TRITON™ surfactants (e.g., X-100; The Dow Chemical Company, Midland, MI), TWEEN® surfactants (e.g., TWEEN® 20 (polyoxyethylenesorbitan monolaurate), 21, 22, 23, 28, 40, 60, 61, 65, 80, 81 and 85; Croda International PLC, Edison, NJ) and combinations thereof. Additional examples of dispersants may be found in BAIRD & ZUBLENA.1993. SOIL FACTS: USING WETTING AGENTS (NONIONIC SURFACTANTS) ON SOIL (North Carolina Cooperative Extension Service Publication AG-439-25) (1993); BURGES, FORMULATION OF MICROBIAL BIOPESTICIDES: BENEFICIAL MICROORGANISMS, NEMATODES AND SEED TREATMENTS (Springer Science & Business Media) (2012); MCCARTY, WETTING AGENTS (Clemson University Cooperative Extension Service Publication) (2001). Examples of drying agents that may be included in formulations of the present disclosure include, but not are not limited to, calcium stearate, clay (e.g., attapulgite clay, montmorillonite clay), graphite, magnesium stearate, magnesium sulfate, powdered milk, silica (e.g., fumed silica, hydrophobically-coated silica, precipitated silica), soy lecithin, talc, and combinations thereof. Additional examples of drying agents may be found in Burges, Formulation of Microbial Biopesticides: Beneficial Microorganisms, Nematodes and Seed Treatments (Springer Science & Business Media) (2012). Non-limiting examples of commercially available drying agents include products sold under the tradenames AEROSIL® and SIPERNAT® from Evonik Corporation (Parsippany, NJ), BENTOLITE® from BYK-Chemie GmbH (Wesel, Germany), and INCOTEC® from INCOTEC Inc. (Salinas, CA). Examples of suitable effect pigments include, but not are not limited to, substrate materials such as talc, silicate materials (e.g., mica), clay minerals, calcium carbonate, kaolin, phlogopite, alumina and similar substances coated with a semi-transparent metal oxide such as titanium dioxide, iron oxide, chromium oxide or zirconium oxide. Non-limiting examples of commercially available effect pigments include products sold under the tradenames DISPERS®, HELIOGEN®, IRAGON®, IRGALITE®, LUCONYL®, MAGNAPEARL®, SUNMICA®, SUNAG™, SUNSPERSE®, UNISPERSE® and XFAST® pigments from SunChemical Colors & Effects GmbH (Ludwigshafen am Rhein, Germany). Examples of suitable growth media include, but not are not limited to, growth media suitable for culturing one or more plant-beneficial microorganisms (e.g., Czapek-Dox medium, glycerol yeast extract, mannitol yeast extract, potato dextrose broth, YEM media). Examples of suitable microbial extracts include, but not are not limited to, bacterial extracts, fungal extracts, mycorrhizal extracts, and combinations thereof. In some embodiments, formulations of the present disclosure comprise comprise one or more extracts of media comprising one or more plant-beneficial microorganisms. See infra. Examples of nutrients that may be included in formulations of the present disclosure include, but not are not limited to, organic acids (e.g., acetic acid, citric acid, lactic acid, malic acid, taurine, etc.), macrominerals (e.g., phosphorous, calcium, magnesium, potassium, sodium, iron, etc.), trace minerals (e.g., boron, cobalt, chloride, chromium, copper, fluoride, iodine, manganese, molybdenum, selenium, zinc, etc.), vitamins, (e.g., vitamin A, vitamin B complex (i.e., vitamin B1, vitamin B2, vitamin B3, vitamin B5, vitamin B6, vitamin B7, vitamin B8, vitamin B9, vitamin B12, choline) vitamin C, vitamin D, vitamin E, vitamin K, carotenoids (α-carotene, β-carotene, cryptoxanthin, lutein, lycopene, zeaxanthin, etc.), and combinations thereof. See also, generally, e.g., US 2014/0235447; WO 2022/029224; WO 2022/029221; WO 2021/255118; WO 2021/247915; US 2021/0300837; US 2020/0148605; US 2012/0247164; US 2016/0355443; US 2020/0055794; US 2011/0154873; US 2006/0243009; US 2017/0088474. Examples of pest attractants and feeding stimulants that may be included in formulations of the present disclosure include, but not are not limited to, brevicomin, ceralure, codlelure, cue-lure, disparlure, dominicalure, eugenol, frontalin, gossyplure, grandlure, hexalure, ipsdienol, ipsenol, japonilure, latitlure, lineatin, litlure, looplure, medlure, megatomic acid, methyl eugenol, moguchun, α-multistriatin, muscalure, orfalure, oryctalure, ostramone, rescalure, siglure, sulcatol, trimedlure, trunc-call, and combinations thereof. See generally, e.g., WO 00/28824; US 5,607,684; US 4,510,133; US 5,290,556; US 60774634; US 6,773,727; WO 2022/051661; EP 0563963; WO 2013/164384; WO 2003/020030; US 8,420,070; US 5,401,506; WO 92/11856. Examples of pH control components that may be included in formulations of the present disclosure include phosphate and other salts capable of buffering at the desired pH, and having an aqueous solubility of more than 1% w/w. A preferred pH control component is a phosphate buffer containing the ionic species HPO₄ ^2- and H₂PO₄-. See generally WO 2023/288294. A pH control component may be a single ionic species that can maintain a constant pH but only provide a buffering effect towards either acidification or basification. An example of such, is HPO4^2- which can ensure an alkaline pH (of approximately 9) and provide a buffering effect against acidification. It may be beneficial in an agricultural setting to keep the pH constant at an alkaline pH, as most environmental factors will cause acidification of the droplet and deposit. In preferred embodiments, the pH control component does not significantly change pH (+/- 0.5 pH units) or change in a desired direction upon drying when the solvent evaporates from the droplet on the leaf surface. Some buffers will, upon drying, change pH as a result of differences in solubility of the buffer components. As an example, the pH of a sodium phosphate buffer constituting of Na2HPO4 and NaH2PO4 can reduce to pH 4 or lower upon drying since the dibasic form (Na₂HPO₄) will crystallize to a larger degree. On the contrary, the pH of a potassium phosphate buffer constituting of K2HPO4 and KH2PO4 will approach pH 9 upon drying since the monobasic form (KH2PO4) has the lowest solubility (Sarciaux 1999). A pH control component is most effective (highest buffer capacity) when the pKa is close to the desired pH of the composition. This will reduce the amount of buffer needed to maintain a desired pH. In an embodiment, the buffer includes salts having a neutral/alkaline pKa, such as a pKa in the range of 6.5 to 10. As a rule of thumb, a pH control component can be used to control the pH of a solution at a pH +/- 1 pH-unit from its pKa value. pH control components with a pKa value above 6.5 are useful for controlling the pH at 7.5 or above. Examples of suitable pH control component includes, but are not limited to: Sodium/potassium phosphate (pKa₁2.12, pKa₂7.21, pKa₃ 12.67), sodium/potassium carbonate (pKa16.37, pKa210.32), 2-amino-2-(hydroxymethyl)-1,3-propanediol (TRIS) (pKa 8.1), [Bis(2-hydroxyethyl)amino]acetic acid (Bicine) (pKa 8.35), N-[tris(hydroxymethyl)methyl]glycine (Tricine) (pKa 8.15), 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) (pKa₁3.0, pKa₂7.5), N-[tris(hydroxymethyl)methyl]- 2-aminoethanesulfonic acid (TES) (pKa 7.55), 3-(N-morpholino)propanesulfonic acid (MOPS) (pKa 7.2), tris(hydroxymethyl)methylamino]propanesulfonic acid (TAPS) (pKa 8.44), N-[tris(hydroxymethyl)methyl]-3-amino-2- hydroxypropanesulfonic acid (TAPSO) (pKa 7.6), glycylglycine (pKa1 3.14 pKa2 8.17), 2-(N- cyclohexylamino)ethanesulfonic acid (CHES) (pKa 9.3), sodium/potassium borate (pKa₁9.24, pKa₂12.4, pKa₃13.3), 2- amino-2-methyl-1,3-propanediol (ammediol) (pKa 8.8), triethanol amine (pKa 7.74), 2-amino-2-methyl-1-propanol (pKa 9.7), glycine (pKa12.34, pKa29.6), histidine (pKa11.82, pKa26.00, pKa39.17), and other amino acid buffers. Non-preferred pH control components include, but are not limited to, pH control components with an unfavorable pKa (pKa <6.5 for an enzyme that requires an alkaline pH), volatile pH control component, pH control component that display significant phytotoxicity (this may sometimes include the above-mentioned "suitable" pH control components, as phytotoxicity is depended on buffer concentration, pH and target crop), and pH control components that are unwanted in the environment and therefore regulated by authorities (this may sometimes include the above-mentioned "suitable" pH control component, as regulations varies throughout the world). In some embodiments, formulations of the present disclosure comprise one or more pH control components in an amount of about/at least 0.01–10% w/w, preferably about/at least 0.05–5% w/w. In some embodiments, formulations of the present disclosure can maintain an alkaline pH. pH control components may be used to obtain such formulations. For example, in some preferred embodiments, formulations of the present disclosure comprise one or more pH control components selected to provide a composition having an alkaline pH within the operable pH range(s) of each enzyme in the formulation, most preferably within +/- 1 pH-unit from the optimal pH value of each enzyme in the formulation. Thus, in some embodiments, formulations of the present disclosure comprise a pH control component, such as a buffer, where an 1% w/w aqueous solution of the pH control component (buffer) has an alkaline pH in which each enzyme in the formulation is operable. In some embodiments, formulations of the present disclosure can maintain an acidic pH. pH control components may be used to obtain such formulations. For example, in some preferred embodiments, formulations of the present disclosure comprise one or more pH control components selected to provide a composition having an acidic pH within the operable pH range(s) of each enzyme in the formulation, most preferably within +/- 1 pH-unit from the optimal pH value of each enzyme in the formulation. Thus, in some embodiments, formulations of the present disclosure comprise a pH control component, such as a buffer, where an 1% w/w aqueous solution of the pH control component (buffer) has an acidic pH in which each enzyme in the formulation is operable. Examples of plant-beneficial microbes that may be included in formulations of the present disclosure include, but not are not limited to, diazotrophs, phosphate-solubilizing microorganisms, mycorrhizae, biopesticides, and combinations thereof. See generally, e.g., WO 92/08355; US 2003/0082164; US 2008/0320615; US 2016/0345588; US 2018/0168168; US 2005/0187107; US 2006/0258534; US 2018/0279624; US 10,820,594; US 2019/0014786; US 10,874,109; US 10,856,552; US 2019/0014787; US 11,076,603; US 2020/0093125; US 2020/0085065; US 2020/0000098; US 2019/0345572; US 2020/0263734; WO 2021/101949; WO 2021/101937; WO 2016/201284; WO 2018/186307; WO 2007/142543; WO 2017/205800; WO 2015/003908; WO 2021/018321; WO 2003/016510; WO 2016/044542; WO 92/11856. In some embodiments, formulations of the present disclosure comprise one or more of the following: Azospirillum brasilense Ab-V5, Azospirillum brasilense Ab-V6, Azospirillum brasilense INTA Az-39, Bacillus amyloliquefaciens D747, Bacillus amyloliquefaciens NRRL B-50349, Bacillus amyloliquefaciens NRRL B-50350, Bacillus amyloliquefaciens TJ1000, Bacillus amyloliquefaciens FZB24, Bacillus amyloliquefaciens FZB42, Bacillus amyloliquefaciens IN937a, Bacillus amyloliquefaciens IT-45, Bacillus amyloliquefaciens TJ1000, Bacillus amyloliquefaciens MBI600, Bacillus amyloliquefaciens BS27 (deposited as NRRL B-5015), Bacillus amyloliquefaciens BS2084 (deposited as NRRL B-50013), Bacillus subtilis GB07, Bacillus subtilis QST-713, Bacillus subtilis FZB24, Bacillus subtilis D747, Bacillus subtilis 3BP5 (deposited as NRRL B-50510), Bacillus subtilis DSM 17231, Bacillus subtilis DSM 32324, Bacillus subtilis DSM 33113, Bacillus subtilis RTI477 (deposited as ATCC PTA-121167), Bacillus thuringiensis AQ52 (deposited as NRRL B-21619), Bacillus thuringiensis ATCC 13367, Bacillus thuringiensis GC-91, Bacillus thuringiensis NRRL B-21619, Bacillus thuringiensis ABTS-1857, Bacillus thuringiensis SAN 401 I, Bacillus thuringiensis ABG-6305, Bacillus thuringiensis ABG-6346, Bacillus thuringiensis AM65-52, Bacillus thuringiensis SA-12, Bacillus thuringiensis SB4, Bacillus thuringiensis ABTS-351, Bacillus thuringiensis HD-1, Bacillus thuringiensis EG 2348, Bacillus thuringiensis EG 7826, Bacillus thuringiensis EG 7841, Bacillus thuringiensis DSM 2803, Bacillus thuringiensis NB-125, Bacillus thuringiensis NB-176, Bacillus thuringiensis RTI545 (deposited as ATCC PTA-122161), Bacillus velezensis DSM 34878, Bradyrhizobium spp. 8A57, Bradyrhizobium elkanii SEMIA 501, Bradyrhizobium elkanii SEMIA 587, Bradyrhizobium elkanii SEMIA 5019, Bradyrhizobium japonicum 61A227, Bradyrhizobium japonicum 61A228, Bradyrhizobium japonicum 61A273, Bradyrhizobium japonicum E-109, Bradyrhizobium japonicum NRRL B-50586 (also deposited as NRRL B-59565), Bradyrhizobium japonicum NRRL B-50587 (also deposited as NRRL B-59566), Bradyrhizobium japonicum NRRL B-50588 (also deposited as NRRL B-59567), Bradyrhizobium japonicum NRRL B-50589 (also deposited as NRRL B-59568), Bradyrhizobium japonicum NRRL B-50590 (also deposited as NRRL B-59569), Bradyrhizobium japonicum NRRL B-50591 (also deposited as NRRL B-59570), Bradyrhizobium japonicum NRRL B-50592 (also deposited as NRRL B-59571), Bradyrhizobium japonicum NRRL B-50593 (also deposited as NRRL B-59572), Bradyrhizobium japonicum NRRL B-50594 (also deposited as NRRL B-50493), Bradyrhizobium japonicum NRRL B-50608, Bradyrhizobium japonicum NRRL B-50609, Bradyrhizobium japonicum NRRL B-50610, Bradyrhizobium japonicum NRRL B-50611, Bradyrhizobium japonicum NRRL B-50612, Bradyrhizobium japonicum NRRL B-50726, Bradyrhizobium japonicum NRRL B-50727, Bradyrhizobium japonicum NRRL B-50728, Bradyrhizobium japonicum NRRL B-50729, Bradyrhizobium japonicum NRRL B-50730, Bradyrhizobium japonicum SEMIA 566, Bradyrhizobium japonicum SEMIA 5079, Bradyrhizobium japonicum SEMIA 5080, Bradyrhizobium japonicum USDA 6, Bradyrhizobium japonicum USDA 110, Bradyrhizobium japonicum USDA 122, Bradyrhizobium japonicum USDA 123, Bradyrhizobium japonicum USDA 127, Bradyrhizobium japonicum USDA 129, Bradyrhizobium japonicum USDA 532C, Erwinia billingiae NRRL B-67766, Gliocladium virens ATCC 52045, Gliocladium virens GL-21, Glomus intraradices RTI-801, Lysinibacillus sphaericus NRRL B-67350, Lysinibacillus sphaericus NRRL B-67351, Lysinibacillus sphaericus NRRL B- 67486, Metarhizium anisopliae F52, Paenibacillus graminis NRRL B-68249, Paenibacillus kribbensis NRRL B-68250, Paenibacillus peoriae NRRL B-67884, Paenibacillus peoriae NRRL B-67885, Paenibacillus sonchi NRRL B-68251, Penicillium bilaiae ATCC 18309, Penicillium bilaiae ATCC 20851, Penicillium bilaiae ATCC 22348, Penicillium bilaiae NRRL 50162, Penicillium bilaiae NRRL 50169, Penicillium bilaiae NRRL 50776, Penicillium bilaiae NRRL 50777, Penicillium bilaiae NRRL 50778, Penicillium bilaiae NRRL 50777, Penicillium bilaiae NRRL 50778, Penicillium bilaiae NRRL 50779, Penicillium bilaiae NRRL 50780, Penicillium bilaiae NRRL 50781, Penicillium bilaiae NRRL 50782, Penicillium bilaiae NRRL 50783, Penicillium bilaiae NRRL 50784, Penicillium bilaiae NRRL 50785, Penicillium bilaiae NRRL 50786, Penicillium bilaiae NRRL 50787, Penicillium bilaiae NRRL 50788, Penicillium bilaiae NRRL 67154, Penicillium bilaiae NRRL 67155, Penicillium bilaiae NRRL 67156, Penicillium bilaiae NRRL 67157, Penicillium bilaiae NRRL 67158, Penicillium bilaiae NRRL 67159, Penicillium bilaiae RS7B-SD1, Penicillium brevicompactum AgRF18, Penicillium canescens ATCC 10419, Penicillium expansum ATCC 24692, Penicillium expansum YT02, Penicillium fellatanum ATCC 48694, Penicillium gaestrivorus NRRL 50170, Penicillium glabrum DAOM 239074, Penicillium glabrum CBS 229.28, Penicillium janthinellum ATCC 10455, Penicillium lanosocoeruleum ATCC 48919, Penicillium radicum ATCC 201836, Penicillium radicum FRR 4717, Penicillium radicum FRR 4719, Penicillium radicum N93/47267, Penicillium raistrickii ATCC 10490, Pseudomonas jessenii PS06, Pseudomonas koreensis NRRL B-67883, Rhizobium leguminosarum SO12A-2 (IDAC 080305-01), Sinorhizobium fredii CCBAU114, Sinorhizobium fredii USDA 205, Streptomyces sp. NRRL B-30145, Streptomyces sp. M1064, Streptomyces WYE 53, Streptomyces glabus NRRL 30232, Streptomyces lydicus WYEC 108 (deposited as ATCC 55445), Streptomyces violaceusniger YCED 9, Trichoderma asperellum SKT-1, Trichoderma asperellum ICC 012, Trichoderma atroviride LC52, Trichoderma atroviride CNCM 1- 1237, Trichoderma fertile JM41R, Trichoderma gamsii ICC 080, Trichoderma hamatum ATCC 52198, Trichoderma harzianum ATCC 52445, Trichoderma harzianum KRL-AG2, Trichoderma harzianum T-22, Trichoderma harzianum TH- 35, Trichoderma harzianum T-39, Trichoderma harzianum ICC012, Trichoderma reesi ATCC 28217, Trichoderma virens ATCC 58678, Trichoderma virens GI-3, Trichoderma virens GI-21, Trichoderma virens GL-21, Trichoderma virens G-41, Trichoderma viridae ATCC 52440, Trichoderma viridae ICC080, Trichoderma viride TV1, Yersinia entomophaga MH96, Yersinia entomophaga NRRL B-67598, Yersinia entomophaga NRRL B-67599, Yersinia entomophaga NRRL B-67600 and Yersinia entomophaga NRRL B-67601. Non-limiting examples of commercially available plant-beneficial microorganisms include products sold under the tradenames SERIFEL® from BASF (Ludwigshafen, Germany); VOTIVO® from Bayer Crop Science (Creve Coeur, MO, USA); AGREE®, AGRIPHAGE™, AGSIL®, ANCORA, AZATIN®, BOTANIGARD®, BOTEGHA®, BUG-N- SLUGGO®, CARB-O-NATOR®, CRYMAX®, CUEVA®, CYD-X®, DEFGUARD®, DELIVER®, DES-X®, DOUBLE NICKEL®, FIREFIGHTER™, GEMSTAR®, GROTTO®, HOMEPLATE®, JAVELIN®, KALMOR®, KOCIDE®, LIFEGARD®, MADEX®, MELOCON®, MYCOTROL®, NEEMIX®, OSO™, PFR-97™, SEDUCE™, SIL-MATRIX®, SLUGGO®, SOILGARD®, THURICIDE®, TRIACT®, TRIATHLON® and TRILOGY® from Certis (Columbia, MD); BEXFOND™ and HEARKEN® from Corteva Agroscience (Indianapolis, IN, USA); ACCUDO®, FURAGRO®, PRESENCE®, QUARTZO®, SEAMAC® and ZIRONAR® from FMC Corporation (Philadelphia, PA, USA); B.SUB™, BAM™, BIO-N™, BIO-P™, BIO-PLEX™, MICRO-FORCE™, MYCO-FORCE™, PLATFORM™, ROOT-GUARD™, and TRICHO-SHIELD™ from Nutri-Tech Solutions Pty Ltd. (Yandina, Queensland, Australia); PROVEN® and RETURN® from Pivot Bio (Berkeley, CA); ATTIS® and NEMIX® from Chr Hansen (Hoersholm, Denmark); INTENSE® from Matra Asia (Pvt) Ltd. (Lahore, Pakistan); ATAPLAN®, AVIZON®, PRESENCE®, PROVILAR® and QUARTZO® from FMC; NIMAXXA® from UPL Corp. (London, United Kingdom); ACTINOVATE®, AZOMAX®, B300®, B360®, BIONIQ®, BOLT®, CANESHAKTI™, CELL-TECH®, CTS-200®, CTS-400®, CTS-500®, CTS-1000®, CUE®, GLYCIMAX®, JUMPSTART®, LEGUMAX®, MYCOPLEX®, NITRAGIN®, NODPRO®, OPTIMIZE®, PROVENTUS®, QUICKROOTS®, RATCHET®, REVV®, RHIZOMAX®, RHIZOMYCO®, RHIZOMYX®, RHHIZOPLEX®, TAEGRO®, TAGTEAM®, TORQUE® and WAVE® from Novozymes (Bagsvaerd, Denmark). Examples of plant signal molecules that may be included in formulations of the present disclosure include, but are not limited to, auxins, chitin oligomers, chitins, chitosans, cytokinins, gibberellins, glutathiones, jasmonic acid, karrikin, linoleic acid, linolenic acid, lipo-chitooligosaccharides, phenolic acids, strigolactones, and combinations thereof. See generally, e.g., US 7,262,151, WO 97/00614, WO 2007/117500, WO 2009/115496, WO 2013/036922, WO 2013/040366, WO 2013/044208, WO 2014/044214, WO 2014/070757, WO 2014/143620, WO 2015/069708, WO 2019/147660. Examples of preservatives that may be included in formulations of the present disclosure include, but are not limited to, benzoates (e.g., sodium benzoate), benzoic acid, methyl paraben, phenoxy ethanol, proprionates (e.g., ammonium proprionate, calcium proprionate, sodium proprionate), proprionic acid, sorbates (e.g., potassium sorbate, sodium sorbate), 1,2-benzisothiazolin-3-one (PROXEL®; Basel, Switzerland), and combinations thereof. Examples of suitable rain fasteners include, but not are not limited to, organo-modified siloxanes (organosiloxanes), such as organo-modified trisiloxanes (e.g., polyether-modified trisiloxanes, such as polyalkyleneoxide- modified heptamethyltrisiloxane), organo-modified polysiloxanes (e.g., polyether-modified polysiloxanes), and combinations thereof. See generally, e.g., EP 0245970; US 5,496,568; WO 2008/144024; WO 2009/135049; WO 2011/126832; WO 2017/083049; WO 2020/225276; WO 2021/055316; WO 2022/096688; WO 2022/096691; WO 2022/096692; WO 2022/096693; WO 2022/096694; WO/2022/096695; WO 2022/096696; WO 2023/288294. In some embodiments, formulations of the present disclosure comprise one or more organo-modified siloxanes having the general molecular structure of Formula 1: R¹ ₃SiO[R¹ ₂SiO]_A[R¹R²SiO]_BSiR¹ ₃ in which R¹ represents identical or different from each other hydrocarbon substituents of 1-10 carbons or hydrogen, preferred are methyl, ethyl, propyl and phenyl substituents, particularly preferred are methyl substituents; R² represents identical or different from each other polyether substituents of the general Formula II: -R³O[CH2CH2O]C[CH2CH(CH3)O]D[CHR⁴CHR⁴O]ER⁵ wherein R³ represents identical or different from each other hydrocarbon moieties of 1-8 carbons, which optionally is interrupted by oxygen atoms. Preferred is linear hydrocarbons of 2-4 carbons, particularly preferred is -CH₂-CH₂-CH₂- R⁴ represents identical or different from each other hydrocarbon substituents of 1-12 carbons or hydrogen, preferred is methyl, ethyl, phenyl or hydrogen substituents R⁵ represents identical or different from each other hydrocarbon substituents of 1-16 carbons, which optionally contains urethane, carbonyl or carboxylic acid functionality, or hydrogen. Methyl or hydrogen substituents are preferred, with hydrogen being most preferred. A is 0-200, preferably 0-1, more preferably 0. B is 0-200, preferably 0.5-2, more preferably 1. In preferred embodiments, A+B > 0. C is 0-60, preferably 1-15. D is 0-60, preferably 0-10. E is 0-20, preferably 0-10, more preferably 0. In preferred embodiments, C+D+E > 0. A trisiloxane may be defined as a molecule of the general Formula I with A = 0 and B = 1, whereas a polysiloxane is a molecule of the general formula I with A + B >1 and A >1. Non-limiting examples of commercially available organo-modified siloxanes include products sold under the tradenames BIOSPREAD® surfactants (Grosafe Chemicals Ltd., New Zealand); BREAK-THRU® surfactants (Evonik Operations Gmbh, Essen, Germany), such as BREAK-THRU® AF 5503, BREAK-THRU® AF 9902, BREAK-THRU® AF 9903, BREAK-THRU® OE 440, BREAK-THRU® OE 444, BREAK-THRU® OE 446, BREAK-THRU® S 200, BREAK-THRU® S 233, BREAK-THRU® S 240, BREAK-THRU® S 255, BREAK-THRU® S 279, BREAK-THRU® S 301, BREAK-THRU® SD 260, and BREAK-THRU® UNION; BYK® surfactants (BYK-Chemie GmbH, Wesel, Germany), such as BYK® -348; ECOSPREAD® surfactants (Grosafe Chemicals Ltd., New Zealand); HI-WETT® surfactants (Loveland Products, Inc., Greeley, CO, USA); and SILWET™ surfactants (Momentive, Inc., Waterford, NY, USA), such as SILWET™ L-77, SILWET™ HS-312, SILWET™ 408, SILWET™ 618, SILWET™ 625, SILWET™ 636, SILWET™ 641, SILWET™ 806, SILWET™ DA-40, SILWET™ DRS-60, SILWET™ ECO, SILWET™ FUSION, SILWET™ HS 312, SILWET™ HS 604, SILWET™ HSEC, SILWET™ LF, SILWET™ OC, and SILWET™ STIK 2. Examples of suitable rhealogical agents include, but not are not limited to, alginates, carrageenan, clays (e.g., attapulgites, sepiolites), gums (e.g., guar gum, xanthan gum), polymerics, silicas, and combinations thereof. Non-limiting examples of commercially available rhealogical agents include products sold under the tradenames ATLOX RHEOSTRUX™ from Croda Inc. (Plainsboro, NJ). Examples of suitable safeners include, but not are not limited to, benoxacor, cloquintocetmexyl, cymetrinil, dichlormid, fenclorim, flurazole, fluxofenim, isoxadifenethyl, mefenpyrdiethyl, napthalic anhydride, and combinations thereof. See generally, Siddique, EUR. J. ADVANCES ENG. TECH.19(11):40–6 (2023) Examples of suitable seed flowability agents include, but not are not limited to, lubricants such as fats and oils, natural and synthetic waxes (e.g., beeswax, carnauba wax, candelilla wax, ouricury wax, paraffin wax, spermaceti), graphite, talc, fluoropolymers (e.g., polytetrafluoroethylene), solid lubricants such as molybdenum disulfide and tungsten disulfide, and combinations thereof. Non-limiting examples of commercially available wax materials include products sold under the tradenames AQUAKLEAN 418 supplied by Micro Powders, Inc. (an anionic aqueous emulsion comprising extra light carnauba wax at 35% solids content). Examples of suitable stabilizing agents include, but not are not limited to, boric acid, boric acid derivatives, inorganic salts, lactic acid, polyols, sugars, sugar alcohols, reversible protease inhibitors, and combinations thereof. See generally, e.g., WO 2007/113241; WO 01/04279; WO 2013/004636; WO 95/02046; WO 2009/118375; WO 2020/115179; WO 96/41859; WO 2007/025549; WO 96/23062; WO 2018/130654; WO 96/22366; WO 92/17571; WO 2017/044473; WO 2017/044545, WO 2017/116837, WO 2017/116846, WO 2017/210163, WO 2017/210166, WO 2018/118740, WO 2018/175681, WO 2018/183491, WO 2018/218008, WO 2018/218016; WO 2018/218035. Examples of suitable UV protectants include, but not are not limited to, aromatic amino acids (e.g., tryptophan, tyrosine), carotenoids, cinnamates, lignosulfonates (e.g., calcium lignosulfonate, sodium lignosulfonate), melanins, mycosporines, polyphenols, salicylates, and combinations thereof. Non-limiting examples of commercially available UV protectants include products sold under the tradenames Borregaard LignoTech™ lignosulfonates (e.g., Borresperse 3A, Borresperse CA, Borresperse NA, Marasperse AG, Norlig A, Norlig 11D, Ufoxane 3A, Ultrazine NA, Vanisperse CB; Borregaard Lignotech, Sarpsborg, Norway) and combinations thereof. Additional examples of UV protectants may be found in Burges, Formulation of Microbial Biopesticides: Beneficial Microorganisms, Nematodes and Seed Treatments (Springer Science & Business Media) (2012). Examples of suitable wetting agents include, but are not limited to, naphthalene sulfonates, such as alkyl naphthalene sulfonates (e.g., sodium alkyl naphthalene sulfonate), isopropyl naphthalene sulfonates (e.g., sodium isopropyl naphthalene sulfonate), butyl naphthalene sulfonates (e.g., sodium n-butyl naphthalene sulfonate), and combinations thereof. Formulations of the present disclosure may comprise any suitable combination of adhesives, anti-freezing agents, anti-settling agents, biostimulants, chemical actives, dispersants, drying agents, effect pigments, emulsifiers, growth media, microbial extracts, nutrients, pest attractants and feeding stimulants, pH control components, plant-beneficial microorganisms, plant signal molecules, preservatives, rain fasteners, rhealogical agents, safeners, seed flowability agents, stabilizing agents, UV protectants and/or wetting agents. In some embodiments, formulations of the present disclosure comprise two, three, four, five, six, seven, eight, nine, ten or more of the components described above. Conversely, in some embodiments, one, two, three, four, five, six, seven, eight, nine, ten or more of the components described above are expressly excluded from formulations of the present disclosure. Formulations of the present disclosure may comprise adhesives, anti-freezing agents, anti-settling agents, biostimulants, chemical actives, dispersants, drying agents, effect pigments, emulsifiers, growth media, microbial extracts, nutrients, pest attractants and feeding stimulants, pH control components, plant-beneficial microorganisms, plant signal molecules, preservatives, rain fasteners, rhealogical agents, safeners, seed flowability agents, stabilizing agents, UV protectants, wetting agents, etc. in any suitable amount(s)/concentration(s). The absolute value of the amount/concentration that is/are sufficient to cause the desired effect(s) may be affected by factors such as the type, size and volume of material to which the composition will be applied, the type(s) of microorganisms in the composition, the number of microorganisms in the composition, the stability of the microorganisms in the composition and storage conditions (e.g., temperature, relative humidity, duration). Those skilled in the art will understand how to select effective amounts/concentrations/combinations using routine dose-response experiments. Guidance for the selection of appropriate amounts/concentrations/combinations can be found throughout the relevant literature, including, for example, in WO 2017/044473, WO 2017/044545, WO 2017/116837, WO 2017/116846, WO 2017/210163, WO 2017/210166, WO 2018/118740, WO 2018/175681, WO 2018/183491, WO 2018/218008, WO 2018/218016 and WO 2018/218035. As will be understood by those skilled in the art, compositions of the present disclosure have many uses, including, but not limited to a) enhancing plant growth environments; b) catalyzing hydrolysis of phytic acids in plant growth media and fertilizers; c) removing phosphate from myo-inositol hexakisphosphates in plant growth media and fertilizers; d) removing phosphate from myo-inositol pentakisphosphates in plant growth media and fertilizers; e) removing phosphate from myo-inositol tetrakisphosphates in plant growth media and fertilizers; f) removing phosphate from myo-inositol trisphosphates in plant growth media and fertilizers; g) removing phosphate from myo-inositol diphosphates in plant growth media and fertilizers; h) removing phosphate from myo-inositol monophosphates in plant growth media and fertilizers; i) producing/releasing soluble forms of phosphorous in plant growth media and fertilizers; j) producing/releasing soluble forms of minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in plant growth media and fertilizers; k) increasing nutrient availability in plant growth media and fertilizers (e.g., phosphorous, calcium, iron, magnesium, manganese, potassium, zinc availability); l) improving nutrient stability in plant growth media and fertilizers (e.g., stabilizing levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in plant growth media and fertilizers); m) increasing nutrient uptake in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; n) increasing nutrient accumulation in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; o) increasing nutrient utilization in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; p) enhancing plant growth; q) enhancing plant yield; r) reducing the amount(s) of exogenous fertilizer needed to achieve a desired result (e.g., the amount of exogenous phosphorous required to produce X bushels of corn); s) reducing nutrient washout/runoff from plant growth media (e.g., phosphorous washout/runoff from field soil); t) enhancing soil microbiomes; u) stimulating growth and/or proliferation of plant-beneficial microorganisms in plant growth media (e.g., growth and/or proliferation of plant-beneficial diazotrophs, phosphate-solubilizers and/or mycorrhizae); v) enhancing plant root nodulation; w) enhancing plant root mycorrhization; x) enhancing the abilities of plants and plant parts to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; y) reducing disease severity in plants and plant parts affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; z) reducing phytopathogen loads in plant growth media; aa) reducing detrimental effects of pesticide-induced phytotoxicity; bb) enhancing the abilities of plant and plant parts to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; cc) reducing disease severity in plants and plant parts affected by abiotic stresses, such as drought, salinity and extreme temperatures; dd) degrading organic materials in plant growth media and fertilizers; and ee) enhancing turnover of organic materials in plant growth media and fertilizers. Compositions of the present disclosure may be particularly useful for catalyzing hydrolysis of phytic acids in plant growth media and fertilizers, thereby releasing soluble forms of phosphorous and cationic minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, into the plant growth media, thus increasing the availability of such nutrients for plant uptake/accumulation/utilization and enhancing plant health/growth/yield. Healthier, more robust plants will be more resistant to infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds, and will be more tolerant of abiotic stresses, such as drought, salinity, extreme temperatures and exposure to chemical pesticides. The present disclosure thus extends to methods of using compositions of the present disclosure (e.g., proteins, formulations, polynucleotides and organisms of the present disclosure) for a) enhancing plant growth environments; b) catalyzing hydrolysis of phytic acids in plant growth media and fertilizers; c) removing phosphate from myo-inositol hexakisphosphates in plant growth media and fertilizers; d) removing phosphate from myo-inositol pentakisphosphates in plant growth media and fertilizers; e) removing phosphate from myo-inositol tetrakisphosphates in plant growth media and fertilizers; f) removing phosphate from myo-inositol trisphosphates in plant growth media and fertilizers; g) removing phosphate from myo-inositol diphosphates in plant growth media and fertilizers; h) removing phosphate from myo-inositol monophosphates in plant growth media and fertilizers; i) producing/releasing soluble forms of phosphorous in plant growth media and fertilizers; j) producing/releasing soluble forms of minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in plant growth media and fertilizers; k) increasing nutrient availability in plant growth media and fertilizers (e.g., phosphorous, calcium, iron, magnesium, manganese, potassium, zinc availability); l) improving nutrient stability in plant growth media and fertilizers (e.g., stabilizing levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in plant growth media and fertilizers); m) increasing nutrient uptake in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; n) increasing nutrient accumulation in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; o) increasing nutrient utilization in plants and plant parts (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) by, for example, increasing the availability of nutrients in plant growth media and fertilizers; p) enhancing plant growth; q) enhancing plant yield; r) reducing the amount(s) of exogenous fertilizer needed to achieve a desired result (e.g., the amount of exogenous phosphorous required to produce X bushels of corn); s) reducing nutrient washout/runoff from plant growth media (e.g., phosphorous washout/runoff from field soil); t) enhancing soil microbiomes; u) stimulating growth and/or proliferation of plant-beneficial microorganisms in plant growth media (e.g., growth and/or proliferation of plant-beneficial diazotrophs, phosphate-solubilizers and/or mycorrhizae); v) enhancing plant root nodulation; w) enhancing plant root mycorrhization; x) enhancing the abilities of plants and plant parts to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; y) reducing disease severity in plants and plant parts affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; z) reducing phytopathogen loads in plant growth media; aa) reducing detrimental effects of pesticide-induced phytotoxicity; bb) enhancing the abilities of plant and plant parts to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; cc) reducing disease severity in plants and plant parts affected by abiotic stresses, such as drought, salinity and extreme temperatures; dd) degrading organic materials in plant growth media and fertilizers; and/or ee) enhancing turnover of organic materials in plant growth media and fertilizers. Compositions of the present disclosure (e.g., proteins, formulations, polynucleotides and organisms of the present disclosure) are suitable for use across a range of environmentally relevant conditions, including, but not limited to, pHs in the range of about 4 to about 9 (e.g., about 4, 4.5, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9) and temperatures in the range of about 15 to about 25 °C (e.g., about 15, 15.5, 16, 16.5, 17, 17.5, 18, 18.5, 19, 19.5, 20, 20.5, 21, 21.5, 22, 22.5, 23, 23.5, 24, 24.5, 25 °C). In some embodiments, one or more compositions of the present disclosure is introduced into a plant growth medium in an amount/concentration effective to: a) enhance one or more properties of said plant growth medium; b) catalyze hydrolysis of one or more phytic acids in said plant growth medium; c) remove phosphate from myo-inositol hexakisphosphates in said plant growth medium; d) remove phosphate from myo-inositol pentakisphosphates in said plant growth medium; e) remove phosphate from myo-inositol tetrakisphosphates in said plant growth medium; f) remove phosphate from myo-inositol trisphosphates in said plant growth medium; g) remove phosphate from myo-inositol diphosphates in said plant growth medium; h) remove phosphate from myo-inositol monophosphates in said plant growth medium; i) produce/release soluble forms of phosphorous in said plant growth medium; j) produce/release soluble forms of minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in said plant growth medium; k) increase nutrient availability in said plant growth medium (e.g., phosphorous, calcium, iron, magnesium, manganese, potassium, zinc availability); l) improve nutrient stability in said plant growth medium (e.g., stabilizing levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in said plant growth medium); m) increase nutrient uptake in a plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) grown in said plant growth medium by, for example, increasing the availability of nutrients in said plant growth medium; n) increase nutrient accumulation in a plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) grown in said plant growth medium by, for example, increasing the availability of nutrients in said plant growth medium; o) increase nutrient utilization in a plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) grown in said plant growth medium by, for example, increasing the availability of nutrients in said plant growth medium; p) enhance the growth of a plant grown in said plant growth medium; q) enhance the yield of a plant grown in said plant growth medium; r) reduce the amount(s) of exogenous fertilizer needed to achieve a desired result (e.g., the amount of exogenous phosphorous required to produce X output from plants grown in said plant growth medium); s) reduce nutrient washout/runoff from said plant growth medium; t) enhance the soil microbiome in said plant growth medium; u) stimulate growth and/or proliferation of plant-beneficial microorganisms in said plant growth medium (e.g., growth and/or proliferation of plant-beneficial diazotrophs, phosphate- solubilizers and/or mycorrhizae); v) enhance plant root nodulation in said plant growth medium; w) enhancing plant root mycorrhization in said plant growth medium; x) enhance the abilities of plants and plant parts grown in said plant growth medium to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; y) reduce disease severity in plants and plant parts grown in said plant growth medium when they are affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; z) reduce phytopathogen loads in said plant growth medium; aa) reduce one or more detrimental effects of pesticide-induced phytotoxicity in plants and plant parts grown in said plant growth medium; bb) enhance the abilities of plant and plant parts grown in said plant growth medium to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; cc) reduce disease severity in plants and plant parts grown in said plant growth medium when they are affected by abiotic stresses, such as drought, salinity and extreme temperatures; dd) degrade one or more organic materials (e.g., plant materials) in said plant growth medium; and/or ee) enhance turnover of one or more organic materials (e.g., plant materials) in said plant growth medium. In some embodiments, one or more compositions of the present disclosure is applied to a plant propagation material (e.g., a seed) in an amount/concentration effective to: a) enhance one or more properties of a plant growth medium into which said plant propagation material is introduced; b) catalyze hydrolysis of one or more phytic acids in a plant growth medium into which said plant propagation material is introduced; c) remove phosphate from myo-inositol hexakisphosphates in a plant growth medium into which said plant propagation material is introduced; d) remove phosphate from myo-inositol pentakisphosphates in a plant growth medium into which said plant propagation material is introduced; e) remove phosphate from myo-inositol tetrakisphosphates in a plant growth medium into which said plant propagation material is introduced; f) remove phosphate from myo-inositol trisphosphates in a plant growth medium into which said plant propagation material is introduced; g) remove phosphate from myo-inositol diphosphates in a plant growth medium into which said plant propagation material is introduced; h) remove phosphate from myo-inositol monophosphates in a plant growth medium into which said plant propagation material is introduced; i) produce/release soluble forms of phosphorous in a plant growth medium into which said plant propagation material is introduced; j) produce/release soluble forms of minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in a plant growth medium into which said plant propagation material is introduced; k) increase nutrient availability in a plant growth medium into which said plant propagation material is introduced (e.g., phosphorous, calcium, iron, magnesium, manganese, potassium, zinc availability); l) improve nutrient stability in a plant growth medium into which said plant propagation material is introduced (e.g., stabilizing levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in plant growth media); m) increase nutrient uptake in said plant propagation material and/or a plant grown from said plant propagation material (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) by, for example, increasing the availability of nutrients in the plant growth medium into which said plant propagation material is introduced; n) increase nutrient accumulation in said plant propagation material and/or a plant grown from said plant propagation material (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) by, for example, increasing the availability of nutrients in the plant growth medium into which said plant propagation material is introduced; o) increase nutrient utilization in said plant propagation material and/or a plant grown from said plant propagation material (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) by, for example, increasing the availability of nutrients in the plant growth medium into which said plant propagation material is introduced; p) enhance the growth of said plant propagation material and/or a plant grown from said plant propagation material; q) enhance the yield of a plant grown from said plant propagation material; r) reduce the amount(s) of exogenous fertilizer needed to achieve a desired result (e.g., the amount of exogenous phosphorous required to produce X yield from a plant grown from said plant propagation material); s) reduce nutrient washout/runoff from a plant growth medium into which said plant propagation material is introduced (e.g., phosphorous washout/runoff from a field soil); t) enhance the soil microbiome in a plant growth medium into which said plant propagation material is introduced; u) stimulate growth and/or proliferation of plant-beneficial microorganisms in a plant growth medium into which said plant propagation material is introduced (e.g., growth and/or proliferation of plant-beneficial diazotrophs, phosphate-solubilizers and/or mycorrhizae); v) enhance root nodulation of a plant grown from said plant propagation material; w) enhance root nodulation of plants grown in a plant growth medium into which said plant propagation material is introduced; x) enhance root mycorrhization a plant grown from said plant propagation material; y) enhance root mycorrhization of plants grown in a plant growth medium into which said plant propagation material is introduced; z) enhance the ability of a plant grown from said plant propagation material to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; aa) enhance the abilities of plants and plant parts grown in a plant growth medium into which said plant propagation material is introduced to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; bb) reduce disease severity in a plant grown from said plant propagation material when it is affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; cc) reduce disease severity in plants and plant parts grown in a plant growth medium into which said plant propagation material is introduced when they are affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; dd) reduce one or more phytopathogen loads in a plant growth medium into which said plant propagation material is introduced; ee) reduce one or more detrimental effects of pesticide-induced phytotoxicity in a plant grown from said plant propagation material; ff) reduce one or more detrimental effects of pesticide-induced phytotoxicity in plants and plant parts grown in a plant growth medium into which said plant propagation material is introduced; gg) enhance the abilities of a plant grown from said plant propagation material to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; hh) enhance the abilities of plants and plants grown in a plant growth medium into which said plant propagation material is introduced to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; ii) reduce disease severity in a plant grown from said plant propagation material when it is affected by abiotic stresses, such as drought, salinity and extreme temperatures; jj) reduce disease severity in plants and plant parts grown in a plant growth medium into which said plant propagation material is introduced when they are affected by abiotic stresses, such as drought, salinity and extreme temperatures; kk) degrade organic materials (e.g. plant materials) in a plant growth medium into which said plant propagation material is introduced; and/or ll) enhance turnover of organic materials (e.g., plant materials) in a plant growth medium into which said plant propagation material is introduced. In some embodiments, one or more compositions of the present disclosure is introduced into a fertilizer in an amount/concentration effective to: a) enhance one or more properties of said fertilizer; b) catalyze hydrolysis of one or more phytic acids in said fertilizer; c) remove phosphate from myo-inositol hexakisphosphates in said fertilizer; d) remove phosphate from myo-inositol pentakisphosphates in said fertilizer; e) remove phosphate from myo-inositol tetrakisphosphates in said fertilizer; f) remove phosphate from myo-inositol trisphosphates in said fertilizer; g) remove phosphate from myo-inositol diphosphates in said fertilizer; h) remove phosphate from myo-inositol monophosphates in said fertilizer; i) produce/release soluble forms of phosphorous in said fertilizer; j) produce/release soluble forms of minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in said fertilizer; k) increase nutrient availability in said fertilizer (e.g., phosphorous, calcium, iron, magnesium, manganese, potassium, zinc availability); l) improve nutrient stability in said fertilizer (e.g., stabilizing levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in said fertilizer); m) increase nutrient uptake in a plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) grown in association with said fertilizer by, for example, increasing the availability of nutrients in said fertilizer; n) increase nutrient accumulation in a plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) grown in association with said fertilizer by, for example, increasing the availability of nutrients in said fertilizer; o) increase nutrient utilization in a plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) grown in the presence of said fertilizer by, for example, increasing the availability of nutrients in said fertilizer; p) enhance the growth of a plant grown in association with said fertilizer; q) enhance the yield of a plant grown in association with said fertilizer; r) reduce the amount(s) of said fertilizer needed to achieve a desired result (e.g., the amount of said fertilizer required to produce X output from plants grown in association with said fertilizer); s) reduce nutrient washout/runoff from said fertilizer; t) enhance the soil microbiome in a plant growth medium into which said fertilizer has been introduced; u) stimulate growth and/or proliferation of plant-beneficial microorganisms in a plant growth medium into which said fertilizer has been introduced (e.g., growth and/or proliferation of plant-beneficial diazotrophs, phosphate-solubilizers and/or mycorrhizae); v) enhance plant root nodulation of plants grown in a plant growth medium into which said fertilizer has been introduced; w) enhancing plant root mycorrhization of plants and plant parts grown in a plant growth medium into which said fertilizer has been introduced; x) enhance the abilities of plants and plant parts grown in a plant growth medium into which said fertilizer has been introduced to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; y) reduce disease severity in plants and plant parts grown in a plant growth medium into which said fertilizer has been introduced when they are affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; z) reduce phytopathogen loads in a plant growth medium into which said fertilizer has been introduced; aa) reduce one or more detrimental effects of pesticide-induced phytotoxicity in plants and plant parts grown in a plant growth medium into which said fertilizer has been introduced; bb) enhance the abilities of plant and plant parts grown in a plant growth medium into which said fertilizer has been introduced to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; cc) reduce disease severity in plants and plant parts grown in a plant growth medium into which said fertilizer has been introduced when they are affected by abiotic stresses, such as drought, salinity and extreme temperatures; dd) degrade one or more organic materials (e.g., plant materials) in a plant growth medium into which said fertilizer has been introduced; and/or ee) enhance turnover of one or more organic materials (e.g., plant materials) in a plant growth medium into which said fertilizer has been introduced. In some embodiments, one or more compositions of the present disclosure is applied to a plant or plant part (e.g., roots) in an amount/concentration effective to: a) enhance one or more properties of a plant growth medium into which said plant or plant part is introduced; b) catalyze hydrolysis of one or more phytic acids in a plant growth medium into which said plant or plant part is introduced; c) remove phosphate from myo-inositol hexakisphosphates in a plant growth medium into which said plant or plant part is introduced; d) remove phosphate from myo-inositol pentakisphosphates in a plant growth medium into which said plant or plant part is introduced; e) remove phosphate from myo-inositol tetrakisphosphates in a plant growth medium into which said plant or plant part is introduced; f) remove phosphate from myo-inositol trisphosphates in a plant growth medium into which said plant or plant part is introduced; g) remove phosphate from myo- inositol diphosphates in a plant growth medium into which said plant or plant part is introduced; h) remove phosphate from myo-inositol monophosphates in a plant growth medium into which said plant or plant part is introduced; i) produce/release soluble forms of phosphorous in a plant growth medium into which said plant or plant part introduced; j) produce/release soluble forms of minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in a plant growth medium into which said plant or plant part is introduced; k) increase nutrient availability in a plant growth medium into which said plant or plant part is introduced (e.g., phosphorous, calcium, iron, magnesium, manganese, potassium, zinc availability); l) improve nutrient stability in a plant growth medium into which said plant or plant part is introduced (e.g., stabilizing levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in plant growth media); m) increase nutrient uptake in said plant or plant part and/or a plant grown from said plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) by, for example, increasing the availability of nutrients in the plant growth medium into which said plant or plant part is introduced; n) increase nutrient accumulation in said plant or plant part and/or a plant grown from said plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) by, for example, increasing the availability of nutrients in the plant growth medium into which said plant or plant part is introduced; o) increase nutrient utilization in said plant or plant part and/or a plant grown from said plant or plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) by, for example, increasing the availability of nutrients in the plant growth medium into which said plant or plant part is introduced; p) enhance the growth of said plant or plant part; q) enhance the yield of said plant or plant part; r) reduce the amount(s) of exogenous fertilizer needed to achieve a desired result (e.g., the amount of exogenous phosphorous required to produce X yield from said plant or plant part); s) reduce nutrient washout/runoff from a plant growth medium into which said plant or plant part is introduced (e.g., phosphorous washout/runoff from a field soil); t) enhance the soil microbiome in a plant growth medium into which said plant or plant part is introduced; u) stimulate growth and/or proliferation of plant-beneficial microorganisms in a plant growth medium into which said plant or plant part is introduced (e.g., growth and/or proliferation of plant-beneficial diazotrophs, phosphate-solubilizers and/or mycorrhizae); v) enhance root nodulation of said plant or plant part; w) enhance root nodulation of plants grown in a plant growth medium into which said plant or plant part is introduced; x) enhance root mycorrhization of said plant or plant part; y) enhance root mycorrhization of plants grown in a plant growth medium into which said plant or plant part is introduced; z) enhance the ability of said plant or plant part to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; aa) enhance the abilities of other plants and plant parts grown in a plant growth medium into which said plant or plant part is introduced to resist infestations/infections of/by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; bb) reduce disease severity in a said plant or plant part when it is affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; cc) reduce disease severity in other plants and plant parts grown in a plant growth medium into which said plant or plant part is introduced when they are affected by phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; dd) reduce one or more phytopathogen loads in a plant growth medium into which said plant or plant part is introduced; ee) reduce one or more detrimental effects of pesticide-induced phytotoxicity in said plant or plant part; ff) reduce one or more detrimental effects of pesticide-induced phytotoxicity in other plants and plant parts grown in a plant growth medium into which said plant or plant part is introduced; gg) enhance the abilities of said plant or plant part to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; hh) enhance the abilities of other plants and plants grown in a plant growth medium into which said plant or plant part is introduced to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; ii) reduce disease severity in said plant or plant part when it is affected by abiotic stresses, such as drought, salinity and extreme temperatures; jj) reduce disease severity in other plants and plant parts grown in a plant growth medium into which said plant or plant part is introduced when they are affected by abiotic stresses, such as drought, salinity and extreme temperatures; kk) degrade organic materials (e.g., plant materials) in a plant growth medium into which said plant or plant part is introduced; and/or ll) enhance turnover of organic materials (e.g., plant materials) in a plant growth medium into which said plant or plant part is introduced. In preferred embodiments, the composition introduced into the plant growth medium and/or applied to the plant propagation material comprises one or more of the proteins described above. The present disclosure encompasses methods of using one or more compositions of the present disclosure for enhancing the environments in which plants are grown by, for example, changing the pH of the environment, increasing the availability of nutrients, stimulating plant-beneficial microorganisms and/or suppressing/eliminating harmful microorganisms. The present disclosure encompasses methods of using one or more compositions of the present disclosure for improving plant growth, development and/or yield characteristics by, for example, increasing nutrient availability, increasing nutrient uptake, improving nutrient uptake efficiency, improving water use efficiency, stimulating the production of plant growth promoters, stimulating plant defense mechanisms, and/or preventing, treating, suppressing, eliminating and/or reducing the severity of pest infestations/infections. The present disclosure encompasses methods of using one or more compositions of the present disclosure for increasing the availability of one or more nutrients by, for example, fixing atmospheric nitrogen, retaining nitrogen in different oxidation stages, mineralizing organic phosphate, solubilizing phosphate, releasing organic acids, and/or solubilizing micronutrients. For example, introducing an enzyme of the present disclosure into soil in the vicinity of a plant may increase the bioavailability of one or more vitamins, macrominerals, micronutrients, organic acids and/or trace minerals, as compared to a control soil lacking said enzyme. Phosphate bioavailability may be increased with myriad compositions of the present disclosure, including, but not limited to, proteins exhibiting one or more activities belonging to EC 3.1.3 (e.g., EC 3.1.3.8, EC 3.1.3.26, EC 3.1.3.72), (and corresponding formulations, polynucleotides and organisms). In some embodiments, phosphate bioavailability is increased using one or more of SEQ ID NO(s): 1–3, 7–19, 21–35, 37–46, 48–50, 52–107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162–177, 179–253, 255–261, 263–271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416–480, and enzymatically active fragments/mutants/variants thereof. Compositions of the present disclosure may be applied to / used to treat any plant type, including, but not limited to, row crops and vegetables. In some embodiments, compositions of the present disclosure are formulated for the treatment of one or more plants selected from the families Amaranthaceae (e.g., chard, spinach, sugar beet, quinoa), Asteraceae (e.g., artichoke, asters, chamomile, chicory, chrysanthemums, dahlias, daisies, echinacea, goldenrod, guayule, lettuce, marigolds, safflower, sunflowers, zinnias), Brassicaceae (e.g., arugula, broccoli, bok choy, Brussels sprouts, cabbage, cauliflower, canola, collard greens, daikon, garden cress, horseradish, kale, mustard, radish, rapeseed, rutabaga, turnip, wasabi, watercress, Arabidopsis thaliana), Caricaceae (e.g., papaya), Cucurbitaceae (e.g., cantaloupe, cucumber, honeydew, melon, pumpkin, squash (e.g., acorn squash, butternut squash, summer squash), watermelon, zucchini), Fabaceae (e.g., alfalfa, beans, carob, clover, guar, lentils, mesquite, peas, peanuts, soybeans, tamarind, tragacanth, vetch), Malvaceae (e.g., cacao, cotton, durian, hibiscus, kenaf, kola, okra), Poaceae (e.g., bamboo, barley, corn, fonio, lawn grass (e.g., Bahia grass, Bermudagrass, bluegrass, Buffalograss, Centipede grass, Fescue, or Zoysia), millet, oats, ornamental grasses, rice, rye, sorghum, sugar cane, triticale, wheat and other cereal crops, Polygonaceae (e.g., buckwheat), Rosaceae (e.g., almonds, apples, apricots, blackberry, blueberry, cherries, peaches, plums, quinces, raspberries, roses, strawberries), Rutaceae (e.g., curry, grapefruit, lemon, lime, kumquat, mandarin, orange), Solanaceae (e.g., bell peppers, chili peppers, eggplant, petunia, potato, tobacco, tomato) and Vitaceae (e.g., grape). Non-limiting examples of plants and plant parts (e.g., plant propagation materials) that may be treated with compositions of the present disclosure include plants sold under the ACCELERON®, AGRIPRO®, AGRISURE®, AGROESTE®, AGVENTURE®, ALFOREX™, ASGROW®, AQUAMAX®, BOLLGARD II™, BOLLGARD™ 3, BREVANT™, CHANNEL™, CONFIDOR™, CORTEVA AGRISCIENCE™, CORVUS™, CREDENZ®, CROPSTAR™, DAIRYLAND™, DEKALB®, DELTAPINE™, DERUITER™, DROUGHTGARD®, ENLIST E3®, ENOGEN®, FIBERMAX®, GAUCHO™, GENUITY®, GOLDENHARVEST®, HOEGEMEYER™, INTACTA RR2 PRO™, INVIGOR®, LIBERTY LINK®, NEXGROW®, NK®, NUTECH SEED®, OPTIMUM®, PHYTOGEN®, PIONEER®, QROME®, RIB COMPLETE®, ROUNDUP READY®, ROUNDUP READY 2 YIELD®, ROUNDUP READY 2 XTEND®, SEMETES AGROCERES™, SEMINIS™, SMARTSTAX®, STONEVILLE®, SYNGENTA®, TRUFLEX™, VT DOUBLE PRO®, VT TRIPLE PRO®, YIELDGARD®, YIELDGARD VT ROOTWORM/RR2®, YIELDGARD VT TRIPLE® and/or XTENDFLEX™ tradenames. Compositions of the present disclosure may be applied to any part/portion of a plant. In some embodiments, the compositions are applied to plant propagation materials (e.g., cuttings, rhizomes, seeds and tubers). In some embodiments, the compositions are applied to the roots of a plant. In some embodiments, the compositions are applied to the foliage of a plant. In some embodiments, the compositions are applied to both the roots and the foliage of a plant. In some embodiments, the compositions are applied to plant propagation materials and to the plants that grow from said plant propagation materials. Compositions of the present disclosure may be applied to any plant growth medium, including, but not limited to, soil. Compositions of the present disclosure may be applied to plants, plant parts and/or plant growth media in any suitable manner, including, but not limited to, on-seed application, in-furrow application and foliar application. Compositions of the present disclosure may be applied using any suitable method(s), including, but not limited to, coating, dripping, dusting, encapsulating, fogging, immersing, spraying, and soaking. Batch systems, in which predetermined batch sizes of material and composition are delivered into a mixer, may be employed. Continuous treatment systems, which are calibrated to apply composition at a predefined rate in proportion to a continuous flow of material, may also be employed. In some embodiments, compositions of the present disclosure are applied directly to plant propagation material (e.g., seeds). According to some embodiments, plant propagation materials are soaked in a composition of the present disclosure for at least 0.1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1, 1.25, 1.5, 1.75, 2, 3, 4, 5, 6, 9, 12, 15, 18, 21, 24, 36, 48 hours. According to some embodiments, plant propagation materials are coated with the compositions. Plant propagation materials may be coated with one or more additional layers (e.g., one or more protective layers that serve to enhance the stability and/or activity of an enzyme/organism of the present disclosure and/or one or more sequestration layers comprising substances that may reduce the stability and/or activity of an enzyme/organism of the present disclosure if included in the same layer as the enzyme/organism of the present disclosure). In some embodiments, the coating comprises, consists essentially of, or consists of a composition of the present disclosure and a drying powder. In some embodiments, compositions of the present disclosure are applied directly to a plant growth medium (e.g., a soil). According to some embodiments, the compositions are applied in the vicinity of a plant propagation material (e.g., a seed). According to some embodiments, the compositions are applied to the root zone of a plant. According to some embodiments, the compositions are applied using a drip irrigation system. In some embodiments, compositions of the present disclosure are applied directly to plants. According to some embodiments, the compositions are fogged, misted, sprayed and/or sprinkled onto the plant(s) to be treated (e.g., foliar sprays). In some embodiments, compositions of the present disclosure are applied to harvested plants and/or plant parts. Individual components of the compositions (e.g., proteins of the present disclosure and chemical pesticides) may be applied separately or together. For example, in some embodiments, compositions of the present disclosure may be incorporated into integrated pest management strategies (e.g., a formulation comprising one or more proteins of the present disclosure may be applied to an orchard/vineyard as part of an integrated pest management strategy that includes separate applications of 2, 3, 4, 5 or more distinct pesticides in a rotation designed to reduce/prevent chemical pesticide-induced phytotoxicity and/or pest resistance). In some embodiments, compositions of the present disclosure are freeze- spray- or spray-freeze-dried and then applied to plants/plant parts. For examples, in some embodiments, a formulation comprising and enzyme/organism of the present disclosure and one or more stabilizing components (e.g., one or more maltodextrins having a DEV of about 15 to about 20) is freeze- spray- or spray-freeze-dried, mixed with a drying powder (e.g., a drying powder comprising calcium stearate, attapulgite clay, montmorillonite clay, graphite, magnesium stearate, silica (e.g., fumed silica, hydrophobically- coated silica and/or precipitated silica) and/or talc), then coated on seed that was been pre-treated with one or more adhesives (e.g., an adhesive composition comprising one or more maltodextrins, one or more mono-, di- or oligosaccharides, one or more peptones, etc.), one or more pesticides and/or one or more plant signal molecules (e.g., one or more LCOs). See, generally, e.g., US 11472981; US 2020/0085065; US 10820594. Compositions of the present disclosure may be applied to plant growth media (e.g., soil), plants, and plant parts (e.g., plant propagation materials) at any time, including, but not limited to, prior to planting, at the time of planting, after planting, prior to germination, at the time of germination, after germination, prior to seedling emergence, at the time of seedling emergence, after seedling emergence, prior to the vegetative stage, during the vegetative stage, after the vegetative stage, prior to the reproductive stage, during the reproductive stage, after the reproductive stage, prior to flowering, at the time of flowering, after flowering, prior to fruiting, at the time of fruiting, after fruiting, prior to ripening, at the time of ripening, after ripening, prior to harvest, at the time of harvest, and after harvesting. In some embodiments, compositions of the present disclosure are applied to plant growth media prior to introducing a plant into the plant growth media (e.g., prior to planting seed). In some embodiments, compositions of the present disclosure are applied to plant growth media concurrently with the introduction of a plant into the plant growth media (e.g., at the time of planting). In some embodiments, compositions of the present disclosure are applied to plant growth media after introducing a plant into the plant growth media (e.g., by drip irrigation following planting). In some embodiments, compositions of the present disclosure are applied to plant propagation materials (e.g., seeds) about/at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 28, 32, 36, 40, 44, 48, 52, 56, 60, 64, 68, 72, 76, 80, 84, 88, 92, 96, 100, 104 weeks prior to planting. In some embodiments, compositions of the present disclosure are applied to plant propagation materials (e.g., seeds) at the time of planting. In some embodiments, compositions of the present disclosure are applied to plant propagation materials (e.g., seeds) after planting but before germination. In some embodiments, compositions of the present disclosure are applied to plants following emergence. In some embodiments, compositions of the present disclosure are applied to a plant or plant part pre-harvest (i.e., within 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or more days before the plant or plant part is (to be) harvested). Compositions of the present disclosure may be applied to plants, plant parts and/or plant growth media in any suitable amount(s)/concentration(s). In some embodiments, compositions of the present disclosure comprise one or more proteins of the present disclosure in an amount ranging from about 0.001 to about 100 milligrams per gram and/or milliliter of composition. For example, compositions of the present disclosure may comprise about/at least 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100 milligrams of protein per gram and/or milliliter of composition. In some embodiments, compositions of the present disclosure comprise about/at least 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, or 0.5 milligrams of protein per gram and/or milliliter of composition. In some embodiments, one or more proteins of the present disclosure comprise about 0.00000001 to about 95% (by weight) of the composition. In some embodiments, one or more proteins of the present disclosure comprise about/at least 1 x 10^-15, 1 x 10^-14, 1 x 10^-13, 1 x 10^-12, 1 x 10^-11, 1 x 10^-10, 1 x 10^-9, 1 x 10^-8, 1 x 10^-7, 1 x 10^-6, 1 x 10^-5, 1 x 10^-4, 1 x 10- ³, 1 x 10^-2, 1 x 10^-1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95% or more (by weight) of the composition. In some embodiments, the composition is applied at a rate that is equivalent to about 1 x 10¹ to about 1 x 10¹⁵ phytase activity units (at optimum conditions) of each protein of the present disclosure per kilogram of plant propagation material. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure the plant propagation materials are coated with about/at least 1 x 10¹, 1 x 10², 1 x 10³, 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 1 x 10¹⁰, 1 x 10¹¹, 1 x 10¹², 1 x 10¹³, 1 x 10¹⁴ or 1 x 10¹⁵ phytase activity units (at optimum conditions) of each protein of the present disclosure per kilogram of plant propagation material. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure that an average of about/at least 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 1 x 10¹⁰, 1 x 10¹¹, or 1 x 10¹² phytase activity units (at optimum conditions) of each protein of the present disclosure is applied to each seed. In some embodiments, the composition is applied at a rate that is equivalent to about 1 x 10¹ to about 1 x 10¹⁵ phytase activity units (at optimum conditions) of each protein of the present disclosure per plant. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure each plant is treated with about/at least 1 x 10¹, 1 x 10², 1 x 10³, 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 1 x 10¹⁰, 1 x 10¹¹, 1 x 10¹², 1 x 10¹³, 1 x 10¹⁴ or 1 x 10¹⁵ phytase activity units (at optimum conditions) of each protein of the present disclosure. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure that an average of about/at least 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 1 x 10¹⁰, 1 x 10¹¹, or 1 x 10¹² phytase activity units (at optimum conditions) of each protein of the present disclosure is applied to each plant. In some embodiments, the composition is applied at a rate that is equivalent to about 1 x 10¹ to about 1 x 10¹⁵ phytase activity units (at optimum conditions) of each protein of the present disclosure per hectare/acre of treated crops. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure each hectare/acre of treated crops is treated with about/at least 1 x 10¹, 1 x 10², 1 x 10³, 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 1 x 10¹⁰, 1 x 10¹¹, 1 x 10¹², 1 x 10¹³, 1 x 10¹⁴ or 1 x 10¹⁵ phytase activity units (at optimum conditions) of each protein of the present disclosure. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure that an average of about/at least 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 1 x 10¹⁰, 1 x 10¹¹, or 1 x 10¹² phytase activity units (at optimum conditions) of each protein of the present disclosure is applied to each hectare/acre of treated crops. In some embodiments, the composition is applied at a rate that is equivalent to about 1 x 10¹ to about 1 x 10¹⁵ phytase activity units (at optimum conditions) of each protein of the present disclosure per hectare/acre of plant growth media. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure each hectare/acre of plant growth media is treated with about/at least 1 x 10¹, 1 x 10², 1 x 10³, 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 1 x 10¹⁰, 1 x 10¹¹, 1 x 10¹², 1 x 10¹³, 1 x 10¹⁴ or 1 x 10¹⁵ phytase activity units (at optimum conditions) of each protein of the present disclosure. According to some embodiments, compositions of the present disclosure are are applied in an amount sufficient to ensure that an average of about/at least 1 x 10⁴, 1 x 10⁵, 1 x 10⁶, 1 x 10⁷, 1 x 10⁸, 1 x 10⁹, 1 x 10¹⁰, 1 x 10¹¹, or 1 x 10¹² phytase activity units (at optimum conditions) of each protein of the present disclosure is applied to each hectare/acre of plant growth media. In some embodiments, the composition is applied at a rate that is equivalent to about 0.001 to about 100 milligrams of protein of the present disclosure per kilogram of plant propagation material. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure the plant propagation materials are coated with about/at least 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100 milligrams of protein of the present disclosure per kilogram of plant propagation material. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure that an average of about/at least 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, or 0.5 milligrams of protein of the present disclosure is applied to each seed. In some embodiments, the composition is applied at a rate that is equivalent to about 0.001 to about 100 milligrams of protein of the present disclosure per plant. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure each plant is treated with about/at least 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100 milligrams of protein of the present disclosure. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure that an average of about/at least 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, or 0.5 milligrams of protein of the present disclosure are applied to each plant. In some embodiments, the composition is applied at a rate that is equivalent to about 0.001 to about 100 milligrams of protein of the present disclosure per hectare/acre of treated crops. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure each hectare/acre of treated crops is treated with about/at least 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100 milligrams of protein of the present disclosure. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure that an average of about/at least 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, or 0.5 milligrams of protein of the present disclosure are applied to each hectare/acre of treated crops. In some embodiments, the composition is applied at a rate that is equivalent to about 0.001 to about 100 milligrams of protein of the present disclosure per hectare/acre of plant growth media. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure each hectare/acre of plant growth media is treated with about/at least 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100 milligrams of protein of the present disclosure. According to some embodiments, compositions of the present disclosure are applied in an amount sufficient to ensure that an average of about/at least 0.05, 0.06, 0.07, 0.08, 0.09, 0.1, 0.15, 0.2, 0.25, 0.3, 0.35, 0.4, 0.45, or 0.5 milligrams of protein of the present disclosure are applied to each hectare/acre of plant growth media. In some embodiments, compositions of the present disclosure are applied at a rate of about 0.05 to about 100 milliliters and/or grams of composition per kilogram of plant propagation material. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure the plant propagation materials are coated with about/at least 0.05, 0.1, 0.125, 0.15, 0.175, 0.2, 0.225, 0.2.5, 0.275, 0.3, 0.325, 0.35, 0.375, 0.4, 0.425, 0.45, 0.475, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9, 9.5, 10, 20, 30, 40, 50, 60, 70, 80, 90 or 100 milliliters and/or grams of compositions per kilogram of plant propagation material. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure that an average of about/at least 0.05, 0.1, 0.125, 0.15, 0.175, 0.2, 0.225, 0.2.5, 0.275, 0.3, 0.325, 0.35, 0.375, 0.4, 0.425, 0.45, 0.475, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75 or 5 milliliters and/or grams of composition is applied to each seed. In some embodiments, compositions of the present disclosure are applied at a rate of about 0.5 to about 100 milliliters and/or grams of composition per plant. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure each plant is treated with about/at least 0.05, 0.1, 0.125, 0.15, 0.175, 0.2, 0.225, 0.2.5, 0.275, 0.3, 0.325, 0.35, 0.375, 0.4, 0.425, 0.45, 0.475, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9, 9.5, 10, 20, 30, 40, 50, 60, 70, 80, 90 or 100 milliliters and/or grams of composition. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure that an average of about/at least 0.05, 0.1, 0.125, 0.15, 0.175, 0.2, 0.225, 0.2.5, 0.275, 0.3, 0.325, 0.35, 0.375, 0.4, 0.425, 0.45, 0.475, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75 or 5 milliliters and/or grams of composition is applied to each plant. In some embodiments, compositions of the present disclosure are applied at a rate of about 0.5 to about 100 milliliters and/or grams of composition per hectare/acre of treated crops. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure each hectare/acre of treated crops is treated with about/at least 0.05, 0.1, 0.125, 0.15, 0.175, 0.2, 0.225, 0.2.5, 0.275, 0.3, 0.325, 0.35, 0.375, 0.4, 0.425, 0.45, 0.475, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9, 9.5, 10, 20, 30, 40, 50, 60, 70, 80, 90 or 100 milliliters and/or grams of composition. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure that an average of about/at least 0.05, 0.1, 0.125, 0.15, 0.175, 0.2, 0.225, 0.2.5, 0.275, 0.3, 0.325, 0.35, 0.375, 0.4, 0.425, 0.45, 0.475, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75 or 5 milliliters and/or grams of composition is applied to each hectare/acre of treated crops. In some embodiments, compositions of the present disclosure are applied at a rate of about 0.5 to about 100 milliliters and/or grams of composition per hectare/acre of plant growth media. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure each hectare/acre of plant growth media is treated with about/at least 0.05, 0.1, 0.125, 0.15, 0.175, 0.2, 0.225, 0.2.5, 0.275, 0.3, 0.325, 0.35, 0.375, 0.4, 0.425, 0.45, 0.475, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9, 9.5, 10, 20, 30, 40, 50, 60, 70, 80, 90 or 100 milliliters and/or grams of composition. According to some embodiments, one or more compositions of the present disclosure is/are applied in an amount sufficient to ensure that an average of about/at least 0.05, 0.1, 0.125, 0.15, 0.175, 0.2, 0.225, 0.2.5, 0.275, 0.3, 0.325, 0.35, 0.375, 0.4, 0.425, 0.45, 0.475, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75 or 5 milliliters and/or grams of composition is applied to each hectare/acre of plant growth media. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to a) enhance a plant growth environment; b) catalyze hydrolysis of phytic acids in a plant growth medium; c) remove phosphate from myo- inositol hexakisphosphates in a plant growth medium; d) remove phosphate from myo-inositol pentakisphosphates in a plant growth medium; e) remove phosphate from myo-inositol tetrakisphosphates in a plant growth medium; f) remove phosphate from myo-inositol trisphosphates in a plant growth medium; g) remove phosphate from myo-inositol diphosphates in a plant growth medium; h) remove phosphate from myo-inositol monophosphates in a plant growth medium; i) produce/release soluble forms of phosphorous in a plant growth medium; j) produce/release soluble forms of one or more minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in a plant growth medium; k) increase nutrient availability in a plant growth medium (e.g., phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc availability); l) improve nutrient stability in a plant growth medium (e.g., stabilize levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in a plant growth medium); m) increase nutrient uptake (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) in a plant or plant part; n) increase nutrient accumulation (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) in a plant or plant part; o) increase nutrient utilization (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) in a plant or plant part; p) enhance plant growth; q) enhance plant yield; r) reduce the amount(s) of exogenous fertilizer needed to achieve a desired result (e.g., the amount of exogenous phosphorous required to produce a desired crop yield); s) reduce nutrient washout/runoff from a plant growth medium (e.g., phosphorous washout/runoff from a field soil); t) enhance a soil microbiome; u) stimulate growth and/or proliferation of one or more plant-beneficial microorganisms in a plant growth medium (e.g., growth and/or proliferation of plant-beneficial diazotrophs, phosphate-solubilizers and/or mycorrhizae in a field soil); v) enhance plant root nodulation; w) enhance plant root mycorrhization; x) enhance the ability of a plant or plant part to resist infestation/infection of/by one or more phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; y) reduce disease severity in a plant or plant part affected by one or more phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; z) reduce one or more phytopathogen loads in a plant growth medium; aa) reduce one or more detrimental effects of a pesticide-induced phytotoxicity; bb) enhance the ability of a plant or plant part to tolerate one or more abiotic stresses, such as drought, salinity and extreme temperatures; cc) reduce disease severity in a plant or plant part affected by one or more abiotic stresses, such as drought, salinity and extreme temperatures; dd) degrade one or more organic materials (e.g., plant materials) in a plant growth medium; and/or ee) enhance turnover of one or more organic materials (e.g., plant materials) in a plant growth medium. In some embodiments, the composition is applied at a rate sufficient to increase one or more desired effect(s) (e.g., phytic acid hydrolysis and/or plant growth/yield) by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, the composition is applied at a rate sufficient to decrease one or more undesired effect(s) (e.g., detrimental effects of phytotoxicity, infestation/infection and/or abiotic stress) by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100%, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to increase phytic acid hydrolysis by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to increase the amount/concentration of soluble phosphorous in a plant growth medium by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to increase the amount/concentration of a soluble cationic mineral, such as calcium, copper, iron, magnesium, manganese, potassium and/or zinc, in a plant growth medium by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to increase nutrient availability, uptake and/or accumulation, optionally phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc availability, uptake and/or accumulation, in a plant or plant part by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to increase nutrient utilization, optionally phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc utilization, in a plant or plant part by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to enhance one or more plant growth and/or development characteristics, optionally biomass, carbohydrate biosynthesis, chlorophyll content, cold tolerance, drought tolerance, height, leaf length, leaf mass, leaf number, leaf surface area, leaf volume, nutrient uptake (e.g., calcium, magnesium, nitrogen, phosphorous and/or potassium uptake), rate(s) of photosynthesis, root area, root diameter, root length, root mass, root nodulation (e.g., nodule mass, nodule number, nodule volume), root number, root surface area, root volume, salt tolerance, seed germination, seedling emergence, shoot diameter, shoot length, shoot mass, shoot number, shoot surface area, shoot volume, spread, stomatal conductance and/or survival rate, by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to enhance one or more plant yield characteristics, optionally biomass, bushels per acre, grain weight per plot (GWTPP), nutritional content, percentage of plants in a given area (e.g., plot) that fail to produce grain, yield at standard moisture percentage (YSMP), yield per plot (YPP) and/or yield reduction (YRED), by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to reduce the amount(s) of exogenous fertilizer, optionally exogenous boron, calcium, carbon, copper, iron, magnesium, manganese, molybdenum, nitrogen, phosphorous, potassium, sulfur and/or zinc, needed to achieve a desired result by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100%, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to reduce nutrient washout and/or runoff, optionally boron, calcium, carbon, copper, iron, magnesium, manganese, molybdenum, nitrogen, phosphorous, potassium, sulfur and/or zinc washout and/or runoff, by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100%, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to increase the growth and/or proliferation of one or more microorganisms, optionally one or more diazotrophs, mycorrhizae and/or phosphate- solubilizing microorganisms, in a plant growth medium by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to increase root mycorrhization by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to reduce one or more aspects of disease severity (e.g., one or more symptoms in a plant or plant part infested/infected by a phytopathogenic pest and/or one or more symptoms of abiotic stress) by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to enhance the ability of a plant or plant part to resist infestation/infection by one or more phytopathogenic pests by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to reduce the rate of infestation/infection by one or more phytopathogenic pests by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to reduce the amount/concentration of one or more phytopathogenic pests in a plant growth medium by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to enhance the ability of a plant or plant part to tolerate one or more abiotic stresses, optionally drought, salinity and/or extreme temperature, by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to reduce one or more symptoms of abiotic stress (e.g., chlorosis, defoliation, dieback, discoloration, necrosis, stunted growth, wilting) by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to increase degradation and/or turnover of organic materials, optionally organic plant materials, in a plant growth medium by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230, 235, 240, 245, 250% or more, as compared to an untreated control. In some embodiments, compositions of the present disclosure are applied at a rate sufficient to reduce one or more symptoms of pesticide-induced phytotoxicity (e.g., leaf browning, chlorosis, cupping, curling, discoloration, necrosis, speckling, twisting and/or wilting, stunted growth, premature leaf drop) by about/at least 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100% or more, as compared to an untreated control. The present disclosure extends to plant growth media, plants, and plant parts (e.g., plant propagation materials) and that have been treated with a composition of the present disclosure (e.g., plant propagation materials coated with a formulation comprising one or more enzymes of the present disclosure, plants sprayed with a formulation comprising one or more enzymes of the present disclosure, harvested plant parts coated with a formulation comprising one or more enzymes of the present disclosure), to plants grown from plant propagation materials that were treated with a composition of the present disclosure, to plant parts harvested from plants that have been treated with a composition of the present disclosure, to plant parts harvested from plants grown from plant propagation materials that were treated with a composition of the present disclosure, to crops comprising a plurality of plants that were treated with a composition of the present disclosure, to crops comprising a plurality of plants grown from plant propagation materials that were treated with a composition of the present disclosure, to crops treated with a composition of the present disclosure, to processed products derived from plants that were treated with a composition of the present disclosure, to processed products derived from plants grown from plant parts that were treated with a composition of the present disclosure, and to processed products treated with a composition of the present disclosure. The present disclosure encompasses coated plant propagation materials comprising, consisting essentially of, or consisting of a plant propagation material and a coating that covers at least a portion of the outer surface of the plant propagation material, said coating comprising, consisting essentially of, or consisting of one or more compositions of the present disclosure. In some embodiments, the coating comprises two, three, four, five or more layers. According to some embodiments, the coating comprises an inner layer that contains one or more proteins of the present disclosure and one or more outer layers free or substantially free of proteins of the present disclosure. In some embodiments, the coating comprises an inner layer that is a composition of the present disclosure and an outer layer that is equivalent to a composition of the present disclosure except that it does not contain proteins of the present disclosure. In some embodiments, the coating comprises, consists essentially of, or consists of a composition of the present disclosure and a drying powder. Drying powders may be applied in any suitable amount(s)/concentration(s). The absolute value of the amount/concentration that is/are sufficient to cause the desired effect(s) may be affected by factors such as the type, size and volume of material to which the composition will be applied, the type(s) of proteins in the composition, the number of proteins in the composition, the stability of the proteins in the composition and storage conditions (e.g., temperature, relative humidity, duration). Those skilled in the art will understand how to select an effective amount/concentration using routine dose-response experiments. Guidance for the selection of appropriate amounts/concentrations can be found, for example, in International Patent Application Nos. PCT/US2016/050529 and PCT/US2016/050647 and U.S. Provisional Patent Application Nos. 62/296,798; 62/271,857; 62/347,773; 62/343,217; 62/296,784; 62/271,873; 62/347,785; 62/347,794; and 62/347,805. In some embodiments, the drying powder is applied in an amount ranging from about 0.5 to about 10 grams of drying powder per kilogram of plant propagation material. For example, in some embodiments, about 0.5, 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, 3, 3.25, 3.5, 3.75, 4, 4.25, 4.5, 4.75, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9, 9.5, 10 grams or more of drying powder (e.g., drying powder comprising magnesium stearate, magnesium sulfate, powdered milk, silica, soy lecithin and/or talc) is applied per kilogram of seed. In some embodiments, a drying powder comprising calcium stearate, attapulgite clay, montmorillonite clay, graphite, magnesium stearate, silica (e.g., fumed silica, hydrophobically-coated silica and/or precipitated silica) and/or talc is applied to seeds coated with a composition of the present disclosure at a rate of about 1, 1.25, 1.5, 1.75, 2, 2.25, 2.5, 2.75, or 3 grams per kilogram of seed. In some embodiments, the coating completely covers the outer surface of the plant propagation material. In some embodiments, the average thickness of the coating is at least 1.5, 1.6, 1.7, 1.8, 1.9, 2.0, 2.1, 2.2, 2.3, 2.4, 2.5, 2.6, 2.7, 2.8, 2.9, 3.0, 3.1, 3.2, 3.3, 3.4, 3.5, 4, 4.5, 5 µm or more. In some embodiments, the average thickness of the coating is about 1.5 to about 3.0 µm. The present disclosure extends to kits comprising, consisting essentially of, or consisting of one or more plants and/or plant parts (e.g., coated plant propagation materials) that have been treated with the compositions of the present disclosure and a container housing the treated plant(s) and/or plant part(s). In some embodiments, the kit further comprises one or more oxygen scavengers, such as activated carbon, ascorbic acid, iron powder, mixtures of ferrous carbonate and metal halide catalysts, sodium chloride and/or sodium hydrogen carbonate. The container may comprise any suitable material(s), including, but not limited to, materials that reduce the amount of light, moisture and/or oxygen that contact the coated plant propagation material when the container is sealed. In some embodiments, the container comprises, consists essentially of, or consists of a material having light permeability of less than about 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70 or 75%. In some embodiments, the container comprises, consists essentially of, or consists of a material having an oxygen transmission rate of less than about 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 60, 70, 80, 90, 100, 125, 150, 175, 200, 225, 250, 275, 300, 325, 350, 375, 400, 425, _{450, 475, or 500 cm} ^{3/m2·day (as measured in accordance with ASTM D3985).} In some embodiments, the container reduces the amount of ambient light that reaches said coated plant propagation material by about 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100% when sealed. In some embodiments, the container reduces the amount of ambient moisture that reaches said plant propagation material by about 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100% when sealed. In some embodiments, the container reduces the amount of ambient oxygen that reaches said plant propagation material by about 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100% when sealed. In some embodiments, kits of the present disclosure comprise 1, 2, 3, 4, 5 or more additional containers. The additional containers may comprise any suitable component(s) or composition(s), including, but not limited to, adhesives, anti-freezing agents, anti-settling agents, biostimulants, chemical actives, dispersants, drying agents, effect pigments, emulsifiers, growth media, microbial extracts, nutrients, pest attractants and feeding stimulants, pH control components, plant-beneficial microorganisms, plant signal molecules, preservatives, rain fasteners, rhealogical agents, safeners, seed flowability agents, stabilizing agents, UV protectants and wetting agents. Examples of adhesives, anti-freezing agents, anti- settling agents, biostimulants, chemical actives, dispersants, drying agents, effect pigments, emulsifiers, growth media, microbial extracts, nutrients, pest attractants and feeding stimulants, pH control components, plant-beneficial microorganisms, plant signal molecules, preservatives, rain fasteners, rhealogical agents, safeners, seed flowability agents, stabilizing agents, UV protectants and wetting agents that may be included in the additional containers are described above. The present disclosure also extends to kits comprising, consisting essentially of, or consisting of one or more compositions of the present disclosure and instructions for using the same. For example, in some embodiments, kits of the present disclosure include instructions for applying enzymatically active proteins and formulations of the present disclosure to a plant, plant part and/or plant growth medium. As noted above, proteins of the present disclosure may be formulated into compositions comprising a variety of components, such as adhesives, anti-freezing agents, anti-settling agents, biostimulants, chemical actives, dispersants, drying agents, effect pigments, emulsifiers, growth media, microbial extracts, nutrients, pest attractants and feeding stimulants, pH control components, plant-beneficial microorganisms, plant signal molecules, preservatives, rain fasteners, rhealogical agents, safeners, seed flowability agents, stabilizing agents, UV protectants and wetting agents. It is to be understood that compositions and methods of the present disclosure may likewise be used in combination with such components as separate and distinct compositions (as part of an integrated pest management strategy, for example). It is to be understood that compositions and methods of the present disclosure may be combined with known compositions and methods, such as fertilization compositions/methods, inoculant compositions/methods, pesticide compositions/methods, and post-harvest compositions/methods. In some instances, compositions and methods of the present disclosure are used as part of an Integrated Pest Management program/strategy. According to some embodiments, one or more proteins, organisms and/or formulations of the present disclosure is/are applied to a plant, plant part or plant growth medium as part of an Integrated Pest Management program/strategy comprising one or more biological pesticides and/or one or more chemical pesticides. The following is a non-exhaustive listing of concepts and embodiments encompassed by the present disclosure: Use of a composition of the present disclosure (e.g., a protein or formulation of the present disclosure) for any one, two, three, four, five, six, seven, eight, nine, ten or more of the following: 1) treating (e.g., drenching, fogging, misting, spraying) a plant growth medium; 2) improving one or more soil characteristics; 3) enhancing a plant growth environment; 4) catalyzing hydrolysis of a phytic acid in a plant growth medium; 5) removing phosphate from a myo-inositol hexakisphosphate in a plant growth medium; 6) removing phosphate from a myo-inositol pentakisphosphate in a plant growth medium; 7) removing phosphate from a myo-inositol tetrakisphosphate in a plant growth medium; 8) removing phosphate from a myo-inositol trisphosphate in a plant growth medium; 9) removing phosphate from a myo-inositol diphosphate in a plant growth medium; 10) removing phosphate from a myo-inositol monophosphate in a plant growth medium; 11) producing/releasing a soluble form of phosphorous in a plant growth medium; 12) producing/releasing one or more soluble minerals, optionally a soluble calcium, copper, iron, magnesium, manganese, potassium and/or zinc, in a plant growth medium; 13) improving nutrient availability, optionally, phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc availability, in a plant growth medium; 14) improving nutrient stability, optionally phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc stability, in a plant growth medium; 15) increasing nutrient uptake, optionally phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake, in a plant or plant part by, for example, increasing the availability of nutrients in a plant growth medium; 16) improving nutrient accumulation, optionally phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation, in a plant or plant part by, for example, increasing the availability of nutrients in a plant growth medium; 17) increasing nutrient utilization, optionally phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization, in a plant or plant part by, for example, increasing the availability of nutrients in a plant growth medium; 18) enhancing plant growth; 19) enhancing plant yield; 20) reducing the need for exogenous fertilizer; 21) reducing an amount(s) of exogenous fertilizer needed to achieve a desired result, optionally an amount of exogenous phosphorous required to produce a desired crop yield; 22) reducing nutrient washout/runoff from a plant growth medium, optionally phosphorous washout/runoff from a field soil; 23) enhancing a soil microbiome; 24) stimulating growth and/or proliferation of one or more plant-beneficial microorganisms, optionally one or more diazotrophs, phosphate-solubilizing microorganisms and/or mycorrhizae, in a plant growth medium; 25) enhancing plant root nodulation; 26) enhancing plant root mychorrhization; 27) treating (e.g., coating, dipping, drenching, fogging, misting, soaking, spraying) a plant or plant part; 28) enhancing an ability of a plant or plant part to resist infestations/infections of/by one or more phytopathogenic pests, optionally one or more arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes protozoa, viruses and/or weeds; 29) reducing one or more aspects of disease severity in a plant or plant part affected by one or more phytopathogenic pests, optionally one or more arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes protozoa, viruses and/or weeds; 30) reducing a phytopathogen load in a plant growth medium; 31) inclusion as part of an Integrated Pest Management program/strategy, optionally an Integrated Pest Management program/strategy comprising one or more chemical pesticides; 32) reducing one or more detrimental effects of pesticide-induced phytotoxicity in a plant or plant part; 33) enhancing the abilities of a plant or plant part to tolerate abiotic stresses, such as drought, salinity and extreme temperatures; 34) reducing disease severity in a plant or plant part affected by abiotic stresses, such as drought, salinity and extreme temperatures; 35) degrading one or more organic materials, optionally one or more plant materials, in a plant growth medium; 36) enhancing turnover of one or more organic materials, optionally one or more plant materials, in a plant growth medium. Any of the foregoing uses in which any one, two, three, four, five, six, seven, eight, nine, ten or more of the following is true: 1) the composition comprises, consists essentially of or consists of an enzyme; 2) the composition comprises, consists essentially of or consists of an enzyme belonging to EC 3; 3) the composition comprises, consists essentially of or consists of an enzyme belonging to EC 3.1.3; 4) the composition comprises, consists essentially of or consists of an enzyme belonging to EC 3.1.3.26; 5) the composition comprises, consists essentially of or consists of one or more polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of any one or more of SEQ ID NOs: 1–3 and 7– 480, wherein the three-dimensional structure is determined using AlphaFold; 6) the composition comprises, consists essentially of or consists of one or more polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to any one or more of SEQ ID NOs: 1–3 and 7–480; 7) the composition comprises, consists essentially of or consists of one or more polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to any one or more of SEQ ID NOs: 1–3 and 7–480; 8) the composition comprises, consists essentially of or consists of one or more polypeptides encoded by a polynucleotide having about/at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to any one or more of SEQ ID NO(s): 4–6 or the cDNA sequence thereof; ) the composition comprises, consists essentially of or consists of one or more polypeptides derived from any one of SEQ ID NO(s): 1–3, 7–19, 21–35, 37–46, 48–50, 52–107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162– 177, 179–253, 255–261, 263–271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416–480 by substitution, deletion, or insertion of one or more amino acids; 0) the composition comprises, consists essentially of or consists of one or more polypeptides derived from any one of 5) through 9) wherein the N- and/or C-terminal end has been extended by the addition of one or more amino acids;1) the composition comprises, consists essentially of or consists of an enzymatically active fragment/mutant/variant of any one of 5) through 10); 2) the composition comprises a fusion protein comprising a first polypeptide and a second polypeptide wherein at least one of said first and second polypeptides is a protein of the present disclosure; 3) the composition comprises 2, 3, 4, 5, 6, 7, 8, 9, 10 or more proteins of the present disclosure; 4) the composition is an aqueous enzyme solution, optionally an aqueous enzyme solution comprising, consisting essentially of or consisting of water, one or more proteins of the present disclosure and one or more preservatives (e.g., potassium sorbate, sodium benzoate, 1,2-benzisothiazolin-3-one) and/or stabilizing agents (e.g., glycerol, potassium chloride, propylene glycol, sodium chloride, sorbitol); 5) the composition comprises an agronomically acceptable carrier; 6) the composition comprises a seed-compatible carrier; 7) the composition comprises a foliar-compatible carrier; 8) the composition comprises a soil-compatible carrier; 9) the composition comprises one or more adhesives (stickers), optionally one or more disaccharides (e.g., sucrose), gums and/or maltodextrins; 0) the composition comprises one or more plant-beneficial agents; 1) the composition comprises one or more microorganisms; 2) the composition comprises one or more diazotrophs; 3) the composition comprises one or more phosphate-solubilizing microorganisms; 4) the composition comprises one or more mycorrhizae; 5) the composition comprises one or more bacteria, optionally one or more Alkalihalobacillus, Azospirillum, Bacillus, Bradyrhizobium, Campylobacter, Chryseobacterium, Citrobacter, Clostridium, Cronobacter, Dicytoglomus, Effusibacillus, Enterococcus, Erwinia, Escherichia, Flavobacterium, Fusobacterium, Geobacillus, Helicobacter, Ilyobacter, Kosakonia, Lactobacillus, Lactococcus, Lederbergia, Lysinibacillus, Lysobacter, Neisseria, Neobacillus, Nocardiopsis, Oceanobacillus, Paenibacillus, Pseudomonas, Rhizobium, Salmonella, Sinorhizobium, Staphylococcus, Streptococcus, Streptomyces, Sutcliffiella, Ureaplasma and/or Yersinia; 6) the composition comprises one or more fungi, optionally one or more Acremonium, Acrophialophora, Aspergillus, Aureobasidium, Bjerkandera, Ceriporiopsis, Chaetomium, Chrysosporium, Colletotrichum, Coprinopsis, Coprinus, Coriolus, Cryphonectria, Cryptococcus, Evansstolkia, Filibasidium, Fusarium, Gliocladium, Glomus, Humicola, Magnaporthe, Metarhizium, Microdochium, Mucor, Myceliophthora, Neocallimastix, Neurospora, Ostropa, Paecilomyces, Penicillium, Peniophora, Phlebia, Piromyces, Pleurotus, Podospora, Pseudoplectania, Schizophyllum, Sodiomyces, Stenocarpella, Talaromyces, Thermoascus, Themochaetoides, Thermomyces, Thermothielavioides, Thermothelomyces, Thielavia, Tolypocladium, Trametes, Trichoderma, Trichophaea and/or Urnula; ) the composition comprises one or more yeast, optionally one or more Candida, Hansenula, Komagataella, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces and/or Yarrowia; ) the composition comprises one or more plant cells, optionally one or more Amaranthaceae, Asteraceae, Brassicaceae, Caricaceae, Cucurbitaceae, Fabaceae, Malvaceae, Poaceae, Polygonaceae, Rosaceae, Rutaceae, Solanaceae and/or Vitaceae cells; ) the composition comprises one or more biological pesticides, optionally one or more biological acaricides, biological bactericides, biological fungicides, biological gastropodicides, biological herbicides, biological insecticides, biological miticides, biological nematicides, biological oomyceticides and/or biological protozoacides; ) the composition comprises one or more chemical pesticides, optionally one or more chemical acaricides, chemical bactericides, chemical fungicides, chemical gastropodicides, chemical herbicides, chemical insecticides, chemical miticides, chemical nematicides, chemical oomyceticides and/or chemical protozoacides; ) the composition comprises one or more microbial pesticides, optionally one or more microbial acaricides, microbial bactericides, one or more microbial fungicides, microbial gastropodicides, microbial herbicides, microbial insecticides, microbial miticides, microbial nematicides, microbial oomyceticides and/or microbial protozoacides;) the composition comprises one or more dispersants, optionally one or more alcohol ethoxylates and/or polyvinylpyrrolidones; ) the composition comprises one or more drying agents; ) the composition comprises one or more nutrients, optionally one or more organic acids (e.g., acetic acid, citric acid, lactic acid, malic acid, taurine, etc.), macrominerals (e.g., phosphorous, calcium, magnesium, potassium, sodium, iron, etc.), trace minerals (e.g., boron, cobalt, chloride, chromium, copper, fluoride, iodine, manganese, molybdenum, selenium, zinc, etc.), and/or vitamins (e.g., vitamin A, vitamin B complex (i.e., vitamin B1, vitamin B2, vitamin B3, vitamin B₅, vitamin B₆, vitamin B₇, vitamin B₈, vitamin B₉, vitamin B₁₂, choline) vitamin C, vitamin D, vitamin E, vitamin K, carotenoids (α-carotene, β-carotene, cryptoxanthin, lutein, lycopene, zeaxanthin, etc.); ) the composition comprises one or more pest attractants; ) the composition comprises one or more pest feeding stimulants; ) the composition comprises one or more pH control components; ) the composition has a pH within the operable range for each enzyme therein; ) the composition has a pH within +/- 1 pH-unit of the optimal pH for at least one enzyme therein; ) the composition has a pH within +/- 1 pH-unit of the optimal pH for each enzyme therein; ) the composition has a pH of about 2 to about 9; ) the composition has a pH of about 2 to about 8.5; ) the composition has a pH of about 2 to about 8; ) the composition has a pH of about 2 to about 7.5; ) the composition has a pH of about 2 to about 7; ) the composition has a pH of about 2 to about 6.5; ) the composition has a pH of about 2 to about 6; ) the composition has a pH of about 2 to about 5.5; ) the composition has a pH of about 2 to about 5; ) the composition has a pH of about 2 to about 4.5; ) the composition has a pH of about 2 to about 4; ) the composition has a pH of about 2 to about 3.5; ) the composition has a pH of about 2 to about 3; ) the composition has a pH of about 2 to about 2.5; ) the composition has a pH of about 2.5 to about 9; ) the composition has a pH of about 2.5 to about 8.5;) the composition has a pH of about 2.5 to about 8;) the composition has a pH of about 2.5 to about 7.5;) the composition has a pH of about 2.5 to about 7;) the composition has a pH of about 2.5 to about 6.5;) the composition has a pH of about 2.5 to about 6;) the composition has a pH of about 2.5 to about 5.5;) the composition has a pH of about 2.5 to about 5;) the composition has a pH of about 2.5 to about 4.5;) the composition has a pH of about 2.5 to about 4;) the composition has a pH of about 2.5 to about 3.5;) the composition has a pH of about 2.5 to about 3;) the composition has a pH of about 3 to about 9;) the composition has a pH of about 3 to about 8.5;) the composition has a pH of about 3 to about 8;) the composition has a pH of about 3 to about 7.5;) the composition has a pH of about 3 to about 7;) the composition has a pH of about 3 to about 6.5;) the composition has a pH of about 3 to about 6;) the composition has a pH of about 3 to about 5.5;) the composition has a pH of about 3 to about 5;) the composition has a pH of about 3 to about 4.5;) the composition has a pH of about 3 to about 4;) the composition has a pH of about 3 to about 3.5;) the composition has a pH of about 3.5 to about 9;) the composition has a pH of about 3.5 to about 8.5;) the composition has a pH of about 3.5 to about 8;) the composition has a pH of about 3.5 to about 7.5;) the composition has a pH of about 3.5 to about 7;) the composition has a pH of about 3.5 to about 6.5;) the composition has a pH of about 3.5 to about 6;) the composition has a pH of about 3.5 to about 5.5;) the composition has a pH of about 3.5 to about 5;) the composition has a pH of about 3.5 to about 4.5;) the composition has a pH of about 3.5 to about 4;) the composition has a pH of about 4 to about 9;) the composition has a pH of about 4 to about 8.5;) the composition has a pH of about 4 to about 8;) the composition has a pH of about 4 to about 7.5;) the composition has a pH of about 4 to about 7;) the composition has a pH of about 4 to about 6.5;) the composition has a pH of about 4 to about 6;) the composition has a pH of about 4 to about 5.5;) the composition has a pH of about 4 to about 5; ) the composition has a pH of about 4 to about 4.5;) the composition has a pH of about 4.5 to about 9;) the composition has a pH of about 4.5 to about 8.5;) the composition has a pH of about 4.5 to about 8;) the composition has a pH of about 4.5 to about 7.5;) the composition has a pH of about 4.5 to about 7;) the composition has a pH of about 4.5 to about 6.5;) the composition has a pH of about 4.5 to about 6;) the composition has a pH of about 4.5 to about 5.5;) the composition has a pH of about 4.5 to about 5;) the composition has a pH of about 5 to about 9;) the composition has a pH of about 5 to about 8.5;) the composition has a pH of about 5 to about 8;) the composition has a pH of about 5 to about 7.5;) the composition has a pH of about 5 to about 7;) the composition has a pH of about 5 to about 6.5;) the composition has a pH of about 5 to about 6;) the composition has a pH of about 5 to about 5.5;) the composition has a pH of about 5.5 to about 8.5;) the composition has a pH of about 5.5 to about 8;) the composition has a pH of about 5.5 to about 7.5;) the composition has a pH of about 5.5 to about 7;) the composition has a pH of about 5.5 to about 6.5;) the composition has a pH of about 5.5 to about 6;) the composition has a pH of about 6 to about 9;) the composition has a pH of about 6 to about 8.5;) the composition has a pH of about 6 to about 8;) the composition has a pH of about 6 to about 7.5;) the composition has a pH of about 6 to about 7;) the composition has a pH of about 6 to about 6.5;) the composition has a pH of about 6.5 to about 9;) the composition has a pH of about 6.5 to about 8.5;) the composition has a pH of about 6.5 to about 8;) the composition has a pH of about 6.5 to about 7.5;) the composition has a pH of about 6.5 to about 7;) the composition has a pH of about 7 to about 9;) the composition has a pH of about 7 to about 8.5;) the composition has a pH of about 7 to about 8;) the composition has a pH of about 7 to about 7.5;) the composition has a pH of about 7.5 to about 9;) the composition has a pH of about 7.5 to about 8.5;) the composition has a pH of about 7.5 to about 8;) the composition has a pH of about 8 to about 9;) the composition has a pH of about 8 to about 8.5; ) the composition has a pH of about 8.5 to about 9; ) the composition has a pH of less than 3; ) the composition has a pH of more than 3; ) the composition has a pH of less than 4; ) the composition has a pH of more than 4; ) the composition has a pH of less than 5; ) the composition has a pH of more than 5; ) the composition has a pH of less than 6; ) the composition has a pH of more than 6; ) the composition has a pH of less than 6.5; ) the composition has a pH of more than 6.5; ) the composition has a pH of less than 7; ) the composition has a pH of more than 7; ) the composition has a pH of less than 7.5; ) the composition has a pH of more than 7.5; ) the composition has a pH of less than 8; ) the composition has a pH of more than 8; ) the composition has a pH of less than 9; ) the composition comprises one or more postharvest treatments; ) the composition comprises one or more essential oils; ) the composition comprises one or more ethylene biosynthesis inhibitors; ) the composition comprises one or more cyclopropenes; ) the composition comprises one or more waxes; ) the composition comprises one or more preservatives; ) the composition comprises one or more benzoates (e.g., sodium benzoate); ) the composition comprises benzoic acid; ) the composition comprises methyl paraben; ) the composition comprises phenoxy ethanol; ) the composition comprises one or more proprionates (e.g., ammonium proprionate, calcium proprionate, sodium proprionate); ) the composition comprises proprionic acid; ) the composition comprises one or more sorbates (e.g., potassium sorbate, sodium sorbate); ) the composition comprises 1,2-benzisothiazolin-3-one (PROXEL®; Basel, Switzerland); ) the composition comprises one or more rain fasteners; ) the composition comprises one or more organo-modified siloxanes; ) the composition comprises one or more trisiloxanes; ) the composition comprises one or more polysiloxanes; ) the composition comprises one or more rhealogical agents; ) the composition comprises one or more safeners; ) the composition comprises one or more stabilizing agents, optionally one or more boric acid derivatives, inorganic salts, lactic acid, polyols, sugars, sugar alcohols and/or reversible protease inhibitors; ) the composition comprises boric acid; ) the composition comprises glycerol; ) the composition comprises one or more UV protectants, optionally one or more aromatic amino acids, carotenoids, cinnamates, lignosulfonates, melanins, mycosporines, polyphenols and/or salicylates; ) the composition comprises one or more wetting agents, optionally one or more naphthalene sulfonates; ) the composition is applied prior to planting; ) the composition is applied at the time of planting; ) the composition is applied after planting; ) the composition is applied prior to germination; ) the composition is applied at the time of germination; ) the composition is applied after germination; ) the composition is applied prior to seedling emergence; ) the composition is applied at the time of seedling emergence; ) the composition is applied after seeding emergence; ) the composition is applied prior to vegetative stage; ) the composition is applied during vegetative stage; ) the composition is applied after vegetative stage; ) the composition is applied prior to reproductive stage; ) the composition is applied during reproductive stage; ) the composition is applied after reproductive stage; ) the composition is applied prior to flowering; ) the composition is applied at the time of flowering; ) the composition is applied after flowering; ) the composition is applied prior to fruiting; ) the composition is applied at the time of fruiting; ) the composition is applied after fruiting; ) the composition is applied prior to ripening; ) the composition is applied at the time of ripening; ) the composition is applied after ripening; ) the composition is applied prior to pruning; ) the composition is applied at the time of pruning; ) the composition is applied after pruning; ) the composition is applied prior to harvest; ) the composition is used in combination with one or more adhesives; ) the composition is used in combination with one or more plant-beneficial agents; ) the composition is used in combination with one or more microorganisms; ) the composition is used in combination with one or more diazotrophs; ) the composition is used in combination with one or more phosphate-solubilizing microorganisms; ) the composition is used in combination with one or more mycorrhizae; ) the composition is used in combination with one or more bacteria, optionally one or more Alkalihalobacillus, Azospirillum, Bacillus, Bradyrhizobium, Campylobacter, Citrobacter Chryseobacterium, Clostridium, Cronobacter, Dicytoglomus, Effusibacillus, Enterococcus, Erwinia, Escherichia, Flavobacterium, Fusobacterium, Geobacillus, Helicobacter, Ilyobacter, Kosakonia, Lactobacillus, Lactococcus, Lederbergia, Lysinibacillus, Lysobacter, Neisseria, Neobacillus, Nocardiopsis, Oceanobacillus, Paenibacillus, Pseudomonas, Rhizobium, Salmonella, Sinorhizobium, Staphylococcus, Streptococcus, Streptomyces, Sutcliffiella, Ureaplasma and/or Yersinia; 222) the composition is used in combination with one or more fungi, optionally one or more Acremonium, Acrophialophora, Aspergillus, Aureobasidium, Bjerkandera, Ceriporiopsis, Chaetomium, Chrysosporium, Colletotrichum, Coprinopsis, Coprinus, Coriolus, Cryphonectria, Cryptococcus, Evansstolkia, Filibasidium, Fusarium, Gliocladium, Glomus, Humicola, Magnaporthe, Metarhizium, Microdochium, Mucor, Myceliophthora, Neocallimastix, Neurospora, Ostropa, Paecilomyces, Penicillium, Peniophora, Phlebia, Piromyces, Pleurotus, Podospora, Pseudoplectania, Schizophyllum, Sodiomyces, Stenocarpella, Talaromyces, Thermoascus, Themochaetoides, Thermomyces, Thermothielavioides, Thermothelomyces, Thielavia, Tolypocladium, Trametes, Trichoderma, Trichophaea and/or Urnula; 223) the composition is used in combination with one or more yeast, optionally one or more Candida, Hansenula, Komagataella, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces and/or Yarrowia; 224) the composition is used in combination with one or more biological pesticides, optionally one or more biological acaricides, biological bactericides, biological fungicides, biological gastropodicides, biological herbicides, biological insecticides, biological miticides, biological nematicides, biological oomyceticides and/or biological protozoacides; 225) the composition is used in combination with one or more chemical pesticides, optionally one or more chemical acaricides, chemical bactericides, chemical fungicides, chemical gastropodicides, chemical herbicides, chemical insecticides, chemical miticides, chemical nematicides, chemical oomyceticides and/or chemical protozoacides; 226) the composition is used in combination with one or more microbial pesticides, optionally one or more microbial acaricides, microbial bactericides, one or more microbial fungicides, microbial gastropodicides, microbial herbicides, microbial insecticides, microbial miticides, microbial nematicides, microbial oomyceticides and/or microbial protozoacides; 227) the composition is used in combination with one or more plant growth regulators; 228) the composition is used in combination with one or more rain fasteners; 229) the composition is used in combination with one or more organo-modified siloxanes; 230) the composition is used in combination with one or more trisiloxanes; 231) the composition is used in combination with one or more polysiloxanes; 232) the composition is used in combination with one or more preharvest treatments; 233) the composition is used in combination with one or more postharvest treatments; 234) the composition is used in combination with one or more essential oils; 235) the composition is used in combination with one or more ethylene biosynthesis inhibitors; 236) the composition is used in combination with one or more cyclopropenes; 237) the composition is used in combination with one or more waxes; 238) the composition is used in combination with one or more stabilizing agents, optionally one or more boric acid derivatives, inorganic salts, lactic acid, polyols, sugars, sugar alcohols and/or reversible protease inhibitors; 239) the composition is used in combination with one or more UV protectants, optionally one or more aromatic amino acids, carotenoids, cinnamates, lignosulfonates, melanins, mycosporines, polyphenols and/or salicylates; 240) the composition is used in combination with one or more wetting agents, optionally one or more naphthalene sulfonates Transgenic microorganisms, plants or plant parts for which any one, two, three, four, five, six, seven, eight, nine, ten or more of the following are true: 1) comprises one or more polynucleotides encoding a polypeptide having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of any one or more of SEQ ID NOs: 1–3 and 7–480, wherein the three- dimensional structure is determined using AlphaFold; ) comprises one or more polynucleotides encoding a polypeptide having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to any one or more of SEQ ID NOs: 1–3 and 7–480; ) comprises one or more polynucleotides encoding a polypeptide having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4. 85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to any one or more of SEQ ID NOs: 1–3 and 7–480; ) comprises one or more polynucleotides encoding a polypeptide derived from any one of SEQ ID NO(s): 1–3, 7–19, 21–35, 37–46, 48–50, 52–107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162–177, 179–253, 255–261, 263– 271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416– 480 by substitution, deletion, or insertion of one or more amino acids; ) comprises one or more polynucleotides encoding a polypeptide derived from the polypeptide of any one of 1) through 4) wherein the N- and/or C-terminal end has been extended by the addition of one or more amino acids; ) comprises one or more polynucleotides encoding an enzymatically active fragment/mutant/variant of the polypeptide of any one of 1) through 5); ) comprises one or more polynucleotides encoding a fusion protein comprising a first polypeptide and a second polypeptide wherein at least one of said first and second polypeptides is a protein of the present disclosure; ) comprises one or more polynucleotides encoding 2, 3, 4, 5, 6, 7, 8, 9, 10 or more proteins of the present disclosure;) comprises one or more polynucleotide having about/at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to any one or more of SEQ ID NO(s): 4–6 or the cDNA sequence thereof; 0) expresses one or more polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.850.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three- dimensional structure of any one or more of SEQ ID NOs: 1–3 and 7–480, wherein the three-dimensional structure is determined using AlphaFold; 1) expresses one or more polypeptides having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to any one or more of SEQ ID NOs: 1–3 and 7–480; 2) expresses one or more polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to any one or more of SEQ ID NOs: 1–3 and 7–480; 3) expresses one or more polypeptides derived from any one of SEQ ID NO(s): 1–3, 7–19, 21–35, 37–46, 48–50, 52– 107, 109–122, 124–126, 128–138, 140–156, 158, 160, 162–177, 179–253, 255–261, 263–271, 273–275, 277–288, 290–321, 323–336, 338–340, 342–358, 360–367, 369–388, 3901–391, 393–414, and 416–480 by substitution, deletion, or insertion of one or more amino acids; 14) expresses one or more polypeptides derived from the polypeptide of any one of 10) through 13) wherein the N- and/or C-terminal end has been extended by the addition of one or more amino acids; 15) expresses an enzymatically active fragment/mutant/variant of the polypeptide of any one of 10) through 14); 16) expresses a fusion protein comprising a first polypeptide and a second polypeptide wherein at least one of said first and second polypeptides is a protein of the present disclosure; 17) expresses 2, 3, 4, 5, 6, 7, 8, 9, 10 or more proteins of the present disclosure. EXAMPLES The following examples are provided to illustrate certain embodiments and are not to be construed as limiting the inventive concepts described in the present disclosure. Enzyme treatments are described in the corresponding Figures with reference to the predominant enzyme(s) comprised therein. It is to be understood that enzyme treatments may possess other enzymatic activities not expressly disclosed in the corresponding Figures. For example, an enzyme treatment having a predominant phytase activity may exhibit lesser side activities, such as one or more phosphatase activities (e.g., alkaline phosphatase activity belonging to EC 3.1.3.1, acid phosphatase activity belonging to EC 3.1.3.2, etc.). Example 1 Exemplary Polypeptide Sequences of the Present Disclosure <SEQ ID NO: 1; AA; Peniophora lycii> QLPIPAQNTSNWGPYSPFFPVEPYAAPPEGCTVTQVNLIQRHGARWPTSGARSRQVAAVAKIQMARPFTDPKYEFLNDFVY TFGVADLLPFGANQSYQTGTDMYTRYSTLFEGGDVPFVRAAGDQRVVDSSTNWTAGFGDASGETVLPTLQVVLQEEGNCTL CNNMCPNWVKGDESTTWLGVFAPNITARLNAAAPSANLSDSDALTLMDMCPFDTLSSGNASPFCDLFTAEEYTSYEYYYDL DKYYGTGPGNALGPVQGVGYVNELLARLTGQAVRDETQTNRTLDSDPATFPLNRTFYADFSHDNTMVAIFAALGLFNATAL DPLKPDENRLWVVSKLVPFSGHMTVEKLACSGKEAVRVLVNDAVQPLEFCGGVDGVCELSAFVESQTYARENGQGDFAKCG FVPSE <SEQ ID NO: 2; AA; Citrobacter braakii> EEQNGMKLERVVIVSRHGVRAPTKFTPIMKCVTPDQWPQWDVPLGWLTPRGCELVSYLGQYQRLWFTSKGLLPNQTCPSPG QVAVIADTDQRTRKTGECFLAGLAPKCQIQVHYQKDEEKPDPLFNPVKMGKCQFNTLQVCNAILERAGGNIELFTQRYQSS FRTLENVLNFSQSECCKTTEKSTKCTLPEALPSELKCTPDLVSLTGAWSLSSTLTEIFLLQEAQGMPQVAWGRITGEKEWR DLLSLHNAQFDLLQRTPEVARSRATPLLDLIDTALLTNGTTENRYGIKLPVSLLFIAGHDTNLANLSGALDLNWSLPGQPD NTPPGGELVFEKWKRTSDNTDWVQVSFVYQTLRDMRDIQPLSLEKPAGKVDLKLIACEEKNSQGMCSLKSFSRLIKEIRVP ECAVTE <SEQ ID NO: 3; AA; Citrobacter braakii > EEQNGMKLERVVIVSRHGVRAPTKFTPIMKNVTPDQWPQWDVPLGWLTPRGGELVSELGQYQRLWFTSKGLLNNQTCPSPG QVAVIADTDQRTRKTGEAFLAGLAPKCQIQVHYQKDEEKNDPLFNPVKMGKCSFNTLQVKNAILERAGGNIELYTQRYQSS FRTLENVLNFSQSETCKTTEKSTKCTLPEALPSELKVTPDNVSLPGAWSLSSTLTEIFLLQEAQGMPQVAWGRITGEKEWR DLLSLHNAQFDLLQRTPEVARSRATPLLDMIDTALLTNGTTENRYGIKLPVSLLFIAGHDTNLANLSGALDLNWSLPGQPD NTPPGGELVFEKWKRTSDNTDWVQVSFVYQTLRDMRDIQPLSLEKPAGKVDLKLIACEEKNSQGMCSLKSFSRLIKEIRVP ECAVTE Example 2 Determination of Phytase Activity 75 microliter phytase-containing enzyme solution, appropriately diluted in 0.25M sodium acetate, 0.005% (w/v) Tween-20, pH5.5, is dispensed in a microtiter plate well, e. g. NUNC 269620, and 75 microliter substrate is added (prepared by dissolving 100mg sodium phytate from rice (Aldrich Cat.No.274321 ) in 10ml 0.25M sodium acetate buffer, pH5.5). The plate is sealed and incubated 15min. shaken with 750rpm at 37°C. After incubation, 75 microliter stop reagent is added (the stop reagent being prepared by mixing 10 ml molybdate solution (10% (w/v) ammonium hepta- molybdate in 0.25% (w/v) ammonia solution), 10ml ammonium vanadate (0.24% commercial product from Bie&Berntsen, Cat.No. LAB17650), and 20ml 21.7% (w/v) nitric acid), and the absorbance at 405nm is measured in a microtiter plate spectrophotometer. The phytase activity is expressed in the unit of FYT, one FYT being the amount of enzyme that liberates 1 micromole inorganic ortho-phosphate per minute under the conditions above. An absolute value for the measured phytase activity may be obtained by reference to a standard curve prepared from appropriate dilutions of inorganic phosphate, or by reference to a standard curve made from dilutions of a phytase enzyme preparation with known activity (such standard enzyme preparation with a known activity is available on request from Novozymes A/S, Krogshoejvej 36, DK-2880 Bagsvaerd). Example 3 Fertilizer Granules Treated with SEQ ID NO: 1 or SEQ ID NO: 3 Exhibited Robust Phytase Activity Fertilizer granules were treated with a 1% w/w dose of a solution comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 1 or SEQ ID NO: 3, air dried, then stored in the dark at 25°C. Weekly samples were taken to evaluate enzymatic activity over an eight-week testing period. Enzymes were extracted from granule samples via incubation in a pH 5.5 buffer for 20 minutes with gentle shaking. Following centrifugation, each supernatant was collected, diluted, spiked with sodium phytate, and then incubated for 1 hour at 37°C. The phosphate concentration within each supernatant was quantified using the Ascorbic Acid Method (Soil Science Society of America, Inc. & American Society of Agronomy, Inc., METHODS OF SOIL ANALYSIS: PART 3 CHEMICAL METHODS, 1996) modified for micro-titer plate quantification. Enzyme activity was calculated as the difference between enzyme-treated granules and untreated control granules. Relative enzyme activity was calculated as activity measured at timepoint, t, divided by the measured activity of a freshly prepared sample x 100. Fertilizer granules treated with the enzymatically active protein comprising SEQ ID NO: 1 retained more than 70% activity throughout the eight-week test period. Fertilizer granules treated with the enzymatically active protein comprising SEQ ID NO: 3 retained more than 70% activity for up to three weeks. Example 4 Liquid Fertilizers Treated with SEQ ID NO: 1 or SEQ ID NO: 3 Exhibited Robust Phytase Activity Liquid fertilizers were treated with a 1% by volume dose of a solution comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 1 or SEQ ID NO: 3, sealed, then stored in the dark at 25°C. Weekly samples were taken to evaluate enzymatic activity over an eight-week testing period. Samples were diluted with a pH 5.5 buffer, spiked with sodium phytate, and then incubated for 1 hour at 37°C. The phosphate concentration within each sample was quantified using the Ascorbic Acid Method (Soil Science Society of America, Inc. & American Society of Agronomy, Inc., METHODS OF SOIL ANALYSIS: PART 3 CHEMICAL METHODS, 1996) modified for micro-titer plate quantification. Enzyme activity was calculated as the difference between enzyme-treated granules and untreated control granules. Relative enzyme activity was calculated as activity measured at timepoint, t, divided by the measured activity of a freshly prepared sample x 100. Liquid fertilizers treated with the enzymatically active protein comprising SEQ ID NO: 1 retained more than 70% activity throughout the eight-week test period. Liquid fertilizers treated with the enzymatically active protein comprising SEQ ID NO: 3 retained more than 70% activity throughout the eight-week test period. Example 5 Corn Plants Grown in Soil Treated with SEQ ID NO: 1 Exhibited Improved Growth & Nutrient Uptake Half-gallon pots were prepared with a custom soil mixture containing sand, soil, calcined clay particles, and a commercial potting media in a 40:20:20:20 ratio. Twenty pots were prepared for each treatment with two hybrid corn seeds planted to a depth of 3 cm in each pot (later thinned to 1 plant per pot). A liquid composition comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 1 was applied at a rate equivalent to 10 oz/ac (i.e., 1.3 mL was mixed with 82 mL DI water and applied at a rate of 0.631 mL/seed); untreated control plants were treated with an equivalent amount of DI water. Pots were placed in a modified Latin square design to control for spatial variation and watered daily. Greenhouse conditions were set to achieve a 15:10 photoperiod with average daytime and nighttime temperatures of 24°C and 20°C, respectively. When plants reached the V8 growth stage the shoots were cut at the soil surface, placed in a paper bag, and dried at 80°C for at least 5 days before weighing. After weighing, plants were submitted to Midwest labs (Omaha, NE) for nutrient analysis. Statistical analysis was performed using JMP 15.0.0 (2019) software using a mixed effects model in which the row and column (room placement) were designated as random effects. Treatment with the enzymatically active protein comprising SEQ ID NO: 1 resulted in a 6.6% increase in shoot dry weight and a 24.7% increase in iron (Fe) content, as compared to the untreated control plants (p-values of 0.02 and 0.07, respectively). Plants grown in soil treated with the enzymatically active protein comprising SEQ ID NO: 1 also exhibited increased boron (B), magnesium (Mg) and manganese (Mn) content—5.9%, 3.4% and 5.3%, respectively—but those results were not deemed to be statistically significant (i.e., p-values were higher than 0.1). Example 6 Soybean Plants Grown in Soil Treated with SEQ ID NO: 1 Exhibited Improved Growth & Nutrient Uptake Half-gallon pots were prepared with a custom soil mixture containing sand, soil, calcined clay particles, and a commercial potting media in a 40:20:20:20 ratio. Seventeen pots were prepared for each treatment with two soybean seeds planted to a depth of 3 cm in each pot (later thinned to 1 plant per pot). Soybean seeds were treated with Bradyrhizobium japonicum at a rate of 1⁶ colony forming units per seed prior to planting to ensure that plants would not experience N stress over the course of the study. A liquid composition comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 1 was applied at a rate equivalent to 10 oz/ac (i.e., 1.3 mL was mixed with 82 mL DI water and applied at a rate of 0.631 mL/seed); untreated control plants were treated with an equivalent amount of DI water. Pots were placed in a modified Latin square design to control for spatial variation and watered daily. Greenhouse conditions were set to achieve a 15:10 photoperiod with average daytime and nighttime temperatures of 22°C and 17°C, respectively. When plants reached the R2 growth stage the shoots were cut at the soil surface, placed in a paper bag, and dried at 80°C for at least 5 days before weighing. Soil was washed from roots, nodules were counted, then roots were placed in individual paper bags and also dried at 80°C for at least 5 days before weighing. After weighing, plant shoots were submitted to Midwest labs (Omaha, NE) for nutrient analysis. Statistical analysis was performed using JMP 15.0.0 (2019) software using a mixed effects model in which the row and column (room placement) were designated as random effects. The experiment was repeated three times. In all three studies, plants grown in soil treated with the enzymatically active protein comprising SEQ ID NO: 1 exhibited enhanced growth and/or increased nutrient (iron, magnesium, manganese, nitrogen, phosphorous, potassium, sulfur and/or zinc) content, as compared to the untreated control plants. Table 1 describes all results deemed to be statistically significant (p≤0.1). Table 1. Statistically Significant Changes in Plant Growth & Nutrient Uptake Example 7 Liquid Fertilizer Supplemented with Phytase Increases Corn Yield Corn seeds are planted in 21 distinct geographical locations in the United States in furrows treated with a standard NPK fertilizer and water (5 gallons/acre), a liquid 6-24-6 starter fertilizer (5 gallons/acre), liquid 6-24-6 starter fertilizer (5 gallons/acre) supplemented with 70 ml/acre of a liquid composition comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 1, liquid 6-24-6 starter fertilizer (5 gallons/acre) supplemented with 50 ml/acre of a liquid composition comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 2, liquid 6-24-6 starter fertilizer (5 gallons/acre) supplemented with 100 ml/acre of a liquid composition comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 2, liquid 6- 24-6 starter fertilizer (5 gallons/acre) supplemented with 20 ml/acre of a liquid composition comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 3, or liquid 6-24-6 starter fertilizer (5 gallons/acre) supplemented with 55 ml/acre of a liquid composition comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 3. Eight replicates are performed at each geographical location. Each of the aforementioned phytase treatments increases corn yield by about 1 to about 5 bushels per acre, as compared to the untreated control treatment (i.e., water). Example 8 Monoammonium Phosphate Fertilizer Treated with Phytase Increases Corn Yield Corn seeds are planted in 22 distinct geographical locations in the United States in fields treated with 100 lb/acre of standard monoammonium phosphate granules or monoammonium phosphate granules that have been treated with a 70 ml/acre or 210 ml/acre of a liquid composition comprising about 2 to about 4% w/w of an enzymatically active protein comprising SEQ ID NO: 1. Eight replicates are performed at each geographical location. Corn plants grown in soil treated with standard MAP granules exhibit increased yield, as compared to corn plants grown in untreated control soil. Both of the aforementioned phytase treatments increase corn yield by about 1 to about 5 bushels per acre, as compared to the standard MAP granules.

Claims

THAT WHICH IS CLAIMED: 1. Use of an enzymatically active protein, a formulation comprising an enzymatically active protein, a polynucleotide encoding an enzymatically active protein, or an organism expressing an enzymatically active protein for: a. treating (e.g., drenching, fogging, misting, spraying) a plant growth medium; b. improving one or more soil characteristics; c. enhancing a plant growth environment; d. catalyzing hydrolysis of phytic acids in a plant growth medium and/or a fertilizer; e. removing phosphate from myo-inositol hexakisphosphates in a plant growth medium and/or a fertilizer; f. removing phosphate from myo-inositol pentakisphosphates in a plant growth medium and/or a fertilizer; g. removing phosphate from myo-inositol tetrakisphosphates in a plant growth medium and/or a fertilizer; h. removing phosphate from myo-inositol trisphosphates in a plant growth medium and/or a fertilizer; i. removing phosphate from myo-inositol diphosphates in a plant growth medium and/or a fertilizer; j. removing phosphate from myo-inositol monophosphates in a plant growth medium and/or a fertilizer; k. producing/releasing soluble forms of phosphorous in a plant growth medium and/or a fertilizer; l. producing/releasing soluble forms of minerals, such as calcium, iron, magnesium, manganese, potassium and zinc, in a plant growth medium and/or a fertilizer; m. increasing nutrient availability in a plant growth medium and/or a fertilizer (e.g., phosphorous, calcium, iron, magnesium, manganese, potassium, zinc availability); n. improving nutrient stability in a plant growth medium and/or a fertilizer (e.g., stabilizing levels of soluble phosphorous, calcium, copper, iron, magnesium, manganese, potassium and/or zinc in plant growth media and fertilizers); o. increasing nutrient uptake in a plant and/or a plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc uptake) by, for example, increasing the availability of nutrients in a plant growth medium and/or a fertilizer; p. increasing nutrient accumulation in a plant and/or a plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc accumulation) by, for example, increasing the availability of nutrients in a plant growth medium and/or a fertilizer; q. increasing nutrient utilization in a plant and/or a plant part (e.g., phosphorous, calcium, iron, potassium, magnesium, manganese and/or zinc utilization) by, for example, increasing the availability of nutrients in a plant growth medium and/or a fertilizer; r. enhancing plant growth; s. enhancing plant yield; t. reducing the amount(s) of exogenous fertilizer needed to achieve a desired result (e.g., the amount of exogenous phosphorous required to produce X bushels of corn); u. reducing nutrient washout/runoff from a plant growth medium (e.g., phosphorous washout/runoff from field soil); v. enhancing soil microbiomes; w. stimulating growth and/or proliferation of one or more plant-beneficial microorganisms in a plant growth medium (e.g., growth and/or proliferation of one or more plant-beneficial diazotrophs, phosphate-solubilizers and/or mycorrhizae); x. enhancing plant root nodulation; y. enhancing plant root mycorrhization; z. treating (e.g., coating, dipping, drenching, fogging, misting, soaking, spraying) a plant or plant part; aa. enhancing the abilities of a plant and/or a plant part to resist infestations/infections of/by one or more phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; bb. reducing disease severity in a plant and/or a plant part affected by one or more phytopathogenic pests, such as arachnids, bacteria, fungi, gastropods, insects, nematodes, oomycetes, protozoa, viruses and weeds; cc. reducing one or more phytopathogen loads in a plant growth medium and/or a fertilizer; dd. inclusion as part of an Integrated Pest Management program/strategy, optionally an Integrated Pest Management program/strategy comprising one or more chemical pesticides; ee. reducing detrimental effects of pesticide-induced phytotoxicity; ff. enhancing the abilities of a plant and/or a plant part to tolerate one or more abiotic stresses, such as drought, salinity and extreme temperatures; gg. reducing disease severity in a plant and/or a plant part affected by one or more abiotic stresses, such as drought, salinity and extreme temperatures; hh. degrading one or more organic materials in a plant growth medium and/or a fertilizer; and/or ii. enhancing turnover of one or more organic materials in a plant growth medium and/or a fertilizer, said enzymatically active protein selected from the group consisting of: i. polypeptides having phytase activity belonging to EC 3.1.3; ii. polypeptides having phytase activity belonging to EC 3.1.3.26; iii. polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.85 0.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 1, wherein the three-dimensional structure is determined using AlphaFold; iv. polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.85 0.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 2, wherein the three-dimensional structure is determined using AlphaFold; v. polypeptides having a TM score of at least 0.80, 0.805, 0.81, 0.815, 0.82, 0.825, 0.83, 0.835, 0.84, 0.845, 0.85 0.855, 0.86, 0.865, 0.87, 0875, 0.88, 0.885, 0.89, 0.895, 0.90, 0.905, 0.91, 0.915, 0.92, 0.925, 0.93, 0.935, 0.94, 0.945, 0.95, 0.955, 0.96, 0.965, 0.97, 0.975, 0.98, 0.985, 0.99, 0.995 or 1.0 relative to the three-dimensional structure of SEQ ID NO: 3, wherein the three-dimensional structure is determined using AlphaFold; vi. polypeptides having phytase activity and at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 1; vii. polypeptides having phytase activity and at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 2; viii. polypeptides having phytase activity and at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to SEQ ID NO: 3; ix. polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1,

2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 1; x. polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 2; xi. polypeptides having at most 0.25, 0.3, 0.35, 0.4, 0.45, 0.5, 0.55, 0.6, 0.65, 0.7, 0.75, 0.8, 0.85, 0.9, 0.95, 1.0, 1.05, 1.1, 1.15, 1.2, 1.25, 1.3, 1.35, 1.4, 1.45, 1.5, 1.55, 1.6, 1.65, 1.7, 1.75, 1.8, 1.85, 1.9, 1.95, 2.0, 2.05, 2.1, 2.15, 2.2, 2.25, 2.3, 2.35, 2.4, 2.45, 2.5, 2.55, 2.6, 2.65, 2.75, 2.8, 2.85, 2.9, 2.95, 3.0, 3.05, 3.1, 3.15, 3.2, 3.25, 3.3, 3.35, 3.4, 3.45, 3.5, 3.55, 3.6, 3.65, 3.7, 3.75, 3.8, 3.85, 3.9, 3.95, 4.0, 4.05, 4.1, 4.15, 4.2, 4.25, 4.3, 4.35, 4.4, 4.45, 4.5, 4.55, 4.6, 4.65, 4.7, 4.75, 4.8, 4.85, 4.9, 4.95 or 5.0% sequence difference(s) as compared to SEQ ID NO: 3; xii. polypeptides having phytase activity and encoded by a polynucleotide having at least 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 90.5, 91, 91.5, 92, 92.5, 93, 93.5, 94, 94.5, 95, 95.5, 96, 96.5, 97, 97.5, 98, 98.1, 98.2, 98.3, 98.4, 98.5, 98.6, 98.7, 98.8, 98.9, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9 or 100% sequence identity to one or more of SEQ ID NO(s): 4–6; xiii. polypeptides consisting of the amino acid sequence of any one of SEQ ID NO(s): 1–3 and 7–480; xiv. enzymatically active fragments/mutants/variants of any one of SEQ ID NO(s): 1–3 and 7–480; xv. enzymatically active polypeptides derived from any one of SEQ ID NO(s): 1–3 and 7–480 by substitution, deletion, or insertion of one or more amino acids; xvi. enzymatically active polypeptides derived from the polypeptide of any one of i) through xv) wherein the N- and/or C-terminal end has been extended by the addition of one or more amino acids; xvii. enzymatically active fragments of the polypeptide of any one of i) through xvi); and xviii. fusion proteins comprising a first polypeptide having a first enzymatic activity and a second polypeptide having a second enzymatic activity, wherein at least one of said first polypeptide and said second polypeptide optionally comprises the polypeptide of any one of i) through xvii). 2. A method comprising applying an enzymatically active protein selected from the group consisting of i) through xviii), as defined in claim 1 above, to a plant, plant part, plant growth medium and/or fertilizer.

3. A formulation comprising an enzymatically active protein selected from the group consisting of i) through xviii), as defined in claim 1 above, in an agronomically acceptable carrier.

4. A method comprising applying the formulation of claim 3 to a plant, plant part, plant growth medium and/or fertilizer.

5. A method comprising applying a cell, optionally a recombinant host cell, that expresses an enzymatically active protein selected from the group consisting of i) through xviii), as defined in claim 1 above, to a plant, plant part, plant growth medium and/or fertilizer.

6. A plant or plant part comprising a heterologous polynucleotide that encodes an enzymatically active protein selected from the group consisting of i) through xviii), as defined in claim 1 above.

7. A plant or plant part that expresses a heterologous enzymatically active protein selected from the group consisting of i) through xviii), as defined in claim 1 above.

8. A method comprising introducing a plant or plant part comprising a heterologous polynucleotide that encodes an enzymatically active protein selected from the group consisting of i) through xviii), as defined in claim 1 above, into a plant growth medium.

9. A method comprising introducing a plant or plant part that expresses a heterologous enzymatically active protein selected from the group consisting of i) through xviii), as defined in claim 1 above, into a plant growth medium.

10. A kit comprising an enzymatically active protein selected from the group consisting of i) through xviii), as defined in claim 1 above, and instructions for applying said protein to a plant, plant part, plant growth medium and/or fertilizer.