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WO2020070249A1 - Compositions de nettoyage - Google Patents

Compositions de nettoyage

Info

Publication number
WO2020070249A1
WO2020070249A1 PCT/EP2019/076825 EP2019076825W WO2020070249A1 WO 2020070249 A1 WO2020070249 A1 WO 2020070249A1 EP 2019076825 W EP2019076825 W EP 2019076825W WO 2020070249 A1 WO2020070249 A1 WO 2020070249A1
Authority
WO
WIPO (PCT)
Prior art keywords
seq
polypeptide
sequence identity
dnase
cleaning composition
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/EP2019/076825
Other languages
English (en)
Inventor
Lilian Eva Tang Baltsen
Rebecca Munk VEJBORG
Klaus GORI
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes AS
Original Assignee
Novozymes AS
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Novozymes AS filed Critical Novozymes AS
Publication of WO2020070249A1 publication Critical patent/WO2020070249A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01109—Endogalactosaminidase (3.2.1.109)
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01052—Beta-N-acetylhexosaminidase (3.2.1.52)

Definitions

  • the present invention relates to cleaning compositions comprising a mix of enzymes.
  • the invention further relates to use of compositions comprising such enzymes in cleaning processes and/or for deep cleaning of biofilm soiling, and methods for removal or reduction of biofilm related soiling.
  • Enzymes have been used in detergents for decades. Usually a cocktail of various enzymes is added to detergent compositions.
  • the enzyme cocktail often comprises various enzymes, wherein each enzyme targets a specific substrate, e.g. amylases are active towards starch stains, proteases towards protein stains and so forth.
  • Textile surface and hard surfaces such as dishes or the inner space of a laundry machine enduring a number of wash cycles, become soiled with many different types of soiling which may compose of proteins, grease, starch etc.
  • One type of soiling may be organic matter, such as biofilm, extracellular polymeric substances (EPS), etc.
  • Organic matter comprises different molecules such as polysaccharides, extracellular DNA (eDNA) and proteins.
  • Some organic matter forms an extracellular polymeric matrix, which may be sticky or gluing, and which when present on textiles attracts soils and may cause redeposition or backstaining of soils, resulting in greying of the textile. Additionally, organic matter such as biofilms often cause malodor, as various malodor molecules can be adhered by the polysaccharides, extracellular eDNA and proteins in the complex extracellular matrix and be slowly released so as to result in noticeable malodor.
  • the cleaning compositions of the present invention are useful in cleaning compositions and are effective in deep cleaning of surfaces such as fabrics, for example for reducing or removing biofilm.
  • Biofilm is an extracellular matrix produced by various microorganisms that is typically composed of polysaccharides, extracellular RNA, DNA and proteins.
  • the cleaning compositions of the invention are also useful for prevention, reduction or removal of malodor, for prevention or reduction of redeposition of soils, and for improving whiteness.
  • the present invention thus relates to a cleaning composition
  • a cleaning composition comprising at least two cleaning enzymes selected from the group consisting of nucleases, hexosaminidases and glycosyl hydrolases and at least two detergent enzymes selected from the group consisting of proteases, amylases, lipases, mannanases, pectate lyases and cellulases.
  • the nuclease is in particular a DNase or an RNase
  • the glycosyl hydrolase is in particular a Glyco_hydro_1 14, GH39 or GHL13 glycosyl hydrolase.
  • the invention relates to use of the cleaning composition for cleaning an item such as a textile, for example for preventing, reducing or removing biofilm and/or body secretions such as dead cells, sebum or sweat from an item, and for a method of cleaning an item such as a textile with the cleaning composition.
  • SEQ ID NO: 1 mature DNase polypeptide obtained from Bacillus cibi
  • SEQ ID NO: 2 mature DNase polypeptide obtained from Bacillus licheniformis
  • SEQ ID NO: 7 mature Glyco_hydro_1 14 polypeptide obtained from Burkholderia sp.
  • SEQ ID NO: 10 mature GH39 polypeptide obtained from Pseudomonas fluorescens
  • SEQ ID NO: 1 mature GH39 polypeptide obtained from Pseudomonas sp.
  • SEQ ID NO: 14 mature GHL13 polypeptide obtained from Escherichia coli
  • SEQ ID NO: 18 mature RNase polypeptide obtained from Fusarium solani
  • SEQ ID NO: 19 mature hexosaminidase polypeptide obtained from Terribacillus saccharophilus
  • SEQ ID NO: 20 mature hexosaminidase polypeptide obtained from Terribacillus saccharophilus
  • SEQ ID NO: 21 mature hexosaminidase polypeptide obtained from Terribacillus saccharophilus
  • SEQ ID NO: 22 mature hexosaminidase polypeptide obtained from Aggregatibacter actinomycetemcomitans
  • SEQ ID NO: 23 mature hexosaminidase polypeptide obtained from Actinobacillus equuli subsp. equuli
  • SEQ ID NO: 24 mature protease polypeptide obtained from Bacillus lentus
  • SEQ ID NO: 25 mature protease polypeptide obtained from Bacillus amyloliquefaciens
  • SEQ ID NO: 26 mature protease polypeptide obtained from Bacillus sp. TY145
  • SEQ ID NO: 27 mature amylase polypeptide obtained from Bacillus sp.
  • SEQ ID NO: 28 mature amylase polypeptide obtained from Bacillus sp.
  • SEQ ID NO: 31 mature lipase polypeptide obtained from Thermomyces lanuginosus
  • SEQ ID NO: 32 mature mannanase polypeptide obtained from Bacillus bogoriensis
  • SEQ ID NO: 34 mature cellulase polypeptide obtained from Bacillus subtilis
  • Biofilm A biofilm is organic matter produced by any group of microorganisms in which cells stick to each other or stick to a surface, such as a textile, dishware or hard surface or another kind of surface. These adherent cells are frequently embedded within a self-produced matrix of extracellular polymeric substance (EPS).
  • EPS extracellular polymeric substance
  • Biofilm EPS is a polymeric conglomeration generally composed of extracellular DNA, proteins and polysaccharides. Biofilms may form on living or non-living surfaces.
  • the microbial cells growing in a biofilm are physiologically distinct from planktonic cells of the same organism, which, by contrast, are single-cells that may float or swim in a liquid medium.
  • EPS is the construction material of bacterial settlements and either remain attached to the cells’ outer surface, or is secreted into its growth medium.
  • organic matters such as EPS contained in many biofilms constitute a challenging type of soiling due to their complex nature. Detergents that are currently commercially available cannot effectively remove or reduce EPS- related soiling.
  • biofilm or EPS-producing bacteria can be found e.g. among the following species: Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Pseudomonas sp., Staphylococcus epidermidis, and Stenotrophomonas sp.
  • the biofilm-producing strain may e.g. be a species of Pseudomonas, for example Pseudomonas aeruginosa, Pseudomonas alcaliphila or Pseudomonas fluorescens.
  • the biofilm is caused by microorganisms or a group of microorganisms which produce Pel.
  • the biofilm produces a polysaccharide that is degradable by the Glyco_hydro_1 14 glycosyl hydrolases of the invention.
  • the biofilm is caused by microorganisms or a group of microorganisms which produce Psl.
  • the biofilm produces a polysaccharide that is degradable by the GH39 glycosyl hydrolases of the invention.
  • the biofilm may be caused by microorganisms that produce the linear exopolysaccharide poly-3-(1 ,6)-N-acetyl-D-glucosamine (PNAG).
  • PNAG linear exopolysaccharide poly-3-(1 ,6)-N-acetyl-D-glucosamine
  • This exopolymer is found in biofilms of both Gram-positive bacteria, e.g. Staphylococcus species, where it is referred to as polysaccharide intercellular adhesion (PIA), and Gram-negative bacteria, e.g. Escherichia coli, where it is referred to as PGA, and species of Bordetella, where it is referred to as Bps.
  • PIA polysaccharide intercellular adhesion
  • PGA species of Bordetella
  • the biofilm that may be formed on the surface of a material such as a textile may be caused by any microorganism or group of microorganisms that forms biofilm, for example a PelA- dependent biofilm, a PsIG-dependent biofilm or a PgaB-dependent biofilm.
  • microorganisms include but are not limited to Acinetobacter sp., Aeromicrobium sp., Brevundimonas sp., Microbacterium sp., Micrococcus luteus, Staphylococcus epidermidis, Staphylococcus aureus, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas alcaliphila, Pseudomonas fluorescens, Stenotrophomonas sp., Paraburkholderia, Burkolderia sp., Candida sp., Bordetella pertussis Yersinia pestis, Escherichia coli and Aspergillus sp.
  • Catalytic domain means the region of an enzyme containing the catalytic machinery of the enzyme.
  • a clade is a group of polypeptides clustered together on the basis of homologous features traced to a common ancestor. Polypeptide clades can be visualized as phylogenetic trees and a clade is a group of polypeptides that consists of a common ancestor and all its lineal descendants.
  • Cleaning enzyme refers to an enzyme selected from the group consisting of nucleases, in particular DNases and RNases, hexosaminidases, in particular dispersins, and glycosyl hydrolases, in particular Glyco_hydro_1 14, GH39 and GHL13 glycosyl hydrolases.
  • cDNA means a DNA molecule that can be prepared by reverse transcription from a mature, spliced, mRNA molecule obtained from a eukaryotic or prokaryotic cell. cDNA lacks 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.
  • Coding sequence means a polynucleotide, which 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.
  • control sequences means nucleic acid sequences necessary for expression of a polynucleotide encoding a mature polypeptide of the present invention.
  • Each control sequence may be native (/ ' .e., from the same gene) or foreign (/ ' .e., from a different gene) to the polynucleotide encoding the polypeptide or native or foreign to each other.
  • control sequences include, but are not limited to, a leader, polyadenylation sequence, propeptide sequence, promoter, signal peptide sequence, and transcription terminator.
  • 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.
  • the cleaning component e.g. a detergent adjunct ingredient
  • a detergent adjunct ingredient is different from the polypeptides (enzymes) of this invention.
  • the precise nature of these additional cleaning or adjunct components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the operation for which it is to be used.
  • Suitable cleaning components include, but are not limited to the components described below such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, other enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric agents, clay soil removal/anti- redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric hueing agents, anti-foaming agents, dispersants, processing aids, and/or pigments.
  • surfactants such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, other enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric agents, clay soil removal/anti- redeposition agents, brighteners, suds suppress
  • cleaning composition includes “detergent composition” and refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles.
  • the detergent composition may be used to e.g. clean textiles for both household cleaning and industrial cleaning.
  • the term encompasses any materials/compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, or spray compositions) and includes, but is not limited to, detergent compositions (e.g., liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; and textile and laundry pre- spotters/pretreatment).
  • the detergent formulation may contain one or more detergent adjunct ingredients such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reductases, bluing agents and fluorescent dyes, antioxidants, and solubilizers.
  • detergent adjunct ingredients such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers, fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, transferase(s), hydrolytic enzymes, oxido reduct
  • Deep cleaning means disruption, reduction or removal of organic components such as polysaccharides such as Pel or PNAG, proteins, RNA, DNA, soil or other components present in organic matter such as biofilm.
  • Detergent enzyme refers to enzymes that are not encompassed by the term“cleaning enzyme” as defined above (i.e. enzymes that are not a DNase, an RNase, a hexosaminidase, a Glyco_hydro_1 14 glycosyl hydrolase, a GH39 glycosyl hydrolase or a GHL13 glycosyl hydrolase).
  • the term “detergent enzyme” includes enzymes traditionally used in detergent compositions, including but not limited to proteases, amylases, lipases, mannanases, pectate lyases and cellulases. Other detergent enzymes may e.g.
  • an enzyme such as a mannanase is considered to be a“detergent enzyme”.
  • Enzyme detergency benefit is defined herein as the advantageous effect an enzyme may add to a detergent compared to the same detergent without the enzyme.
  • Important detergency benefits which can be provided by enzymes are stain removal with no or very little visible soils after washing and/or cleaning, prevention or reduction of redeposition of soils released in the washing process (an effect that also is termed anti- redeposition), restoring fully or partly the whiteness of textiles which originally were white but after repeated use and wash have obtained a greyish or yellowish appearance (an effect that also is termed whitening).
  • Textile care benefits which are not directly related to catalytic stain removal or prevention of redeposition of soils, are also important for enzyme detergency benefits.
  • Examples of such textile care benefits are prevention or reduction of dye transfer from one fabric to another fabric or another part of the same fabric (an effect that is also termed dye transfer inhibition or anti-backstaining), removal of protruding or broken fibers from a fabric surface to decrease pilling tendencies or remove already existing pills or fuzz (an effect that also is termed anti-pilling), improvement of the fabric-softness, colour clarification of the fabric and removal of particulate soils which are trapped in the fibers of the fabric or garment.
  • Enzymatic bleaching is a further enzyme detergency benefit where the catalytic activity generally is used to catalyze the formation of bleaching components such as hydrogen peroxide or other peroxides.
  • expression includes 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 vector means a linear or circular DNA molecule that comprises a polynucleotide encoding a polypeptide and is operably linked to control sequences that provide for its expression.
  • fragment means a polypeptide or a catalytic domain having one or more amino acids absent from the amino and/or carboxyl terminus of a mature polypeptide or domain; wherein the fragment has activity.
  • host cell means any cell type that is susceptible to transformation, transfection, transduction, or the like with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention.
  • host cell encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that occur during replication.
  • Isolated means a substance in a form or environment that does not occur in nature.
  • isolated substances include (1 ) any non-naturally occurring substance, (2) any substance including, but not limited to, any enzyme, variant, nucleic acid, protein, peptide or cofactor, that is at least partially removed from one or more or all of the naturally occurring constituents with which it is associated in nature; (3) any substance modified by the hand of man relative to that substance found in nature; or (4) any substance modified by increasing the amount of the substance relative to other components with which it is naturally associated (e.g., recombinant production in a host cell; multiple copies of a gene encoding the substance; and use of a stronger promoter than the promoter naturally associated with the gene encoding the substance).
  • An isolated substance may be present in a fermentation broth sample; e.g. a host cell may be genetically modified to express the polypeptide of the invention. The fermentation broth from that host cell will comprise the isolated polypeptide.
  • Improved wash performance is defined herein as an enzyme displaying an increased wash performance in a detergent composition relative to the wash performance of same detergent composition without the enzyme e.g. by increased stain removal or less re-deposition.
  • improved wash performance includes wash performance in laundry.
  • Laundering relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a cleaning or detergent composition of the present invention.
  • the laundering process can for example be carried out using e.g. a household or an industrial washing machine or can be carried out by hand.
  • malodor By the term“malodor” is meant an odor which is not desired on clean items.
  • the cleaned item should smell fresh and clean without malodors adhered to the item.
  • malodor is compounds with an unpleasant smell, which may be produced by microorganisms.
  • unpleasant smells can be sweat or body odor adhered to an item which has been in contact with human or animal.
  • malodor can be the odor from spices which sticks to items, for example curry or other spices with a strong smell.
  • Mature polypeptide means a polypeptide in its final form following translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc.
  • a host cell may produce a mixture of two of more different mature polypeptides (/ ' .e., with a different C-terminal and/or N-terminal amino acid) expressed by the same polynucleotide. It is also known in the art that different host cells process polypeptides differently, and thus, one host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., having a different C-terminal and/or N-terminal amino acid) as compared to another host cell expressing the same polynucleotide.
  • Mature polypeptide coding sequence means a polynucleotide that encodes a mature polypeptide having activity.
  • nucleic acid construct means a nucleic acid molecule, 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, which comprises one or more control sequences.
  • operbly linked means a configuration in which a control sequence is placed at an appropriate position relative to the coding sequence of a polynucleotide such that the control sequence directs expression of the coding sequence.
  • Sequence identity The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter“sequence identity”.
  • the sequence identity between two amino acid sequences is determined 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 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.
  • the output of Needle labeled“longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows:
  • variant means a polypeptide having a given enzymatic activity comprising an alteration, i.e., a substitution, insertion and/or deletion, 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 an amino acid adjacent to and immediately following the amino acid occupying a position.
  • the nomenclature“E/Q” means that the amino acid at a given position may be a glutamic acid (Glu, E) or a glutamine (Gin, Q).
  • the nomenclature“V/G/A l” means that the amino acid at this position may be a valine (Val, V), glycine (Gly, G), alanine (Ala, A) or isoleucine (lie, I), and so forth for other combinations as described herein.
  • the amino acid X is defined such that it may be any of the 20 natural amino acids.
  • substitutions are typically indicated with the original amino acid, the position number, and the replacement amino acid.
  • A226V indicates that the original alanine residue in position 226 has been replaced by a valine residue.
  • G184 * indicates that the original glycine residue in position 184 has been deleted.
  • Insertions are indicated by listing the original amino acid, the position number, the original amino acid and the inserted amino acid. For example, S97SD indicates that an aspartic acid residue has been inserted after the serine residue in position 97.
  • the present invention relates to cleaning compositions comprising at least two cleaning enzymes selected from the group consisting of nucleases, hexosaminidases and glycosyl hydrolases and at least two detergent enzymes selected from the group consisting of proteases, amylases, lipases, mannanases, pectate lyases and cellulases, where the nuclease is a DNase or an RNase, the hexosaminidase is a dispersin, and the glycosyl hydrolase is a Glyco_hydro_1 14, GH39 or GHL13 glycosyl hydrolase.
  • the cleaning compositions will typically contain additional components that are commonly used in detergent or cleaning compositions, typically at least one surfactant and optionally at least one additional cleaning component selected from builders and bleach components. Such additional cleaning components are also described in detail further below.
  • the cleaning composition may comprise both a DNase and an RNase, more than one type of glycosyl hydrolase, more than one protease, more than one cellulase, etc.
  • DNase means a nuclease polypeptide having DNase activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in a DNA backbone, thus degrading DNA.
  • DNase activity may be determined according to the procedure described in the Assay 1 or 2 herein.
  • X 1 , 2, 3, 4, 5, 6, 7, 8 or 9 e.g. Deoxyribonuclease I, Deoxyribonuclease IV, Type I site-specific deoxyribonuclease, Type II site-specific deoxyribonuclease, Type III site-specific deoxyribonuclea
  • Y 1 , 2, 4 or 5, e.g. Deoxyribonuclease II, Aspergillus deoxyribonuclease K(1 ), Crossover junction endo- deoxyribonuclease, or Deoxyribonuclease X.
  • the DNase activity is obtained from a microorganism, and the DNase is a microbial enzyme.
  • the DNase is preferably of fungal or bacterial origin.
  • the DNase may be obtained from a bacterium, e.g. Bacillus, such as Bacillus licheniformis, Bacillus subtilis, Bacillus sp., Bacillus ho koshii, Bacillus horneckiae, Bacillus cibi, Bacillus idriensis, Bacillus algicola, Bacillus vietnamensis, Bacillus hwajinpoensis, Bacillus indicus, Bacillus marisflavi, Bacillus luciferensis, or Bacillus sp. SA2-6.
  • Bacillus such as Bacillus licheniformis, Bacillus subtilis, Bacillus sp., Bacillus ho koshii, Bacillus horneckiae, Bacillus cibi, Bacillus idriensis, Bacillus algicola, Bacillus vietnamensis, Bacillus hwajinpoensis, Bacillus
  • the DNase may also be obtained from any of the following: Pyrenochaetopsis sp., Vibrissea flavovirens, Setosphaeria rostrate, Endophragmiella valdina, Corynespora cassiicola, Paraphoma sp., Monilinia fructicola, Curvularia lunata, Penicillium reticulisporum, Penicillium quercetorum, Setophaeosphaeria sp., Alternaria, Alternaria sp., Trichoderma reesei, Chaetomium thermophilum, Scytalidium thermophilum, Metapochonia suchlasporia, Daldinia fissa, Acremonium sp., Acremonium dichromosporum, Sarocladium sp., Metarhizium sp.
  • HNA15-2 Isaria tenuipes Scytalidium circinatum, Metarhizium lepidiotae, Thermobispora bispora, Sporormia fimetaria, Pycnidiophora cf. dispera, Clavicipitaceae sp., Westerdykella sp., Humicolopsis cephalosporioides, Neosartorya massa, Roussoella intermedia, Pleosporales, Phaeosphaeria or Didymosphaeria futilis.
  • the polypeptides having DNase activity are polypeptides comprising the PFAM domain DUF1524 ((http://pfam.xfam.org/), “The Pfam protein families database: towards a more sustainable future”, R.D. Finn, et.al. Nucleic Acids Research (2016) Database Issue 44:D279-D285”).
  • the DUF1524 domain contains a conserved HXXP sequence (where H is the amino acid histidine, P is the amino acid proline, and X is any amino acid motif) commonly found in nucleases (M.A. Machnicka, et al.
  • DUF stands for domain of unknown function, and the polypeptide families comprising, e.g., DUF have been collected together in the Pfam database, which provides sequence alignments and hidden Markov models that define the collected protein domains.
  • the polypeptides having DNase activity in the composition of the invention comprise the DUF1524 domain.
  • DNases comprising the DUF1524 domain see WO 2017/060475, which is hereby incorporated by reference.
  • the DNase is a NUC1 or NUC1_A DNase.
  • a NUC1 DNase is a DNase comprising a domain termed NUC1 , and polypeptides with this domain are in addition to having DNase activity characterized by comprising certain motifs.
  • a NUC1 sub-domain had been identified, termed the NUC1_A domain, which also is characterized by comprising certain motifs.
  • the NUC1 and NUC1_A DNases are described in WO 2017/060475 and WO 2018/184873, which are hereby incorporated by reference.
  • the preparation of the polypeptide having DNase activity as described herein can e.g. be performed as described in WO 2017/059802, in particular in the sections Nucleic Acid Construct, Expression Vectors, Host Cells, Methods of Production and Fermentation Broth Formulations.
  • the cleaning composition of the invention comprises a polypeptide having DNase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 1 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 1.
  • the cleaning composition of the invention comprises a polypeptide having DNase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 2 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 2.
  • the cleaning composition of the invention comprises a polypeptide having DNase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 3 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 3.
  • the cleaning composition of the invention comprises a polypeptide having DNase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 4 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 4.
  • the cleaning composition of the invention comprises a polypeptide having DNase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 5 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 5.
  • the cleaning composition of the invention may comprise any of the DNase polypeptides disclosed in WO 2017/059802, WO 2017/060475, WO 2018/185285 or WO 2018/184873, the contents of which are incorporated herein by reference.
  • the DNase polypeptide When present in a cleaning composition of the invention, the DNase polypeptide will typically be present in an amount of from 0.01 to 1000 ppm, from 0.1 to 1000 ppm, from 1 ppm to 1000 ppm, from 10 ppm to 1000 ppm, from 50 ppm to 1000 ppm, from 100 ppm to 1000 ppm, from 150 ppm to 1000 ppm, from 200 ppm to 1000 ppm, from 250 ppm to 1000 ppm, from 250 ppm to 750 ppm, or from 250 ppm to 500 ppm, based on active protein.
  • the DNases above may be combined with one or more other cleaning enzyme in the composition, e.g. a hexosaminidase and/or a glycosyl hydrolase, to form a blend to be added to the wash liquor solution according to the invention.
  • a hexosaminidase and/or a glycosyl hydrolase e.g. a hexosaminidase and/or a glycosyl hydrolase
  • the concentration of the DNase in the wash liquor solution is typically in the range of from 0.00001 ppm to 10 ppm, from 0.00002 ppm to 10 ppm, from 0.0001 ppm to 10 ppm, from 0.0002 ppm to 10 ppm, from 0.001 ppm to 10 ppm s from 0.002 ppm to 10 ppm, from 0.01 ppm to 10 ppm, from 0.02 ppm to 10 ppm, from 0.1 ppm to 10 ppm, from 0.2ppm to 10 ppm, or from 0.5 ppm to 5 ppm.
  • RNase means a nuclease polypeptide having RNase activity (EC 3.1 .2.7) that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases. The present invention relates especially to endoribonucleases. For purposes of the present invention, RNase activity may be determined according to the procedure described in Assay 3 herein.
  • the polypeptides of the invention having RNase activity preferably comprise a domain from the RNase Barnase (UniProt P00648 (RNBR_BACAM), PF00545 family).
  • a phylogenetic tree has been constructed with polypeptide sequences containing a Barnase domain, as defined in PFAM (PF000545, Pfam version 30.0 Finn (2016), Nucleic Acids Research, Database Issue 44 D279-D285).
  • the phylogenetic tree was constructed from a multiple alignment of mature polypeptide sequences containing at least one Barnase domain. The sequences were aligned using the MUSCLE algorithm version 3.8.31 (Edgar, 2004. Nucleic Acids Research 32(5): 1792-1797), and the trees were constructed using FastTree version 2.1 .8 (Price et al., 2010, PloS one 5(3)) and visualized using iTOL (Letunic & Bork, 2007.
  • Bioinformatics 23(1 ): 127-128) Polypeptides comprising the barnase domain can be separated into multiple distinct sub-clusters, or clades, which can be defined in terms of distinct motifs for each clade. See WO 2018/178061 for further information.
  • the RNase barnase from the PF00545 family of ribonucleases catalyzes hydrolysis at diribonucleotide GpN sites. Cleavage occurs in two steps using a general acid-base mechanism: a cyclic intermediate is formed during the first transesterification step, which is then hydrolysed to release the cleaved RNA.
  • the two most important residues involved in catalysis are Glu73 and His102, which are both believed to be essential for enzymatic activity. Glu73 is the general base whilst His102 is the general acid.
  • Barnase has no disulfide bonds, nor does it require divalent cations or non-peptide components to fold.
  • a polypeptide having RNase activity of the present invention may be obtained from microorganisms of any genus.
  • the term“obtained from” as used herein about a given source shall mean that the polypeptide encoded by a polynucleotide is produced by the source or by a strain in which the polynucleotide from the source has been inserted.
  • the polypeptide obtained from a given source is secreted extracellularly.
  • the RNase is preferably a microbial RNase, preferably obtained from a bacterium or a fungus.
  • the polypeptide is a Paenibacillus polypeptide.
  • One embodiment of this aspect is e.g. a polypeptide obtained from Paenibacillus sp..
  • Another embodiment of this aspect is a polypeptide obtained from Paenibacillus tundrae.
  • the polypeptide is an Amycolatopsis polypeptide, e.g., a polypeptide obtained from Amycolatopsis azurea.
  • the polypeptide is an Acremonium polypeptide, e.g., a polypeptide obtained from Acremonium alcalophilum.
  • the polypeptide is a Stenotrophomonas polypeptide, e.g., a polypeptide obtained from Stenotrophomonas rhizophila.
  • the polypeptide is an Erwinia polypeptide, e.g., a polypeptide obtained from Erwinia persicina.
  • the polypeptide is a Saccharothrix polypeptide, e.g., a polypeptide obtained from Saccharothrix sp.
  • the polypeptide is a Saccharopolyspora polypeptide, e.g., a polypeptide obtained from Saccharopolyspora endophytica.
  • the polypeptide is an Amycolatopsis polypeptide, e.g., a polypeptide obtained from Amycolatopsis circi.
  • the polypeptide is an Alkalimonas polypeptide, e.g., a polypeptide obtained from Alkalimonas sp.
  • the polypeptide is a Nonomuraea polypeptide, e.g., a polypeptide obtained from Nonomuraea dietziae.
  • the polypeptide is a Trichoderma polypeptide, e.g., a polypeptide obtained from Trichoderma harzianum.
  • the polypeptide is a Fusarium polypeptide, e.g., a polypeptide obtained from Fusarium solani.
  • the invention 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.
  • ATCC American Type Culture Collection
  • DSMZ Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH
  • CBS Centraalbureau Voor Schimmelcultures
  • NRRL Northern Regional Research Center
  • the cleaning composition of the invention comprises a polypeptide having RNase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 16 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 16.
  • the cleaning composition of the invention comprises a polypeptide having RNase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 17 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 17.
  • the cleaning composition of the invention comprises a polypeptide having RNase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 18 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 18.
  • the cleaning composition of the invention may comprise any of the RNase polypeptides disclosed in WO 2018/178061 , the contents of which are incorporated herein by reference.
  • the RNase polypeptide When present in a cleaning composition of the invention, the RNase polypeptide will typically be present in an amount of from 0.01 to 1000 ppm, from 0.1 to 1000 ppm, from 1 ppm to 1000 ppm, from 10 ppm to 1000 ppm, from 50 ppm to 1000 ppm, from 100 ppm to 1000 ppm, from 150 ppm to 1000 ppm, from 200 ppm to 1000 ppm, from 250 ppm to 1000 ppm, from 250 ppm to 750 ppm, or from 250 ppm to 500 ppm, based on active protein.
  • the RNases above may be combined with one or more other cleaning enzyme in the composition, e.g. a hexosaminidase and/or a glycosyl hydrolase, to form a blend to be added to the wash liquor solution according to the invention.
  • a hexosaminidase and/or a glycosyl hydrolase e.g. a hexosaminidase and/or a glycosyl hydrolase
  • the concentration of the RNase in the wash liquor solution is typically in the range of from 0.00001 ppm to 10 ppm, from 0.00002 ppm to 10 ppm, from 0.0001 ppm to 10 ppm, from 0.0002 ppm to 10 ppm, from 0.001 ppm to 10 ppm s from 0.002 ppm to 10 ppm, from 0.01 ppm to 10 ppm, from 0.02 ppm to 10 ppm, from 0.1 ppm to 10 ppm, from 0.2ppm to 10 ppm, or from 0.5 ppm to 5 ppm.
  • hexosaminidase including“dispersin’’ and the abbreviation“Dsp”, means a polypeptide having hexosaminidase activity, EC 3.2.1., that catalyzes the hydrolysis of b-1 ,6- glycosidic linkages of N-acetyl-glucosamine polymers found e.g. in biofilm.
  • the term hexosaminidase includes polypeptides having N-acetylglucosaminidase activity and b-N- acetylglucosaminidase activity.
  • Enzymes having hexosaminidase activity include dispersins such as dispersin B (DspB), which is a b-N-acetylglucosaminidase belonging to the Glycoside Hydrolase 20 family.
  • DspB dispersin B
  • polypeptide having hexosaminidase activity may be used interchangeably with the term “hexosaminidase”, and similarly the term “polypeptide having b-N- acetylglucosaminidase activity” may be used interchangeably with the term “b-N- acetylglucosaminidases”.
  • the polypeptide having hexosaminidase activity is a b-N-acetylglucosaminidase targeting poly-b-1 ,6-N-acetylglucosamine, preferably a dispersin.
  • hexosaminidase activity may be determined according to the procedure described in Assay 4 or 5 herein.
  • a polypeptide having hexosaminidase activity may be obtained from a microorganism of any genus.
  • the hexosaminidase or the b-N-acetylglucosaminidase targeting poly-b- 1 ,6-N-acetylglucosamine e.g. a dispersin is obtained from Terribacillus, Curtobacterium, Aggregatibacter, Haemophilus or Actinobacillus, preferably Terribacillus.
  • the cleaning composition of the invention comprises a polypeptide having hexosaminidase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 19 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 19.
  • the cleaning composition of the invention comprises a polypeptide having hexosaminidase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 20 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 20.
  • the cleaning composition of the invention comprises a polypeptide having hexosaminidase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 21 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 21 .
  • the cleaning composition of the invention comprises a polypeptide having hexosaminidase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 22 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 22.
  • the cleaning composition of the invention comprises a polypeptide having hexosaminidase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 23 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 23.
  • the cleaning composition of the invention may comprise any of the hexosaminidase polypeptides disclosed in WO 2017/186936, WO 2017/186937, WO 2017/186943 or WO 2018/184873, the contents of which are incorporated herein by reference.
  • the hexosaminidase polypeptide When present in a cleaning composition of the invention, the hexosaminidase polypeptide will typically be present in an amount of from 0.01 to 1000 ppm, from 0.1 to 1000 ppm, from 1 ppm to 1000 ppm, from 10 ppm to 1000 ppm, from 50 ppm to 1000 ppm, from 100 ppm to 1000 ppm, from 150 ppm to 1000 ppm, from 200 ppm to 1000 ppm, from 250 ppm to 1000 ppm, from 250 ppm to 750 ppm, or from 250 ppm to 500 ppm, based on active protein.
  • hexosaminidases above may be combined with one or more other cleaning enzyme in the composition, e.g. a nuclease and/or a glycosyl hydrolase, to form a blend to be added to the wash liquor solution according to the invention.
  • a nuclease and/or a glycosyl hydrolase e.g. a nuclease and/or a glycosyl hydrolase
  • the concentration of the hexosaminidase in the wash liquor solution is typically in the range of from 0.00001 ppm to 10 ppm, from 0.00002 ppm to 10 ppm, from 0.0001 ppm to 10 ppm, from 0.0002 ppm to 10 ppm, from 0.001 ppm to 10 ppm s from 0.002 ppm to 10 ppm, from 0.01 ppm to 10 ppm, from 0.02 ppm to 10 ppm, from 0.1 ppm to 10 ppm, from 0.2ppm to 10 ppm, or from 0.5 ppm to 5 ppm.
  • the present invention relates to cleaning compositions comprising glycosyl hydrolases (EC 3.2.1.-), which are a widespread group of enzymes that hydrolyze the glyosidic bond between two or more carbohydrates or between a carbohydrate and a non-carbohydrate moiety.
  • glycosyl hydrolases EC 3.2.1.-
  • a classification of glycoside hydrolases in families based on amino acid sequence similarities has been proposed.
  • the glycosyl hydrolase polypeptides of the invention comprise at least one glycosyl hydrolase domain.
  • glycosyl hydrolase domain comprised in such polypeptides may for purposes of the present invention be classified into one of three groups: 1 ) Glyco_hydro_1 14 glycosyl hydrolases, 2) GH39 glycosyl hydrolases, and 3) GHL13 glycosyl hydrolases.
  • a Glyco_hydro_1 14 glycosyl hydrolase is in the context of the present invention a glycosyl hydrolase comprising glycosyl hydrolase domain (DUF297), which here is termed Glyco_hydro_1 14 (Pfam domain id PF03537, Pfam version 31.0 Finn (2016) Nucleic Acids Research, Database Issue 44:D279-D285).
  • These polypeptides may further comprise a polysaccharide deacetylase domain (CE4).
  • the polypeptides of the invention are endo-alpha-1 ,4-polygalactosaminidases.
  • the polypeptides of the invention have at least hydrolytic activity on glyosidic bonds and may also have deacetylase activity.
  • the Glyco_hydro_1 14 glycosyl hydrolase is in particular a PelA enzyme, which is active towards the polysaccharide Pel that is present in many biofilms.
  • the pellicle (Pel) polysaccharide is synthesized e.g. by Pseudomonas aeruginosa and is an important biofilm constituent critical for bacterial virulence and persistence.
  • Pel is a cationic polymer composed of partially acetylated 1 4 glycosidic linkages of N-acetylgalactosamine and N-acetylglucosamine that promote cell-cell interactions within the biofilm matrix through electrostatic interactions with extracellular DNA (Jennings et al. PNAS Sept 2015, vol.1 12, no36, 1 1353-1 1358; Marmont et al. J Biol Chem. 2017 Nov 24;292(47):1941 1 -19422. 2017).
  • Glyco_hydro_1 14 glycosyl hydrolase activity may be determined according to the procedure described in Assay 6 herein.
  • the Glyco_hydro_114 polypeptides of the invention comprise a domain termed here as a CE4_PelA_like domain, which is represented by a protein PelA that is encoded by a gene in the pelA-G gene cluster for pellicle production and biofilm formation in Pseudomonas aeruginosa.
  • PelA and most of the family members contain a domain of unknown function, DUF297 (PF03537), in the N-terminus and a C-terminal domain that shows high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily.
  • CE4 carbohydrate esterase 4
  • the cleaning composition of the invention comprises a polypeptide having Glyco_hydro_114 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 6 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 6.
  • the cleaning composition of the invention comprises a polypeptide having Glyco_hydro_114 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 7 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 7.
  • the cleaning composition of the invention comprises a polypeptide having Glyco_hydro_114 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 8 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 8.
  • the cleaning composition of the invention comprises a polypeptide having Glyco_hydro_114 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 9 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 9.
  • the cleaning composition of the invention may comprise any of the Glyco_hydro_1 14 glycosyl hydrolase polypeptides disclosed in WO 2018/185181 , the contents of which are incorporated herein by reference.
  • the Glyco_hydro_1 14 glycosyl hydrolase polypeptide When present in a cleaning composition of the invention, the Glyco_hydro_1 14 glycosyl hydrolase polypeptide will typically be present in an amount of from 0.01 to 1000 ppm, from 0.1 to 1000 ppm, from 1 ppm to 1000 ppm, from 10 ppm to 1000 ppm, from 50 ppm to 1000 ppm, from 100 ppm to 1000 ppm, from 150 ppm to 1000 ppm, from 200 ppm to 1000 ppm, from 250 ppm to 1000 ppm, from 250 ppm to 750 ppm, or from 250 ppm to 500 ppm, based on active protein.
  • the Glyco_hydro_1 14 glycosyl hydrolases above may be combined with one or more other cleaning enzyme in the composition, e.g. a hexosaminidase and/or a nuclease, to form a blend to be added to the wash liquor solution according to the invention.
  • one or more other cleaning enzyme in the composition e.g. a hexosaminidase and/or a nuclease
  • the concentration of the Glyco_hydro_1 14 glycosyl hydrolase in the wash liquor solution is typically in the range of from 0.00001 ppm to 10 ppm, from 0.00002 ppm to 10 ppm, from 0.0001 ppm to 10 ppm, from 0.0002 ppm to 10 ppm, from 0.001 ppm to 10 ppm, from 0.002 ppm to 10 ppm, from 0.01 ppm to 10 ppm, from 0.02 ppm to 10 ppm, from 0.1 ppm to 10 ppm, from 0.2ppm to 10 ppm, or from 0.5 ppm to 5 ppm.
  • the glycosyl hydrolase in cleaning compositions of the invention may be a GH39 glycosyl hydrolase that comprises the CAZY database domain GH39 (GH, CAZY database http://www.cazy.org/ (Coutinho & Henrissat, 1999).
  • the domain is a functional domain providing hydrolytic activity to the polypeptide.
  • the GH39 glycoside hydrolase family contains two known enzyme activities: b-xylosidase and a-L-iduronidase. Both enzyme activities cleave equatorial glycosidic bonds. The most highly conserved regions in these enzymes are located in their N- terminal sections (Henrissat et al. (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090-7094).
  • the polypeptides of the invention comprising a GH39 domain are homologues of PsIG enzymes, which are proteins that degrade the exopolysaccharide Psl.
  • Psl is a pentasaccharide comprising D-glucose, L-rhamnose and D-mannose, which acts as a glue in e.g. bacteria surface interactions.
  • PsIG is a protein involved in the synthesis of the biofilm matrix exopolysaccharide Psl in Pseudomonas aeruginosa.
  • the polypeptides in GH39 can be separated into distinct sub- clusters defined by particular motifs.
  • the cleaning composition of the invention comprises a polypeptide having GH39 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 10 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 10.
  • the cleaning composition of the invention comprises a polypeptide having GH39 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 1 1 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 1 1.
  • the cleaning composition of the invention comprises a polypeptide having GH39 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 12 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 12.
  • the cleaning composition of the invention may comprise any of the GH39 glycosyl hydrolase polypeptides disclosed in WO 2018/185150, the contents of which are incorporated herein by reference.
  • the GH39 glycosyl hydrolase polypeptide When present in a cleaning composition of the invention, the GH39 glycosyl hydrolase polypeptide will typically be present in an amount of from 0.01 to 1000 ppm, from 0.1 to 1000 ppm, from 1 ppm to 1000 ppm, from 10 ppm to 1000 ppm, from 50 ppm to 1000 ppm, from 100 ppm to 1000 ppm, from 150 ppm to 1000 ppm, from 200 ppm to 1000 ppm, from 250 ppm to 1000 ppm, from 250 ppm to 750 ppm, or from 250 ppm to 500 ppm, based on active protein.
  • the GH39 glycosyl hydrolases above may be combined with one or more other cleaning enzyme in the composition, e.g. a hexosaminidase and/or a nuclease, to form a blend to be added to the wash liquor solution according to the invention.
  • one or more other cleaning enzyme in the composition e.g. a hexosaminidase and/or a nuclease
  • the concentration of the GH39 glycosyl hydrolase in the wash liquor solution is typically in the range of from 0.00001 ppm to 10 ppm, from 0.00002 ppm to 10 ppm, from 0.0001 ppm to 10 ppm, from 0.0002 ppm to 10 ppm, from 0.001 ppm to 10 ppm, from 0.002 ppm to 10 ppm, from 0.01 ppm to 10 ppm, from 0.02 ppm to 10 ppm, from 0.1 ppm to 10 ppm, from 0.2ppm to 10 ppm, or from 0.5 ppm to 5 ppm.
  • the GHL13 glycosyl hydrolase polypeptides in cleaning compositions of the invention are BpsB and PgaB homologs comprising a GHL13 domain and with activity on the PNAG substrate. Some GHL13 glycosyl hydrolases also comprise the CE4 domain. Provided here are thus PgaA/BpsB homologs comprising a C-terminus glycosyl hydrolase domain (GHL13) and optionally a N-terminus deacetylase domain (CE4).
  • GHL13 glycosyl hydrolase activity may be determined according to the procedure described in Assay 7 herein.
  • the glycosyl hydrolase polypeptides comprise the Pfam database domain GHL13 (PFAM domain id PF14883, Pfam version 31.0 Finn (2016). Nucleic Acids Research, Database Issue 44:D279-D285), where this domain is a functional domain providing hydrolytic activity to the polypeptide.
  • the polypeptides preferably in addition to the GHL13 domain also comprise the CE4 domain (CE, CAZY database http://www.cazy.org/ (Coutinho & Henrissat, 1999) and have deacetylase activity.
  • the cleaning composition of the invention comprises a polypeptide having GHL13 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 13 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 13.
  • the cleaning composition of the invention comprises a polypeptide having GHL13 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 14 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 14.
  • the cleaning composition of the invention comprises a polypeptide having GHL13 glycosyl hydrolase activity and a sequence identity to the polypeptide shown in SEQ ID NO: 15 of at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100%.
  • the polypeptide has an amino acid sequence that comprises or consists of SEQ ID NO: 15.
  • the cleaning composition of the invention may comprise any of the GH39 glycosyl hydrolase polypeptides disclosed in WO 2018/185152, the contents of which are incorporated herein by reference.
  • the GHL13 glycosyl hydrolase polypeptide When present in a cleaning composition of the invention, the GHL13 glycosyl hydrolase polypeptide will typically be present in an amount of from 0.01 to 1000 ppm, from 0.1 to 1000 ppm, from 1 ppm to 1000 ppm, from 10 ppm to 1000 ppm, from 50 ppm to 1000 ppm, from 100 ppm to 1000 ppm, from 150 ppm to 1000 ppm, from 200 ppm to 1000 ppm, from 250 ppm to 1000 ppm, from 250 ppm to 750 ppm, or from 250 ppm to 500 ppm, based on active protein.
  • the GHL13 glycosyl hydrolase above may be combined with one or more other cleaning enzyme in the composition, e.g. a hexosaminidase and/or a nuclease, to form a blend to be added to the wash liquor solution according to the invention.
  • one or more other cleaning enzyme in the composition e.g. a hexosaminidase and/or a nuclease
  • the concentration of the GHL13 glycosyl hydrolase in the wash liquor solution is typically in the range of from 0.00001 ppm to 10 ppm, from 0.00002 ppm to 10 ppm, from 0.0001 ppm to 10 ppm, from 0.0002 ppm to 10 ppm, from 0.001 ppm to 10 ppm, from 0.002 ppm to 10 ppm, from 0.01 ppm to 10 ppm, from 0.02 ppm to 10 ppm, from 0.1 ppm to 10 ppm, from 0.2ppm to 10 ppm, or from 0.5 ppm to 5 ppm.
  • the cleaning compositions of the invention include at least two detergent enzymes selected from the group consisting of proteases, amylases, lipases, mannanases, pectate lyases and cellulases. These detergent enzymes are described in more detail below.
  • compositions will typically comprise at least a protease, for example a protease and an amylase.
  • the cleaning composition may comprise three, four, five or more detergent enzymes.
  • the cleaning composition comprises at least one protease, at least one amylase, at least one lipase, at least one mannanase, at least on pectate lyase, and at least one cellulase.
  • the composition may optionally include two or more different enzymes of one type, for example two proteases or two cellulases.
  • the composition may also contain one or more further enzymes such as a carbohydrase, a pectinase, an arabinase, a galactanase, a xylanase or an oxidase, e.g. a laccase and/or peroxidase.
  • a carbohydrase such as a carbohydrase, a pectinase, an arabinase, a galactanase, a xylanase or an oxidase, e.g. a laccase and/or peroxidase.
  • Suitable proteases for the compositions of the invention include those of bacterial, fungal, plant, viral or animal origin, although those of microbial origin are preferred, including chemically modified or protein engineered variants.
  • the protease may be an alkaline protease, such as a serine protease or a metalloprotease.
  • a serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as subtilisin.
  • a metalloprotease may for example be a thermolysin from e.g. family M4 or another metalloprotease such as those from the M5, M7 or M8 families.
  • subtilase proteases are those derived from Bacillus such as Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii, described in e.g. US 7262042 and WO 2009/021867, Subtilisin lentus, Subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168, and e.g. protease PD138 (described in WO 93/18140).
  • Other useful proteases include e.g.
  • trypsin-like proteases are trypsin (e.g. of porcine or bovine origin), the Fusarium protease described in WO 94/25583 and WO 2005/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 2005/052161 and WO 2005/052146.
  • protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 95/23221 , and variants thereof which are described in e.g. WO 92/21760, WO 95/23221 , EP 1921 147 and EP 1921 148.
  • metalloproteases are the neutral metalloprotease as described in WO 2007/044993 such as those derived from Bacillus amyloliquefaciens.
  • proteases are the variants described in: WO 89/06279, WO 92/19729, WO 96/034946, WO 98/201 15, WO 98/201 16, WO 99/01 1768, WO 01/44452, WO 03/006602, WO 2004/03186, WO 2004/041979, WO 2007/006305, WO 201 1/036263, WO 201 1/036264, WO 2014/207227 and WO 2016/087617, especially variants with substitutions in one or more of the following positions: 3, 4, 9, 15, 24, 27, 42, 55, 59, 60, 66, 74, 85, 96, 97, 98, 99, 100, 101 , 102, 104, 1 16, 1 18, 121 , 126, 127, 128, 154, 156, 157, 158, 161 , 164, 176, 179, 182, 185, 188, 189, 193, 198, 199, 200,
  • the protease variants may comprise one or more of the mutations selected from the group consisting of: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G1 16V, G1 16R, H1 18D, H1 18N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, G157P, S158E, Y161A,
  • protease variants are preferably variants of the Bacillus lentus protease (Savinase®) shown in SEQ ID NO: 24 or the Bacillus amyloliquefaciens protease (BPN’) shown in SEQ ID NO: 25, preferably variants having at least 80% sequence identity to one of these two sequences.
  • protease is the TY145 protease of SEQ ID NO: 26 or a variant thereof.
  • Preferred variants of this protease are those comprising a substitution at one or more positions corresponding to positions 171 , 173, 175, 179 or 180 of SEQ ID NO: 26, wherein the variant has a sequence identity of at least 75% to SEQ ID NO: 26.
  • Suitable variants of SEQ ID NO: 26 are disclosed e.g. in WO 2015/014790, WO 2016/097350, WO 2016/097352, WO 2016/097357 and WO 2016/097354, the contents of which are incorporated herein by reference.
  • Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Duralase Tm , Durazyrn Tm , Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® Excel and Progress® In (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect Ox®, Purafect OxP®, Puramax®, FN2®, FN3®, FN4®, Excellase®, Excellenz P1000TM, Excellenz P
  • Preferred proteases for use in the cleaning compositions of the present invention include a) variants of the polypeptide of SEQ ID NO: 24 having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97% or at least 98% sequence identity to SEQ ID NO: 24; b) variants of the polypeptide of SEQ ID NO: 26 having at least 80%, at least 85%, at least 90%, or at least 95% sequence identity to SEQ ID NO: 26; and c) variants of the polypeptide of SEQ ID NO: 37 having at least 90%, at least 95%, at least 96%, at least 97% or at least 98% sequence identity to SEQ ID NO: 37.
  • One preferred protease for use in the cleaning compositions of the present invention is a variant of the polypeptide of SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P.
  • Another preferred protease for use in the cleaning compositions of the present invention is a variant of the polypeptide of SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E.
  • Another preferred protease for use in the cleaning compositions of the present invention is a variant of the polypeptide of SEQ ID NO: 26 with the substitutions S27K, N109K, S1 1 1 E, S171 E, S173P, G174K, S175P, F180Y, G182A, L184F, Q198E, N199K and T297P, corresponding to the polypeptide of SEQ ID NO: 37.
  • amylases include alpha-amylases and/or glucoamylases and may be of bacterial orfungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1 ,296,839.
  • Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 264, 304, 305, 391 , 408, and 444.
  • amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.
  • amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof.
  • Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181 , N190, M197, 1201 , A209 and Q264.
  • hybrid alpha-amylase comprising residues 1 -33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36- 483 of SEQ ID NO: 4 are those having the substitutions:
  • amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99/019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181 , G182, H183, G184, N195, I206, E212, E216 and K269.
  • Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184.
  • Additional amylases which can be used are those having SEQ ID NO: 1 , SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96/023873 or variants thereof having 90% sequence identity to SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7.
  • Preferred variants of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181 , 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181 , 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184.
  • Most preferred amylase variants of SEQ ID NO: 1 , SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.
  • amylases which can be used are amylases having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01/66712.
  • Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201 , 207, 21 1 and 264.
  • amylases having SEQ ID NO: 2 of WO 09/061380 or variants having 90% sequence identity to SEQ ID NO: 2 thereof.
  • Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131 , T165, K178, R180, S181 , T182, G183, M201 , F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475.
  • More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131 I, T165I, K178L, T182G, M201 L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183.
  • Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions:
  • variants are C- terminally truncated and optionally further comprises a substitution at position 243 and/or a deletion at position 180 and/or position 181 .
  • amylases having SEQ ID NO: 1 of W013184577 or variants having 90% sequence identity to SEQ ID NO: 1 thereof.
  • Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: K176, R178, G179, T180, G181 , E187, N192, M199, I203, S241 , R458, T459, D460, G476 and G477.
  • More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241 QADN, R458N, T459S, D460T, G476K and G477K and/or deletion in position R178 and/or S179 or of T180 and/or G181.
  • Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
  • variants optionally further comprise a substitution at position 241 and/or a deletion at position 178 and/or position 179.
  • amylases having SEQ ID NO: 1 of W010104675 or variants having 90% sequence identity to SEQ ID NO: 1 thereof.
  • Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: N21 , D97, V128 K177, R179, S180, 1181 , G182, M200, L204, E242, G477 and G478.
  • SEQ ID NO: 1 More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: N21 D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K and G478K and/or deletion in position R179 and/or S180 or of 1181 and/or G182. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
  • variants optionally further comprise a substitution at position 200 and/or a deletion at position 180 and/or position 181.
  • suitable amylases are the alpha-amylase having SEQ ID NO: 12 in WO01/66712 or a variant having at least 90% sequence identity to SEQ ID NO: 12.
  • Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01/66712: R28, R118, N174; R181 , G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471 , N484.
  • Preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R1 18K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions.
  • amylase variants such as those described in WO201 1/098531 , WO2013/001078 and WO2013/001087.
  • amylases are DuramylTM, TermamylTM, FungamylTM, StainzymeTM, Stainzyme PlusTM, NatalaseTM, Liquozyme X, BANTM, Amplify® and Amplify® Prime (from Novozymes A/S), and RapidaseTM, PurastarTM/EffectenzTM, Powerase, Preferenz S1000, Preferenz S100 and Preferenz S1 10 (from Genencor International Inc./DuPont).
  • the cleaning composition of the invention comprises an amylase which is a variant of the polypeptide of SEQ ID NO: 27 with the mutations W140Y, N195F, D183 * , G184 * , V206Y, Y243F, E260G, G304R and G476K.
  • the cleaning composition of the invention comprises an amylase which is a variant of the polypeptide of SEQ ID NO: 27 with the mutations H 1 * , G7A, G109A, W140Y, N195F, D183 * , G184 * , V206Y, Y243F, E260G, N280S, G304R, E391A and G476K.
  • the cleaning composition of the invention comprises an amylase which is a variant of the polypeptide of SEQ ID NO: 28 with the mutations M9L, G149A, R1 18K, G182T, D183 * , G184 * , G186A, N195F, T246V, T257I, Y295F, N299Y, M323T, A339S and E345R.
  • the cleaning composition of the invention comprises an amylase which is a variant of the polypeptide of SEQ ID NO: 28 with the mutations R1 18K, D183 * , G184 * , N195F, R320K and R458K.
  • the cleaning composition of the invention comprises an amylase which is a variant of the polypeptide of SEQ ID NO: 28 with the mutations M9L, G149A, R1 18K, G182T, D183 * , G184 * , G186A, N195F, M202L, T257I, Y295F, N299Y, M323T, A339S and E345R.
  • the cleaning composition of the invention comprises an amylase which is a variant of the polypeptide of SEQ ID NO: 29 with the mutations H1 * , N54S, V56T, K72R, G109A, F1 13Q, R1 16Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K.
  • the cleaning composition of the invention comprises an amylase which is a variant of the polypeptide of SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T.
  • Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp.
  • Thermomyces e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216
  • cutinase from Humicola e.g. H. insolens
  • strain SD705 (W095/06720 & W096/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyces lipases (W010/065455), lipase from Thermobifida fusca (W01 1/084412), Geobacillus stearothermophilus lipase (W01 1/084417), lipase from Bacillus subtilis (W01 1/084599), and lipase from Streptomyces griseus (W01 1/150157) and S. pristinaespiralis (W012/137147).
  • lipase variants such as those described in EP407225, WO92/05249, WO94/01541 , W094/25578, W095/14783, WO95/30744, W095/35381 , W095/22615,
  • Preferred commercial lipase products include LipolaseTM, LipexTM, LipolexTM and LipocleanTM (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades).
  • lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (W010/11 1 143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (W010/100028).
  • the cleaning composition of the invention comprises a lipase which is a variant of the polypeptide of SEQ ID NO: 31.
  • the cleaning composition of the invention comprises a lipase which is a variant of the polypeptide of SEQ ID NO: 31 with the mutations T231 R and N233R.
  • the cleaning composition of the invention comprises a lipase which is a variant of the polypeptide of SEQ ID NO: 31 with the mutations N33Q, G91 Q, E210Q, T231 R, N233R and I255A.
  • the cleaning composition of the invention comprises a lipase which is a variant of the polypeptide of SEQ ID NO: 31 with the mutations E1 C, D27R, G38A, F51V, D96E, K98I, D1 1 1A, G163K, H198S, Y220F, T231 R, N233C, D254S and P256T.
  • the cleaning composition of the invention comprises a lipase which is a variant of the polypeptide of SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D1 1 1A, G163K, T231 R, N233R, D254S and P256T.
  • Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • the mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens.
  • Suitable mannanases are described e.g. in WO 1999/064619. A commercially available mannanase is Mannaway® (Novozymes A/S).
  • the cleaning composition of the invention comprises a mannanase with the amino acid sequence of SEQ ID NO: 32.
  • a pectate lyase is an enzyme that catalyzes the random cleavage of alpha-1 ,4- glycosidic linkages in pectic acid, also known as polygalacturonic acid, by transelimination.
  • Pectate lyases include the enzyme class polygalacturonate lyase (EC 4.2.2.2) (PGL), also known as poly(1 ,4-alpha-D-galacturonide) lyase.
  • Suitable pectate lyases include those of bacterial or fungal origin. Chemically or genetically modified pectate lyase are included. Pectate lyases have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas. Also from Bacillus subtilis (Nasser et al. (1993) FEBS 335:319-326) and Bacillus sp. YA-14 (Kim et al. (1994) Biosci. Biotech. Biochem. 58:947-949) cloning of a pectate lyase has been described. Variants of a pectate lyase from Bacillus subtilis have been disclosed in WO 2002/092741 and WO 2003/095638.
  • pectate lyases include Xpect® (Novozymes, A/S), Pectawash® (Novozymes, A/S) and Pectaway® (Novozymes, A/S).
  • the cleaning composition of the invention comprises a pectate lyase with the amino acid sequence of SEQ ID NO: 33.
  • Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include those from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, or Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691 ,178, US 5,776,757 and WO 89/09259.
  • cellulases are the alkaline or neutral cellulases having colour care benefits.
  • Examples of such cellulases are those described in EP 0 495 257, EP 0 531 372, WO 96/1 1262, WO 96/29397, WO 98/08940.
  • Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471 , WO 98/12307 and W099/001544.
  • cellulases are e.g. an endo-beta-1 ,4-glucanase enzyme having a sequence of at least 97% identity to the amino acid sequence of positions 1-773 of SEQ ID NO:2 of WO 02/099091 or a family 44 xyloglucanase, which a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40-559 of SEQ ID NO: 2 of WO 01/062903.
  • cellulases include CelluzymeTM, and CarezymeTM (Novozymes A/S) Carezyme PremiumTM (Novozymes A/S), CellucleanTM (Novozymes A/S), Celluclean ClassicTM (Novozymes A/S), CellusoftTM (Novozymes A/S), WhitezymeTM (Novozymes A/S), ClazinaseTM, and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (Kao Corporation).
  • the cleaning composition of the invention comprises a cellulase with the amino acid sequence of SEQ ID NO: 34.
  • the cleaning composition of the invention comprises a cellulase with the amino acid sequence of SEQ ID NO: 35.
  • the cleaning composition of the invention comprises two cellulases, in particular a cellulase with the amino acid sequence of SEQ ID NO: 34 and a cellulase with the amino acid sequence of SEQ ID NO: 35.
  • the cleaning composition of the invention comprises a xyloglucanase with the amino acid sequence of SEQ ID NO: 36.
  • Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
  • a suitable peroxidase is a peroxidase enzyme comprised by the enzyme classification EC 1.1 1.1.7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity.
  • peroxidases examples include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.
  • Commercially available peroxidases include GuardzymeTM (Novozymes A/S).
  • haloperoxidase enzymes such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity.
  • Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.1 1.1.10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase.
  • Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • Caldariomyces e.g., C. fumago
  • Alternaria Curvularia
  • Curvularia e.g., C. verruculosa and C. inaequalis
  • Drechslera Ulocladium and Botrytis.
  • Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.
  • a suitable oxidase also includes any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1 ), an o-aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
  • Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N.
  • crassa Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P. papilionaceus, Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S.
  • thermophilum Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2238885).
  • Suitable examples from bacteria include a laccase derivable from a strain ot Bacillus.
  • a laccase derived from Coprinopsis or Myceliophthora is preferred; in particular, a laccase derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora thermophila, as disclosed in WO 95/33836.
  • the cleaning composition of the invention in its broadest aspect comprises at least two cleaning enzymes selected from the group consisting of nucleases, hexosaminidases and glycosyl hydrolases and at least two detergent enzymes selected from the group consisting of proteases, amylases, lipases, mannanases, pectate lyases and cellulases.
  • the invention relates to a cleaning composition
  • a cleaning composition comprising 1 ) at least two cleaning enzymes selected from the group consisting of nucleases, hexosaminidases and glycosyl hydrolases, wherein the nuclease is a DNase or an RNase, and the glycosyl hydrolase is a Glyco_hydro_1 14, GH39 or GHL13 glycosyl hydrolase; and 2) at least two detergent enzymes selected from the group consisting of proteases, amylases, lipases, mannanases, pectate lyases and cellulases.
  • compositions of the invention will typically comprise a cleaning enzyme selected from at least two of the categories nucleases, hexosaminidases and glycosyl hydrolases.
  • the compositions will typically comprise one of the following combinations: a) at least one nuclease and at least one hexosaminidase; b) at least one nuclease and at least one glycosyl hydrolase; or c) at least one hexosaminidase and at least one glycosyl hydrolase.
  • the compositions may of course comprise one or more enzymes from each of these groups, i.e. at least one nuclease, at least one hexosaminidase and at least one glycosyl hydrolase.
  • compositions comprising a DNase and a Glvco hydro 114 polypeptide
  • One aspect of the invention relates to a cleaning composition
  • a cleaning composition comprising at least a DNase and a Glyco_hydro_1 14 glycosyl hydrolase as the cleaning enzymes. Exemplary embodiments of this aspect of the invention are described below.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 6, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 6;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • o the amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T; o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 7, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 7;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ I D NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 8, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 8;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 9, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 9;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 2, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 2;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 6, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 6;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and • at least one enzyme selected from the group consisting of amylases and cellulases; wherein:
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 2, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 2;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 7, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 7;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33; and o the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 2, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 2;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 8, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 8;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylases • at least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases; wherein: o the amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 2, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 2;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 9, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 9;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises: • a DNase that comprises or consists of SEQ ID NO: 2;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 3, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 3;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 6, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 6;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 3, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 3;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 7, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 7;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 3, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 3;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 8, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 8;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and • at least one enzyme selected from the group consisting of amylases and cellulases; wherein:
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 3, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 3;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 9, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 9;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33; and o the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 4, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 4;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 6, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 6;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylases • at least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases; wherein: o the amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 4, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 4;
  • Glyco_hydro_114 polypeptide that comprises or consists of SEQ ID NO: 7, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 7;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises: • a DNase that comprises or consists of SEQ ID NO: 4;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 4, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 4;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 8, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 8;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 4, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 4;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 9, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 9;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 5, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 5;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 6, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 6;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and • at least one enzyme selected from the group consisting of amylases and cellulases; wherein:
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 5, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 5;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 7, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 7;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33; and o the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 5, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 5;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 8, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 8;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • amylases • at least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases; wherein: o the amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 5, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 5;
  • Glyco_hydro_1 14 polypeptide that comprises or consists of SEQ ID NO: 9, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 9;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises: • a DNase that comprises or consists of SEQ ID NO: 5;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D1 1 1A, G163K, T231 R, N233R, D254S and P256T;
  • o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F1 13Q, R1 16Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N 195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the cleaning composition may optionally comprise one or more of any of the other cleaning enzymes described herein. Any of these compositions may thus comprise one or more of an RNase, a GH39 glycosyl hydrolase, a GHL13 glycosyl hydrolase or a hexosaminidase.
  • compositions comprising a DNase and a GH39 polypeptide
  • One aspect of the invention relates to a cleaning composition
  • a cleaning composition comprising at least a DNase and a GH39 glycosyl hydrolase as the cleaning enzymes. Exemplary embodiments of this aspect of the invention are described below.
  • the composition comprises: • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 10;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • amylases and cellulases • at least one enzyme selected from the group consisting of amylases and cellulases; wherein: o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 1 ;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises: • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 12;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • o the amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T; o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 2, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 2;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 10;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10
  • a protease that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P, or that comprises SEQ ID NO: 37;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 2, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 2;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 1 ;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 2, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 2;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 12;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 3, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 3;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 10;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and • at least one enzyme selected from the group consisting of amylases and cellulases; wherein:
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 3, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 3;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 1 ;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33; and o the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 3, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 3;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 12;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • amylases • at least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases; wherein: o the amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 4, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 4;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 10;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises: • a DNase that comprises or consists of SEQ ID NO: 4;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 4, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 4;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 1 ;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 4, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 4;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 12;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 5, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 5;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 10;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 10;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and • at least one enzyme selected from the group consisting of amylases and cellulases; wherein:
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 5, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 5;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 1 ;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33; and o the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 11 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 5, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 5;
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 12;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • amylases • at least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases; wherein: o the amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D1 1 1A, G163K, T231 R, N233R, D254S and P256T;
  • o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a GH39 polypeptide that comprises or consists of SEQ ID NO: 12;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F1 13Q, R1 16Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N 195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the cleaning composition may optionally comprise one or more of any of the other cleaning enzymes described herein. Any of these compositions may thus comprise one or more of an RNase, a Glyco_hydro_1 14 glucosyl hydrolase, a GHL13 glycosyl hydrolase or a hexosaminidase.
  • compositions comprising a DNase and a GHL13 polypeptide
  • One aspect of the invention relates to a cleaning composition
  • a cleaning composition comprising at least a DNase and a GHL13 glycosyl hydrolase as the cleaning enzymes. Exemplary embodiments of this aspect of the invention are described below.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • GHL13 polypeptide that comprises or consists of SEQ ID NO: 13, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 13;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E;
  • the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • a GHL13 polypeptide that comprises or consists of SEQ ID NO: 14, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 14;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33;
  • the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • a protease that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and • at least one enzyme selected from the group consisting of amylases and cellulases; wherein:
  • o the amylase comprises SEQ ID NO: 29 with the mutations H 1 * , N54S, V56T, K72R, G109A, F113Q, R116Q, W167F, Q172G, A174S, G182 * , D183 * , G184T, N195F, V206L, K391A, P473R and G476K; and o the cellulase comprises SEQ ID NO: 34.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 , or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 1 ;
  • a GHL13 polypeptide that comprises or consists of SEQ ID NO: 15, or which is a variant thereof having at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% sequence identity to SEQ ID NO: 15;
  • a protease selected from: a) a polypeptide that comprises or consists of SEQ ID NO: 24 or SEQ ID NO: 26, or a variant thereof having at least 80%, at least 85%, at least 90% or at least 95% sequence identity to SEQ ID NO: 24 or SEQ ID NO: 26; b) a polypeptide that comprises SEQ ID NO: 24 with the substitutions Y161A, R164S and A188P; c) a polypeptide that comprises SEQ ID NO: 24 with the substitutions S9E, N42R, N74D, V199I, Q200L, Y203W, S253D, N255W and L256E; and d) a polypeptide that comprises SEQ ID NO: 37; and
  • At least one enzyme selected from the group consisting of amylases, lipases, mannanases, pectate lyases and cellulases.
  • the composition comprises:
  • a DNase that comprises or consists of SEQ ID NO: 1 ;
  • amylase comprises SEQ ID NO: 30 with the mutations H183 * , G184 * , I405L, A421 H, A422P and A428T;
  • o the lipase comprises SEQ ID NO: 31 with the mutations D27R, G38A, D96E, D11 1A, G163K, T231 R, N233R, D254S and P256T; o the mannanase comprises SEQ ID NO: 32;
  • o the pectate lyase comprises SEQ ID NO: 33; and o the cellulase comprises SEQ ID NO: 34 or SEQ ID NO: 35.
  • the composition comprises:

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Abstract

La présente invention concerne une composition de nettoyage comprenant au moins deux enzymes de nettoyage choisies dans le groupe constitué de nucléases, d'hexosaminidases et de glycosyl hydrolases, et au moins deux enzymes détergentes choisies dans le groupe constitué par les protéases, les amylases, les lipases, les collagénases, les pectate lyases et les cellulases.
PCT/EP2019/076825 2018-10-03 2019-10-03 Compositions de nettoyage Ceased WO2020070249A1 (fr)

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