TW201035407A - Enzymatic textile bleach-whitening methods - Google Patents

Abstract

A method for bleach-whitening of synthetic textile material is provided comprising contacting said textile material with (a) an enzymatic textile bleaching composition comprising (i) a perhydrolase enzyme, (ii) an ester substrate for said perhydrolase enzyme, (iii) a hydrogen peroxide source, (iv) a surfactant and/or an emulsifier, (v) a peroxide stabilizer, (vi) a sequestering agent, (vii) a buffer which maintains a pH of about 6 to about 8, and (b) at least one fluorescent whitening agent, and, optionally, (c) at least one acid or disperse shading dye for shaded variations of white, for a length of time and under conditions suitable to permit measurable whitening of the textile material, thereby producing a bleached-whitened textile material.

Description

201035407 VI. Description of the invention: [Technical field to which the invention pertains] In particular, the invention relates to an enzyme bleaching/whitening synthetic fabric material. A method of making a fabric material or a fabric material containing polyamine. [Prior Art] Second, when the fabric material such as fiber, yarn or fabric is blocked, the processing or preparation steps are typically taken to properly prepare the 哕箄 _ eight-step use of the monthly money table 忒 4 fabric material for input « It is used in commercial items typically and in the finishing stage. These fabric treatment steps remove the impurities and hairs that are added to the fibers and/or fabrics that are naturally present and woven, so that although the fabric treatment can be different, the treatment and stages of the old sputum are _$ χ π & However, the most common treatments include: "Removal by enzyme, test or oxidative soaking, such as the aggregation of the powder on the temple; refining, that is, by the temperature close to the boiling point", the contact of sodium hydroxide solution In addition to grease, oils, white fats; and bleaching, that is, usually using oxygen (four) j (such as over = 虱 - human citrate and dioxide) or using a reducing agent (such as sulfur dioxide or sulfite) from the fabric In addition to the color body and lightening the color body. The polyamine fiber bleaching-whitening procedure currently used is usually carried out in the presence of a reducing agent such as stabilized (buffered) sodium dithionite. The known deficiencies of these procedures are related to the ecological $(odor, waste water, etc.) and the yellowing problems encountered in subsequent drying when the residual sulfur derivative is not properly and sufficiently removed from the fabric material. θ does not show the above defects and the white effect achieved is significantly improved compared to the whitening obtained by reducing bleaching, so that the enzyme-based 201035407 white-whitening procedure that constitutes the new benchmark will be desirable. Whitening enzyme fabric bleaching and whitening procedures, compared to conventional fabric bleaching - 曰- 目, which minimizes the adverse environmental impact of the fabric. Absorbing... Changing again The problem shown is mainly solved by the method described below. Enzymatic bleaching-whitening Ο 发明 发明 :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: :: , 仓—π β 兴 I 3 is in contact with the following materials—to make the fabric material: touch & time, thereby producing a bleached-whitened fabric material (a) an enzyme fabric bleaching composition comprising: i) perhydrolase enzyme, (11) ester of the perhydrolase enzyme, (out) hydrogen peroxide source, (1V) surfactant and / or emulsifier, (v) peroxide stabilizer, ( Vi) a chelating agent, b) a buffer which maintains a cation of from about 6 to about 8; and a fluorescent whitening agent; and optionally a color difference of white (e.g., -variation) S夂 or knifeing dye. The subject matter of the present invention provides a bleaching and whitening synthetic fabric material, particularly a polyamine fabric material or a contact with an enzymatic bleaching composition for a period of time. A method of fabricizing a polyamide material which is capable of achieving an all white effect. In another aspect, the invention is also applicable to the present invention also providing dyed fabrics made from fabrics prepared according to the enzyme bleaching-whitening process described herein. [Embodiment] The enzyme bleaching-whitening procedure of the present invention is environmentally friendly compared to the whitening obtained by conventional reductive bleaching, and the provision does not exhibit subsequent drying when the residual sulfur derivative is not properly and sufficiently removed. A synthetic fabric material that will encounter yellowing problems. Unless otherwise indicated, the enzymatic bleaching step of the present invention will employ conventional techniques of knives biology (including recombinant techniques), microbiology, cell biology, and biotechnology, which are within the skill of the art. Inside. Such techniques are fully described, for example, in the following documents: d (10), 2nd edition, (Sambr〇〇k et al., 1989); • Mind (MJ Gait, 198; b 〇/〇灯(FM) Ausubel et al., 1994); Pd 7Tje Po/jmerwe i?eac"0„ (Mullis et al., ed., 1994, 'Anti-Gene Transfer and Expression: A Laboratory Manual (Kriegler, 1990) ° unless otherwise defined herein' All technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which the invention pertains. 201035407 The following documents provide those skilled in the art with a number of biotechnology-related techniques used in the present invention. General dictionary explanation: Singlet〇n et al,

Dictionary of Microbiology and Molecular Biology, 2nd edition, John Wiley and Sons, New York (1994); and Hale and Markham,

The Harper Collins Dictionary of Biology, Harper Perennial, New York (1991). Any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention. Numerical ranges provided herein include numbers that define the range. Unless otherwise indicated, the nucleic acids are written from left to right in the range of 51 to 3, respectively; the amino acid sequence is written from the left to the right in the amino to carboxy position. As used herein, the term "bleaching" means treating a fabric material to the fabric material by removing, modifying or masking the color-forming compound in the fabric material for a sufficient period of time and under appropriate pH and temperature conditions. A program that produces a lighter color. Thus, "bleaching" refers to the treatment of fabric materials to effect whitening of the fabric material.

As used herein, the term "bleach" encompasses any portion that is capable of bleaching the fabric. It may require the presence of a bleach activator. Bleaching can generally be carried out using chemical bleaches and/or enzymatic bleaches. Examples of suitable chemical bleaches which can be used in the procedures and methods described herein are sodium peroxide, sodium perborate, potassium permanganate and peracid. In some aspects, H2〇2 produced on the spot can be considered a chemical bleach. "Chemical Bleaching Composition" contains one or more chemical bleaches. An aqueous bleaching composition as described in the context of the present invention contains one or more esterase-based whitening systems capable of producing bleaching agents, or "enzyme-type perhydrolase enzymes" and one or more substrates, and for producing Peracid bleaching 7 Hydrogen peroxide source of 201035407. These enzyme bleaching systems are described, for example, in WO 2005/056782. The term "synthetic fabric material" comprises polyamine, polyurethane, polyacrylic acid. , poly vinegar, poly-hydrocarbon, | propylene vinegar and semi-synthetic materials such as cellulose acetate. The fabric materials cited may take a variety of forms, such as in the form of fibers, yarns, fabrics, garments, knits, knits, and non-woven fabrics. The term "polyamide fabric material or fabric material containing polyamine" comprises synthetic polyamines such as Nylon 6 (polyhexylamine), nylon 6,6 (called 〇116,6). ) (polyhexamethylenediamine), nylon 7 (々1〇117) (polyheptylamine), nylon 6,12 (Nyl〇n6,12) (polydodecanedihexamethylenediamine) , nylon 11 (outer 1〇1111) 'Nylon 12 (outer 1〇1112), and nylon 6,6 or nylon 6 copolymerized guanamine, such as from hexamethylenediamine, hexamethyleneamine and adipic acid a polymer produced, and a polymer prepared from adipic acid, hexamethylenediamine and isophthalic acid or from adipic acid, hexamethyleneamine and 2-mercapto-pentanediamine or 2-ethyl-butanediamine . It also covers blends such as polyamide/wool, polyamide/polyacrylonitrile, polyamine/cellulose, polyamide/polyester, polyamine/cellulose acetate, polyamine/triacetic acid Blends of cellulose, polyamide/cellulose/wool, and blends of all of the above blends with elastomeric fibers. "Perhydrolase" means a fermentation which is capable of catalyzing a perhydrolysis reaction resulting in the production of a sufficient amount of peracids suitable for use in an enzyme fabric bleaching composition according to the methods described herein. Forced in the formula & (4) hydrolyzed _ sulin generally exhibits a high perhydrolysis: hydrolysis ratio. In some embodiments, the perhydrolase comprises the M. smegmatis (10) heart perhydrolase amino acid sequence set forth in SEQ ID NO: 1 or a variant or homolog thereof, the aminoguanidine sequence or variant thereof from 201035407 Or a homologue consists of, or consists essentially of, the amino acid sequence or a variant or homolog thereof. In some embodiments, the perhydrolase enzyme comprises bryotransferase activity and catalyzes an aqueous thiol transfer reaction. Peracid is an organic acid of the formula RC(-0)00H wherein r is an aliphatic, aromatic or araliphatic group. The "ester acceptor" of the enzyme fabric bleaching composition of the present invention described herein means a perhydrolase substrate containing an ester bond. Esters containing aliphatic and/or aromatic carboxylic acids and alcohols can be used as substrates for perhydrolase enzymes. In a specific example, the ester source is selected from the group consisting of one or more of the following acid esters: formic acid, acetic acid, propionic acid, butyric acid, valeric acid, caproic acid, caprylic acid, capric acid, capric acid, dodecanoic acid, Myristic acid, palmitic acid, stearic acid and oleic acid. In some embodiments, the ester source is an acetate. In some embodiments, the ester source is selected from one or more of propylene glycol diacetate, ethylene glycol diacetate, triacetin, ethyl acetate, and tributyrin. As used herein, the term "perhydrolysis" refers to the reaction of a peracid from a source of an ester and a source of hydrogen peroxide. The perhydrolysis reaction is catalyzed by a perhydrolase enzyme such as a bryotransferase or an aryl acetamide. In some specific examples, the peracid is produced by pervaporating an ester of the formula rc(=〇)〇r* in the presence of hydrogen peroxide (H2〇2), wherein MR, the same or different organic moiety. In a specific example, -OR,_0H. In a specific example, _〇R* is replaced by a brewing. In some specific examples, a peracid or a guanamine is used to produce a peracid. As used herein, the term "peracid" refers to a molecule derived from a slow-motion vinegar that reacts with hydrogen peroxide to form a meta-active product of 201035407 capable of transferring an oxygen atom. This transfer of enthalpy makes the peracid (such as peracetic acid) act as a bleaching agent. "Over hydrolysis: hydrolysis ratio .B". The amount of peracid produced by the hydrolyzing enzyme from the hydrolyzed enzyme and the amount of acid produced by the enzyme and the specific sheep in the prescribed conditions and within the prescribed time. In some embodiments, the ~7" check is provided in WO 05/056782 to determine the amount of peracid and acid produced by the use of the enzyme. As used herein, "effective amount of perhydrolase enzyme" refers to the amount of perhydrolase enzyme necessary to achieve the desired enzyme activity in the procedures or methods described herein. Such effective escrow is determined by the general practitioner and is based on a variety of factors, such as the particular enzyme used, the pH used, the temperature used, and the like, and the desired result (eg, bleaching process, . As used herein, the term "transferase" refers to a kinesin that promotes the transfer of a 1-functional group from one substrate to another. For example, thiol transferase can transfer a thiol-transferase. To the peroxidized gas milk and shellfish, thereby forming a peracid.

As used herein, the term "baseline refers to borrowing"? The organic base of the formula RCO-, which is formed by the removal of the -OH group from an organic acid, "「 。. Typically, ending with a suffix - 〇yl" The base name J such as acetamidine (CH3C0-C1) is helium formed from acetic acid (CH3CO-〇H). As used herein, the term "deuterated" is a substituent of a molecule, a chemical conversion by a thiol group substitution, or a procedure in which a thiol group is used in eight molecules. As used herein, "the oxidizing chemical At丄J has a chemical that bleaches the fabric's monthly b-force. The oxidizing chemical exists in a suitable, a, /, white, ρ, and temperature. The term includes (but not Limited to) m-hydrogen and peracid. As used herein, the term "purified KJ and "isolated" refers to the removal of /y dye from 201035407, and/or from at least - fm , ^ species, and Injury removes its natural related pages (eg, proteins, nucleic acids, cells, etc.) means that it is essentially 太 又 又 又 八 八 姊 5 5 5 5 5 5 5 5 5 5 5 5 5 ύ ύ ύ ύ ύ ύ ύ ύ ύ ύ ύ ύ ύ ύ ύ ύ The material of the component. As used herein, the term "multiple JZ Λ4 . . . + J J 4 has any length and any two-dimensional structure and a single or multiple strand (eg, single-stranded, etc.) nucleotide polymerization form, containing red A version of the system /, 3 has depurinated ribonucleotides, ribonucleoside glucosides and / or deoxyribonucleotides or Μ々 ^ Μ Μ Μ Μ 或 或 or modified forms Nucleic acid or base or analog thereof. Because of the degeneracy of the genetic code, more than one codon can be used to encode a specific amino acid, and it is applied to the present invention in the case of φ 夕 > _ is (4) The polynucleic acid in the code encodes a specific amino acid sequence. Any type of core (iv) or acid analog can be used as long as the polynucleic acid retains the desired functional group under the conditions of use, and the desired functional group includes an increase. Modification of nuclease resistance (eg, deoxygenation, 2, 〇-heart, thiopurine, etc.). For detection or capture purposes, it may also be labeled with a radioactive or non-radioactive label or anchor. For example, biotin. The term polynucleotide also includes peptide nucleic acid (PNA). Polynucleic acid may be naturally occurring or non-naturally occurring. The terms "polynucleotide" and "nucleic acid" and "nucleotide" are used interchangeably herein. The polynucleotide of the present invention may contain RNA, DNA or both, and/or modified forms and/or the like. The nucleotide sequence may be heterozygous with a non-nucleotide component. One or more phosphodiester bonds can be replaced by an alternative linking group. Such alternative linking groups include, but are not limited to, phosphate esters via P(0)S ("thiolates"), P(s)s ("dithiolates, (0)NR2 ("guanamines" Specific examples of substitutions of ")", P(〇)R, p(0)0R,, CO or ch2 ("acetal"), wherein each R or R, independently, is Η, or contains a bond as appropriate in 201035407 a substituted or unsubstituted alkyl group (Ci_C2〇) of a (-〇-) bond, an aryl group, a aryl group, a cycloalkyl group, a cycloalkyl group or an aryl group. The bonds required for the polynuclear acid are not all the same. The acid can be linear or toroidal, or a combination of a straight bond and a toroidal moiety. Suitable polynucleotides are described in WO 2005/056782. As used herein, 'polypeptide' refers to any amino acid containing and is familiar to The skilled artisan recognizes the composition of the protein. This article uses the conventional one-letter or three-letter code of the amino acid residue. The terms "polypeptide" and "protein" are used interchangeably herein. An amino acid polymer of any length. The polymer may be linear or branched, it may comprise a modified amino acid, and it may be miscible with a non-amino acid. Also encompasses amino acid polymers that have been naturally modified or modified with the following interventions; for example, formation of disulfide bonds: glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation or modification, such as with labeled components Also included in the definition are, for example, polypeptides containing one or more amino acid analogs (including, for example, unnatural amino acids, etc.) and other modifications known in the art. As used herein, the term "similar sequence" "Homologous protein", "wild-type or natural protein", "wild-type sequence", "native sequence", "naturally occurring sequence", "wild-type gene", "related protein", "derived protein" and " "Variable proteins" are familiar to those skilled in the art and are described in more detail in WO 2005/056782, pages 12, 13 and pages to page 52, which is incorporated herein by reference. In a specific example, a homologous protein is engineered to produce an enzyme having the desired activity. Several methods are known in the art for producing variants of the enzymes described herein. The method of the t, 4 k γ m, and temple includes, but is not limited to, site-saturation mutagenesis, scan mutation induction, insertion mutation induction, random mutation induction, site-directed mutagenesis and directed evolution. And various other reorganization methods.

The degree of homology between the sequences can be determined using any suitable method known in the art. For example, PILEUp is a program suitable for determining the degree of homology of a sequence. PILEUP uses a progressive pairwise pair to establish a multiple sequence alignment from a set of related sequences.丨 You can also plot a tree that shows the relationship between the clusters used to establish the alignment. Another example of a suitable algorithm is the $blast algorithm. Suitable methods and programs are mentioned on pages 59 and 6 of WO 2005/056782, which is incorporated herein by reference. The terms "substantially similar" and "substantially identical" as used in the context of a polynucleotide or polypeptide sequence as compared to a reference (ie, wild type) sequence and a method for determining sequence identity are described in more detail in the text. 2, 5/〇 56782, pages 61 and 62, the disclosure of which is incorporated herein by reference. "Surfactant" means a substance that lowers the surface tension of a liquid. Emulsifier refers to a substance that promotes the suspension of one liquid in another liquid. A chelating agent means a substance capable of reacting with a metal ion to form a water-soluble complex in which the metal remains in a non-ionizable form. The term "aggregate" refers to a compound used in the textile industry to improve the weaving efficiency by increasing the abrasion resistance and strength of the yarn. The dip is usually made of, for example, a starch or a powdered compound. As used herein, the term "de-slurry" refers to the procedure for eliminating pulp (--beat starch) 13 201035407, typically prior to application of a particular conditioner, dye or bleach.

If not, T Chuanxiong; 哔|Sexually remove difficult enzymes. Exemplary enzymes are used in dinosaur enzymes, cellulases, and nectars. The term "refined" means removing impurities, such as most of the impurities naturally present in fabric materials.

潍贞 (for example, pectin, I, wax, etc.). In some embodiments, in addition to the poor natural impurities, the fine-exchange medium removes the residual material introduced in the manufacturing process, such as a spinning, coning or twisting lubricant. In some specific examples, ... the enzyme used to remove at least a portion of the impurities of the term "bioscouring enzyme" is removed from the fabric. Refers to the ability to remove the term pectinase present in fabric materials" means a pectinase defined according to the art, wherein the pectinase is a group of lysed pectin f (mainly poly((4)1-halolactic acid and its derivatives) The enzyme of (4) bond (see Sakai et al. Advances in Applied Micr〇bi〇1〇gy 39:213 294). Preferably, the pectinase suitable for use herein is catalyzed by trans-elimination. A randomly cleaved pectinase of K4·(tetra) bond in pectic acid (also known as polygalactose (IV)), such as acid to cats, SSst enzyme type polygalacturonate dissociation enzyme (Ec 4.2.2.2) (PGL) Also known as ♦ (MaD-galacturonic acid) dissociation enzyme, also known as pectate dissociation enzyme. The term "pectin" means pectin which can be self-contained to a higher or lower degree. Acidate, polygalacturonic acid and pectin. As used herein, the term "cutinase" refers to an enzyme derived from a plant 'bacteria or fungus used in fabric treatment. The chitinase is capable of hydrolyzing the keratin Jiexie Enzyme. Cutinase can decompose fatty acid esters and is processed in fabrics 14 201035407 :: scouring) needs to be removed in the presence of the other will be L = enzyme activity of the solution. In particular, cutinase is enzymatic. Appropriate - the keratin of the bio-polyacetate polymer on the sputum has hydrolysis activity. The horn A enzyme can be divided into many different plant, fungal and bacterial sources. The XMH term "powder enzyme" refers to the cleavage of the straight chain, r yoshikawa-4) (four) bond to form maltose molecular fermentation Ο 淀粉 amylase for the presence in saliva The double enzyme). Temple powder enzymes combine long-chain carbohydrates with m-forms and are also produced by many plants. ##=赢粉) is broken down into smaller units. "Oxidation stability" (4) Powder enzymes are non-oxidative stability and are derived from non-oxidative stability enzymes: enzymes, which are resistant to degradation caused by oxidation. Exhaustion of "protease" means a protein derived from a microorganism (for example, or a polypeptide derived from a plant or an animal and having a catalytic protein, and a plurality of polypeptides of the hydrazine δ main chain in each position of the genus :: Proteins that are capable of cleavage of peptide bonds or as used herein - 'Catalase # is an enzyme of water and oxygen (ie, more catalytically active: "decomposition procedure" or "decomposition process" or " "Batch-by-batch procedures" or "process batches of fabrics, in which each batch is entirely used throughout the entire process", and a part of the designation. Program or program "dye-exhaustion procedure" means pre-treatment of chemically treated components and dyes simultaneously or Add the enzyme pre-dispensing procedure in sequence. The "liquid ratio" in the fabric treatment bath refers to the ratio of the weight of the fabric in the J-Star and the Meridian 15 201035407. Clearly stipulates, otherwise, "a number of indicators. The enzyme fabric bleaching _ whitening side / M discontinuous procedure (one_bath two_steps dye exhaustion method) described in this article can also be immersed. Or a semi-continuous procedure of pressure-crushing, but the bleaching composition used in the enzyme-based fabric bleaching-whitening method according to the present invention contains a perhydrate (tetra) enzyme; the perhydrolase enzyme is suitable for Hydrogen peroxide source and / or hydrogen peroxide in the presence of:: per acid to produce a peracid after the catalytic reaction; surfactant and chemicals; peroxide stabilizer; chelating agent; and maintained in the fabric bleaching process A buffer having a pH of from about 6 to about 8. The enzymatic bleaching composition may further comprise a bioscouring agent or a bio-refining leave-degrading enzyme, as appropriate. (IV) Prime and/or depolymerizing agents or the application of the method according to the invention is described in more detail below. The components, as well as: information on the amount of such components, unless otherwise stated, in parts by weight. Perhydrolase enzymes may use - or a plurality of perhydrolase enzymes for bleaching according to an enzyme fabric as described herein - In the composition of the whitening method. In some specific examples, the perhydrolase enzyme is naturally occurring (also the P cell genome encoded perhydrolase enzyme). In some specific examples I The enzymatic enzyme comprises at least about 80%, 85%, 90%, 95%, 97%, 98%, 99% or 16 201035407 99.5% of the amino acid sequence of the naturally occurring perhydrolase material. , consisting of, or consisting essentially of, the amino acid sequence. In some embodiments, the perhydrolase enzyme is a naturally occurring M. smegmatis perhydrolase enzyme. In some embodiments, The perhydrolase enzyme comprises the amino acid sequence of SEQ ID NO: 1 or a variant or homolog thereof, consisting of, or consisting essentially of, the amino acid sequence or a variant or homolog thereof a variant or homologue thereof. In some embodiments, the perhydrolase enzyme comprises at least about 80%, 85%, 90%, 95% of the amino acid sequence shown in SEQ ID NO: 1 97% '98%, 99% or 99.5% identical amino acid sequence consisting of, or consisting essentially of, the amino acid sequence. The amino acid sequence of Mycobacterium smegmatis perhydrolase is as follows: MAKRILCFGDSLTWGWVPVEDGAPTERFAPDVRWTG VLAQQLGADFEVIEEGLSARTTNIDDPTDPRLNGASYLPSC LATHLPLDLVIIMLGTNDTKAYFRRTPLDIALGMSVLVTQV LTSAGGVGTTYPAPKVLVVSPPPLAPMPHPWFQLIFEGGEQ ❹ KTTELARVYSALASFMKVPFFDAGSVISTDGVDGIHFTEAN NRDLGVALAEQVRSLL (SEQ ID ΝΟ:1). The corresponding polynucleotide sequence encoding M. smegmatis perhydrolase is:

5,-ATGGCCAAGCGAATTCTGTGTTTCGGTGATTCCCT

GACCTGGGGCTGGGTCCCCGTCGAAGACGGGGCACGCAC

CGAGCGGTTCGCCCCCGACGTGCGCTGGACCGGTGTGCT

GGCCCAGCAGCTCGGAGCGGACTTCGAGGTGATCGAGGA

GGGACTGAGCGCGCGCACCACCAACATCGACGACCCCAC

CGATCCGCGGCTCAACGGCGCGAGCTACCTGCCGTCGTG 17 201035407

CCTCGCGACGCACCTGCCGCTCGACCTGGTGATCATCAT

GCTGGGCACCAACGACACCAAGGCCTACTTCCGGCGCAC

CCCGCTCGACATCGCGCTGGGCATGTCGGTGCTCGTCAC

GCAGGTGCTCACCAGCGCGGGCGGCGTCGGCACCACGTA

CCCGGCACCCAAGGTGCTGGTGGTCTCGCCGCCACCGCT

GGCGCCCATGCCGCACCCCTGGTTCCAGTTGATCTTCGA

GGGCGGCGAGCAGAAGACCACTGAGCTCGCCCGCGTGTA

CAGCGCGCTCGCGTCGTTCATGAAGGTGCCGTTCTTCGA

CGCGGGTTCGGTGATCAGCACCGACGGCGTCGACGGAAT

CCACTTCACCGAGGCCAACAATCGCGATCTCGGGGTGGC

CCTCGCGGAACAGGTGCGGAGCCTGCTGTAA-3' (SEQ ID NO: 2). In some embodiments, the perhydrolase enzyme comprises one or more amino acid positions at positions corresponding to the M. smegmatis perhydrolase amino acid sequence set forth in SEQ ID NO: 1. Replaced. In some embodiments, the perhydrolase enzyme comprises any one or any combination of amino acid substitutions selected from the group consisting of: M1, K3, R4, 15, L6, C7, DIO, SI 1, L12, T13, W14, W16, G15, V17, P18, V19, D21, G22, A23, P24, T25, E26, R27, F28, A29, P30, D31, V32, R33, W34, T35, G36, L38, Q40, Q41, D45, L42, G43, A44, F46, E47, V48, 149, E50, E51, G52, L53, S54, A55, R56, T57, T58, N59, 160, D61, D62, P63, T64, D65, P66, R67, L68 ' N69, G70, A71, S72, Y73, S76, C77, L78, A79, T80, L82, P83, L84, D85, L86, V87, N94, D95, T96, K97, Y99F100, R101, R102, P104, L105, 18 201035407 D106, 1107, A108, L109, G110, Mill, S112, V113, L114, V115, T116, Q117, V118, L119, T120, S121, A122, G124, V125, G126, T127, T128, Y129, P146, P148, W149, F150, 1153, F154, 1194, and F196 In some specific examples, the 'perhydrolase enzyme' is equivalent to one or more of SEQ ID NO: 1 The position of the amino acid in the position of the M. smegmatis perhydrolase amino acid sequence comprises one or more of the following substitutions: L12c, q or G; T25S, G or P; L53H, Q, G or S S54V, LA, P, Kenting or Ruler; Eight 550 or 1'; Ruler 671', (), >^〇, ugly, 1^ or? ;1<:9711; V125S, G, R, A or P; F154Y; F196G. In some embodiments, the perhydrolase enzyme is the S54V variant of SEq id NO: 1.

In some embodiments, the perhydrolase enzyme comprises an amino acid at an amino acid position corresponding to the amino acid position in the M. smegmatis perhydrolase amino acid sequence represented by SEQ Ιβ NO··1 Substitution combinations: U2I S54v; L12M S54T; L12T S54V; L12Q T25S S54V; L53H S54V; S54P V125R; S54V V125G; S54V F196G; S54V K97R V125G; or A55G R67T K97R V125G. In some specific shots, the perhydrolase enzyme contains at least a hydrazine: hydrolysis ratio. In some specific examples, the perhydrolase enzyme comprises greater than one hydrolysis: hydrolysis ratio. In some embodiments, the fabric bleaching-whitening method according to the present invention provides a concentration of the total weight of the 7-component (bath) provided for treating the fabric material in the enzymatic fabric bleaching composition. 5 ah to about P about I·5 ppm to about 2.0 PPm (for example, about 1.7 ppm) over 19 201035407 hydrolase enzyme. Ester Acceptance Enzyme bleaching compositions for use in accordance with the methods described herein include a substrate that acts as a perhydrolase enzyme to produce peracids in the presence of hydrogen peroxide. In some embodiments, the ester is subjected to an ester of an aliphatic and/or aromatic carboxylic acid. In some embodiments, the ester is subjected to one or more esters of the following acids: formic acid, acetic acid, propionic acid, butyric acid, valeric acid, caproic acid, caprylic acid, capric acid, capric acid, eleventh acid, tetradecene. Acid, palmitic acid, stearic acid and oleic acid. In some embodiments, triacetin, tributyrin, and other esters serve as sulfhydryl donors for the formation of peracids. In some embodiments, the ester acceptor is selected from the group consisting of propylene glycol diacetate, ethylene glycol diacetate, triacetin, ethyl acetate, and tributyrin. In some embodiments, the ester is subjected to propylene glycol monoacetic acid from hydrazine, ethylene glycol diacetate or ethyl acetate. In one embodiment, the ester is propylene glycol diacetate. In some embodiments, the concentration is from about 2 〇〇〇 ppm to about 4 〇〇〇 ppm, from about 2500 pm to about 35 (8) ppm '% 2 of the total weight of the aqueous composition (bath) used to treat the textile material. Phenol to about 5% or about 3000 Ppm of ester acceptor, such as propylene glycol diacetate. Difficult milk 1G source The enzyme bleaching composition used in accordance with the methods described herein comprises a hydrogen peroxide source. The peroxides can be added directly in batches or continuously on the spot by chemical electrochemistry and/or enzymes. In some embodiments, the source of hydrogen peroxide is hydrogen peroxide. In a 20 201035407 carcass only t 'hydrogen peroxide source is a solid servant machine that spontaneously produces hydrogen peroxide after being added to water. The 4 compounds include cerium peroxide and an organic compound or an organic compound, an adduct of '^'''', which is the most widely used sodium chlorate, also known as sodium percarbonate. The counter inorganic perhydrate salt is a specific example of a hydrogen peroxide source. Examples of the perhydrogen peroxide salt include a chlorinated acid salt, a percarbonate phosphate, a persulfate salt, and a metal salt. ““Over-emulsified weathering salt is usually Ο Ο

...the: Hydrogen peroxide adducts suitable for use in the compositions used in accordance with the methods described herein. % includes an adduct of peroxo-reading zeolite, or urea may comprise a hydrogen peroxide complex in the form of a crystalline and ' or substantially pure solid without additional protection. "It is preferred to ride certain peroxygenate salts and the composition of the composition to be coated with a substance in the form of a coating which provides better stability of the perhydrate. Suitable for: 1: Inorganic salts, such as metal oxides, carbonates or stalks 5, sessile compounds or organic substances such as waxes, oils or fat soaps. In some specific examples, The source of hydrogen peroxide is an enzyme-producing chlorine peroxide production Ί * In the specific example, the 'enzymatic peroxidation gas production system contains emulsified s# and its substrate. The appropriate person's sputum is given, so the rolling enzyme includes (but not Limited to: Glucosamine, Sorbitol Oxidase, Hexose Oxidase, Biliary Oxidase, Alcohol, Enzyme, Oil Oxidase, Cholesterol Oxidase, Asthma Oxidase, Aminoguanidase, Glycine Oxidase, pyruvate oxidation:, face acid oxidase, creatinine oxidase, lysine oxidation oxidase, glycolate oxidase, galactose oxidase, 21 201035407 urinary chymase oxalate oxidase and yellow嗓吟 oxidase. The following system provides a coupling system for the production of hydrogen peroxide by enzymes. An example of glucose + h2o glucose oxidase - > gluconic acid + H2 〇 2 H2O2 + S is a perhydrolase alcohol + peracid. It is not intended that the invention is limited to any particular enzyme, and any suitable receptor produces H2. The enzyme of 〇2 can be used in the present invention. For example, a lactate oxidase of Lactobacillus speeies which is known to form H202 from lactic acid and oxygen can be used. The enzyme produces acid (for example, the above example) The advantage of (4) sugar acid) is that the pH of the test solution is lowered to the pH range in which the peracid is most effective for bleaching (ie, equal to or low; pKa), which can produce hydrogen peroxide (eg Alcohol oxidase, ethylene glycol oxidase, glycerol oxidase, amino acid oxidase, etc.) may also be used together with the vinegar substrate and the perhydrolase enzyme of the present invention to produce a peracid. In some specific examples, The peroxidase-producing oxidase is a carbohydrate oxidase, for example, a fuel cell that can be electrochemically produced and fed with hydrogen gas, which is used to treat textile materials from 1000 ppm to about 3200 ppm to about 2 2 〇〇 ppm In some embodiments, the hydrogen peroxide source is about PPm, from about 1500 ppm to about 2800 ppm, about 2 〇〇〇 or about 2 1 总, based on the total weight of the aqueous composition (bath). Argon peroxide provided at a concentration of ppm. 22 201035407 Surfactant and Emulsifier Ο 酵 The enzyme fabric bleaching composition used in accordance with the method of the present invention contains one or more (i.e., at least one) surfactant and/or at least one emulsification Surfactants suitable for use in the present invention include, but are not limited to, nonionic surfactants (see, for example, U.S. Patent No. 4,565,647, incorporated herein by reference); Cationic surfactants; and zwitterionic surfactants (see, for example, U.S. Patent No. 3,929,678, the disclosure of which is incorporated herein by reference in its entirety in its entirety herein in Alkene sulfonate, alkyl sulfate (fatty alcohol sulphate), alcohol ethoxysulfate, alcohol-based salt, acid-based fat Methyl vinegar, succinic acid or dilute succinic acid and soap. Nonionic surfactants include, but are not limited to, oligosaccharide ethoxylates, isotridecyl alcohol ethoxylates, nonylphenol ethoxylates, alkyl polyglycosides, alkyl dimethylamines Oxide, ethoxylated fatty acid monoethanol decylamine, fatty acid monoethanol decylamine, polyalkyl amide fatty acid guanamine ' and glucosamine Ν 醯 ν ν _ _ _ _ _ ). In some embodiments, the surfactant and/or emulsifier comprises a non-ionic surfactant. In a specific example, the nonionic surfactant is a fatty alcohol ethoxylate. In a specific example towel, the nonionic interfacial surfactant is an isotridecyl alcohol ethoxylate. In a specific embodiment, the nonionic surfactant is a fatty alcohol ethoxylate and an isotridecyl alcohol ethoxylate. Soil In a specific example, the composition package 23 201035407 used in accordance with the method of the present invention contains a surfactant and an emulsifier. The active agent can be used to treat the aqueous composition of the fabric material (bath) in an amount of from about 300 ppm to about 4800 ppm, from about 600 ppm to about 36 Å! ^ or about 3 〇〇 1) 1) 111 It is present at a concentration of about 12〇〇卯111. In two specific examples, the 'enzymatic bleaching composition contains from about 300 ppm to about 3600 ppm, from about 6 Torr to about 3 Å, based on the total weight of the aqueous composition (bath) used to treat the woven material. Melon or a tridecyl alcohol ethoxylate of from about 9 ppm to about 2400 ppm. Peroxide Stabilizer The enzyme bleaching compositions used in the methods described herein contain a peroxide stabilizing agent. Examples of peroxide stabilizers include, but are not limited to, carbaryl, acrylic polymers, magnesium salts, and phosphonic acids. In one embodiment, the peroxide stabilizer is a phosphonic acid. The stabilizer may be present in the enzyme fabric at a concentration of from about 6 〇 Ppm to about 600 ppm, from about 60 ppm to about 120 〇 ppm, or from about 12 Qppm to about (d), based on the total weight of the aqueous composition (bath) used to treat the textile material. In the bleaching composition." Chelating agent The enzyme bleaching composition used in accordance with the methods described herein includes an agent. Examples of the chelating agent include, but are not limited to, an amine-based buffer acid, an amine earthworm _ left-night g An aromatic chelating agent, a polyhydroxy-carboxylic acid, an amine polycarboxylic acid, a polyphosphonate, and a polyacrylic acid, and a mixture thereof, which are suitable for use as a chelating agent, including ethylenediaminetetraacetate. 24 201035407 Hydroxyethylethylenediaminetetraacetate, nitrogen triacetate, ethylenediamine tetrapropionate and diethylidenetetraamine hexaacetate. The aromatic chelating agent obtained by multi-S energy base is also suitable. Compositions herein: (see U.S. Patent No. 3,044). Preferred compounds of this type are: bis-dibasic benzene (such as di-diyl-di-di-di-phenyl-phenyldiethyl-amine pentaacetate) and ethanol diglycolic acid, alkali Metals, ammonium and substituted ammonium salts thereof, and mixtures thereof. Ο 胺 Aminophosphonates are also suitable as chelating agents in the compositions of the invention, although at least low total phosphorus levels are permitted. The degradable sounding agent is ethyienediaminedisuceinate ("EDDs"), especially the [s,s] isomer as described in U.S. Patent No. 4,7G4,233. The chelating agent is polyacrylic acid. The chelating agent can be used to treat the total weight of the aqueous composition (bath) of the textile material from about 60 ppm to about 50,000 ppm, from about ppm to about ppm, or from about 18 pp to about Λ. ΡΡ, 1200 ppm concentration is present in the enzyme fabric bleaching composition. Bleaching agent, < I field also, and σ product form using at least one surfactant and / or ritual agent, at least one peroxidation a stabilizer and at least one chelating agent, the combined product containing - by species surfactant and / or emulsifier, at least one peroxide stabilizer, and at least - for each of the chelating agent in a combination product based bleaching agent and referred ^ Shi Yan

Commercially available, such as CLARITE® LTC (product of Huntsman). 25 201035407 The surfactant may be present at a concentration of from about 5% to about 40%, from about 20% to about 30% or from about 5% to about 10%, based on the total weight of the bleaching treatment. The peroxide stabilizer may be present in the bleaching treatment at a concentration of from about 1% to about 5%, from about 1% to about 10%, or from about 2% to about 8%, based on the total weight of the bleaching treatment. The chelating agent may be present in the bleaching treatment at a concentration of from about 1% to about 5% 〇 〇, from about 5% to about 1%, or from about 3% to about 10%, based on the total weight of the bleaching treatment. In some embodiments, the 'bleaching agent contains from about 5% to about 30%, from about 10% to about 25%, or from about 15% to about 20%, by weight of the total weight of the bleaching agent, of isotridecyl alcohol. Oxylate. The bleaching treatment agent is suitably provided in the form of an aqueous composition comprising the components indicated above. Buffer The enzymatic bleaching composition contains a buffer which is capable of maintaining the composition at a pH of from about 6 to about 8. In one embodiment, the buffer is a carbonate buffer (pH 8). Fluorescent Brighteners Fluorescent whiteners suitable for use in accordance with the methods described herein are, for example, those described in U.S. Patent No. 3,984,399, U.S. Patent No. 5,969, the entire disclosure of U.S. Pat. Vinyl biphenyl derivatives, which are incorporated herein by reference. In a specific example, the distyrylbiphenyl derivative shown corresponds to 26 201035407 in the compound of the formula Ο

Wherein (1) hydrazine is hydrogen, lithium, sodium, potassium, ammonium or alkyl or C2-C6 hydroxyalkyl monosubstituted i ° which is heterogeneous ammonium, or a mixture thereof, and -substituted or tetrasubstituted Ri and R2 is independently of each other hydrogen, c. cvc, halogenate•c6 alkoxy or in another embodiment, formula (1), corresponding to formula (la)

(la) where is defined as specified above. Other suitable glory for white ginseng, G. Panyu, '", for example, U.S. Patent No. 3,485,831, U.S. Patent No. 3,453,268, and U.S. Patent No. 3,994,834, the disclosure of which is incorporated herein by reference. In the eight-body example, the triazolyl indenyl acid derivative shown corresponds to 27 201035407 in the following formula,

Where is defined as specified above. Other fluorescent whitening agents contemplated for use in the practice of the invention are, for example: diamino hydrazine derivatives of the formula:

R4 S03M wherein, as defined above, R3 and R4, independently of one another, are C^-C^alkoxy, alkylthio, substituted or unsubstituted amine or N- which may contain other heteroatoms. a heterocyclic ring; a diphenylpyrazoline derivative of the formula:

FL

I /) - S07 Rr LV 2 ... SO, Μ t Ο 28 201035407 wherein Μ is as defined above, and R5 and R6 are independently of each other hydrogen, Ci-C^alkyl, Ci-Cq alkoxy or halogen The diphenyl σ ratio of the following formula;

Wherein, as defined above, as defined above; a coumarin derivative of the formula:

(6); a benzoxazole derivative of the formula:

R

R8

Wherein B is a group of the formula -CH=CH-, 2,5-thienyl or 1,4-naphthyl, 29 201035407 is independently hydrogen -Ci_c, ~pyrogenic or halogen; Dicyanostyrylbenzene derivatives,

(8). The c-hydroxyalkyl group which may be a heteropolyoxy group which is suitable for the substituent which is monosubstituted, disubstituted, trisubstituted or tetrasubstituted, is typically suitably a formula of the formula: -CH2CH2〇H, even-(3) Outline coffee,

-(CH2)2-0-(CH2)2-0H'-(CH2)2-〇-CH PR υ CH2-ch2-〇h or _(Ch2)2-0- ch2-ch(ch3)-〇h The group. Ci_Cd groups which are suitable for substituents in the meaning of mono-, di-, tri- or tetra-substituted money are propyl, isopropyl, butyl, t-butyl, butyl Or hexyl. R1-A, isobutyl, fluorene, which are defined as Ci-c6 alkyl, are independently of each other, for example, methyl, :yl:propyl, isopropyl, butyl, t-butyl, tert-butyl Isobutene j or hexyl ' and preferably Ci_c4 alkyl, such as ethyl. Ri&& defined as cvcd oxy is independently of each other, for example, methoxy: ethoxy, n-propoxy, isopropoxy, n-butoxy, isobutoxy, or lactyl or hexyloxy Preferably, it is a C1_C4 decyloxy group, such as a methoxy or ethoxylate 30. 201035407 is defined as a halogen of Ri, R2, R5, R6, R7 and r8 independently of each other such as fluorine, gas or bromine, preferably chlorine or Bromine and especially chlorine, these definitions and preferences also apply to the following halogen groups. R3 and R4 which are c丨-C4 alkylthio are independently of each other, for example, methylthio, ethylthio, n-propylthio, isopropylthio or n-butylthio, preferably ethylthio or positive. Propylthio. R3, R4, R5, R6, r7 and r8 of the VC4 alkoxy group are independently of each other, for example, methoxy, ethoxy, n-propoxy, isopropoxy, n-butoxy or iso The butoxy group, preferably a methoxy group or an ethoxy group, is also applicable to the following Ci-CU alkoxy groups. Rs, R7 and R8 of the C!-C4 alkyl group are independently of each other. For example, methyl, ethyl, propyl, isopropyl, butyl, t-butyl, t-butyl or isobutyl, the definitions and preferences also apply to the following Ci_C4 alkyl groups. I and the rule 4 of the substituted amino group are, independently of each other, an unsubstituted amino group, or an amine group substituted on the N atom by, for example, the following group: 〇N-early CVC4 alkylamine group or ν, ν- a Ci_C4 alkylamino group comprising an unsubstituted group (for example an ethylamino group or a diethylamino group) and, for example, an N,N-diCl_C4 alkylamino group, a Ci-C4 group in the alkyl moiety a group substituted with an alkoxy group, a hydroxyl group, a thiol group, a sulfonic acid group or a sulfate group;

a CrC7 cycloalkylamino group comprising an unsubstituted group and a group substituted at the cycloalkyl ring by, for example, a group (especially a methyl group); a phenylamino group or an N-Cl-C4 alkyl group _N a phenylamino group which includes an unsubstituted group and which is, for example, a phenyl ring (which may also be substituted by a phenyl group), a q-C4 alkoxy group, a dentate, an amine mercapto group, and a nitrogen group in the benzene ring. a group substituted with an alkyl group 31 201035407 or a C-C4 hydroxyalkyl group, a monosubstituted or disubstituted amine methyl sulfonyl group, a buffer group, a C1_C4 oxycarbonyl group or a sulfonic acid group; these groups are preferably a benzene ring Unsubstituted or substituted with a sulfonic acid group. In the meaning of the N-heterocyclic ring which may contain other hetero atoms, r3 and independently of each other are, for example, N-morphinyl or β-base-1. The buffer group generally means a group -COOM; a sulfonic acid group - generally means a group -SOM ' wherein hydrazine is hydrogen, lithium, sodium, potassium, ammonium or a Cl_C4 alkyl group or

CrC4 hydroxyalkyl mono-, di-, tri- or tetra-substituted ammonium, or mixtures thereof. In one embodiment, at least one of a stilbene-based stupid derivative and a triazolyl indenyl disulfonic acid derivative is used according to the methods described herein. In another embodiment, at least one of a distyrylbiphenyl derivative of formula (la) and a triazolyl indenyl disulfonic acid derivative of formula (2) is used according to the methods described herein. In some embodiments, a fluorescent whitening agent is provided at a concentration of from about 0.05% to about 0.8%, from about 0.08% to about 5%, from about 1% to about 5% by weight of the textile material. Organic Acids Organic acids are suitably used to adjust the pH to absorb the fluorescent whitening agent. The organic acid is suitably oxalic acid, citric acid and acetic acid. In one embodiment, the organic acid is acetic acid. In some embodiments, the concentration is from about 1 〇〇 ppm to about 4 〇〇〇 ppm, from about 600 叩 111 to about 3000 卯 111, based on the total weight of the aqueous composition (bath) used to treat the textile material. 8〇〇1)1)111 to about 16〇〇卯111 has 32 201035407 organic acid. Suitably, the pH is adjusted to ΡΗ4 to ρΗ5, such as ρΗ45. Enzyme-based fabric bleaching-whitening method is suitable for the 'inventive party', '+_-ti m /, £, + reward is a method of using about 2:1 to about 5::ι, 2〇:1 (for example 20:1 or 1〇) .1 to about too 曰... η liquid ratio. In some specific examples, the Bensing method is dyed in a discontinuous procedure, for example, in a two-step bath. In these specific examples, the enzyme is carried out in the first step! White and in the subsequent second step, the syn-bath is adjusted to ΡΗ4 to ρΗ = as PH 4.5), followed by the eight secret soils 5 ( For example, in a 20-knife clock, about 6 Γ (: to about 95 〇c, a whitening agent is added to the bath, whereby the fluorescing >> 1 is whitened in some specific examples φ, the method is as A semi-continuous procedure for rolling or squeezing the coil. The fabric and the enzyme bleaching composition are at a temperature of from about 55 t to about 6 (TC to about 7 (at a temperature of TC, from about 6 to about 8 C, 、, spoon). From about 20 minutes to about 6 minutes, the white temperature is about 65. (: and the treatment time is about 5 minutes. In some body ~:, the temperature of the enzyme bleaching composition is about 50t from about , example ^

From 20 ° C to about 40 ° C), 田 立 立 八 八 八 initial start 'dish rises about 2 per minute. . Until the treatment temperature for bleaching is reached. In some other specific examples, after the enzyme fabric is bleached, washed, and neutralized, a whitening step (two bath two-step method) is performed in a separate bath. After treating the fabric material with the enzymatic bleaching composition, one or more rinsing steps are performed to remove the bleaching composition. Suitably, the fabric is rinsed with an aqueous composition (water or water composition). In some embodiments, the rinsing temperature is from about two to about, such as about 耽. In some specific real money, water-based rush 33 201035407 The composition contains catalytic peroxygen m. 虱 is a solution of water and oxygen hydrogen peroxide. In a specific example, the fabric was washed twice with an aqueous composition containing 'soil she from a a a a a ' catalase, and the mother rinse lasted for ^ 3 1 〇 minutes. In an in vivo example, residual hydrogen peroxide is removed by rinsing twice with an aqueous composition containing peroxyocta-octaminase at about 5 °C. Suitably, in a two-step bath φ ^ , +., A, after the end of the whitening step, a rinsing step as described above is applied. In some specific examples, the enzyme-based fabric bleaching-whitening method described in the article includes one or more biological refining ^ ^ deep enzymes. The enzymatic fabric bleaching composition may comprise one or more bio-scouring acids, enzymes, or fabrics which may be treated with an enzyme-containing fabric bleaching composition and treated with a bio-scouring enzyme in a subsequent processing step. y, pectinase, hemicellulase, cellulase, hydrolyzed polyglycolic enzymes> (eg, cutinase or lipase) and other biologically scouring enzymes (eg, proteases) are contemplated for use in practicing the invention. Refine the enzymes. The assay for pectinase, #application, and assay for enzymatic activity is described and referred to in greater detail in the stomach of WO 2007/136469, pages 19 to 21, the disclosure of which is incorporated herein by reference. ^ Suitable cellulases, their use, and assays for determining enzyme activity are described and referenced in more detail on pages 22 and 23 of WO 2007/136469, which is incorporated herein by reference. °" For example, proteases, protease variants, and lipases can be used as other bioscouring enzymes contemplated for practicing the present invention. Such enzymes, their use 34 201035407, and assays for determining enzyme activity are described and referred to in greater detail in WO 2007/136469, pages 23 to 25, which is incorporated herein by reference. For example, a cutinase or a lipase can be used as an enzyme suitable for the hydrolysis of the vinegar in the present invention. Such enzymes, their use, and assays for determining enzyme activity are described and referenced in greater detail on pages 21 and 22 of WO 2007/136469, which is incorporated herein by reference. In one embodiment, the bioscouring enzyme is a pectinase. 0 Desizing Enzymes In some embodiments, the enzymatic fabric bleaching-whitening methods described herein include - or a plurality of depolymerizing enzymes. The enzymatic fabric bleaching composition may include - or a plurality of deactivating enzymes, or the fabric may be treated as a pre-treatment step material prior to treatment with the enzyme fabric bleaching composition. Any suitable de-zecoenzyme can be used in the present invention. In some specific "columns", the enzyme is a powder-killing enzyme. Mannanase and Portuguese (4) (4) enzymes can also be used. In some specific examples, (4) the enzyme is a continuous powder enzyme or iS-amylase and a combination thereof. The assay for a suitable powder enzyme, its use, and the determination of enzyme activity is described and referred to in greater detail on pages 2007 and 136469, and is incorporated herein by reference. The invention is intended to be illustrative, and not to limit the invention. Unless otherwise stated, 'other temperatures are in degrees Celsius (5) dragons (four) (6)), parts are parts by weight and percentage data is percentage by weight. The relationship between parts by weight and parts by volume is the same as kilograms per liter. 35 201035407 Experimental part The conventional method of reducing bleaching according to the method of the present invention and using sodium dithionite was compared according to the procedure given below by treating the fabric in a dye-exhausting manner using a Mathis ag Lab Vlstaco® device (ZELTEX). Examples 1A, 2, and 3 Enzyme bleaching and whitening were carried out in a one-bath two-step dye exhaustion process: using a liquid ratio of 20:1, containing the amount of bleaching agent given in Table 1 Treated in a bath of soda ash, ester-derived, hydrogen peroxide and perhydrolase enzymes, pre-refined and 175 Τ: τ heat-set nylon 66 woven 2. Allow temperature to be around 2t per minute The temperature was raised to a target temperature of 65. The bath was then held at 6 rc for 3 minutes and then adjusted to pH 4.5 by the addition of acid (80%). An amount of the fluorescent whitening agent was added to the bath and the treatment was continued for another 20 minutes at the temperature of the machine. After draining, the fabric was rinsed twice at 5 (TC) for 1 minute each and then suppressed (four). The secondary rinse included 〇5 g/l of 25% peroxygen: Enzyme T100 solution (available from Genencor) & 36 201035407 Table 1: Examples ΙΑ, 2 and 3-Enzymatic Bleaching - Whitening Example No. 1A 2 3 Bleaching agent υ [gA] 0.9 0.9 0.9 Sodium carbonate buffer [g/1] 2.0 2.0 2.0 Ester substrate 2) [g/l] 3.0 3.0 3.0 35% hydrogen peroxide [mm] 6.0 6.0 6.0 Perhydrolase Enzyme 3) [mg/1] 1.7 1.7 1.7 FWA (la) 4) [%] 0.4 0.36 FWA ( 2 ) 5) [%] 0.26 Toner Dye 6) 6) 1) CLARITE® LTC (Products of Huntsman). 2) C The alcohol diacetate 3) corresponds to 1.0 g / 1 Primagreen® EcoWhite (1X) (Genencor's products) fluorescent whitening 4) of formula (La) of the;. [%] By weight of the fabric weight. 5) Fluorescent whitening agent of formula (2); [%] based on the weight of the fabric. 6) 0.00025°/. 7-Standyl-5,9-bis(phenylamino)-4,10-disulfonic acid-benzophenanthrionium salt (Benzo phenazinium) hydroxide inner salt monosodium salt and 〇.00019% 7_ a mixture of phenyllithophthalic acid-5-[(4. sulfophenyl)amino]-benzophenanthridine salt hydroxide internal salt monosodium salt; [%] by weight of the fabric. Comparative Examples 1 to 3 Conventional reduction bleaching using sodium dithionite: pre-refined at 175 ° C in a bath containing the components of the amounts given in Table 2 using a liquid ratio of 20:1 Under heat-set nylon 66 fabric. Make the temperature 2 per minute. (The rate is raised from the ambient temperature to the target temperature of 95t: then the bath is held at 95 ° C for 30 minutes. After draining, the fabric is rinsed twice at 5 (rc) for 1 〇 min and then Drying at 7 ° C. 37 201035407 Table 2. Comparison of Examples 1 to 3 - Reduction Bleaching with Sodium Dithionite Comparative Example No. 1 2 3 Wetting Agent υ [g/lj 1.0 1. 〇I 1.0 连Sodium Disulfite 2) [g/1] 3.0 3.0 3.0 FWA (la) 3) [%] 0.4 0.36 FWA (2 ) 4) [%] 0.26 Toner Dye 5) [%] 5) 1) INVADINE® DA or ULTRAVON ® EL (a humectant available from Huntsman). 2) Stable. 3) A fluorescent whitening agent of the formula (1a); [%] based on the weight of the fabric. 4) Fluorescent whitening agent of formula (2); [%] by weight of the fabric. 5) 0.00025% 7-phenyl-5,9-bis(phenylamino)_4,1〇-disulfonic acid group benzophenone hydrazine salt internal salt monosodium salt with 0.00019% 7-phenyl a mixture of sulfonic acid groups of 5-(5-[(4-sulfonylphenyl)amino]-benzophenanthracene hydroxide internal salt monosodium salt; [%] by weight of the product. ,

Example 1B Pre-sperm-enzymatic bleaching-whitening was carried out in a two-bath two-step dye exhaustion process (i) using a liquid ratio of 2:1, in a bath containing the following and hot at 175 °c Shaped nylon 66 fabric: 0.9 g/Ι bleaching agent as given in Table 1, 2·0 g/Ι carbonate buffer, 3.0 gM ester substrate (propylene glycol diacetate), 6.0 ml/ 1 35% hydrogen peroxide, and 38 201035407 1.7 mg/I perhydrolase enzyme, which corresponds to [ο g/丨primagreen8 EcoWhite ( lx) (product of Genenc〇r). The temperature was raised from ambient temperature to 65 at a rate of 2 t: per minute.目标 target temperature. The bath is then brought to 65. . Keep it for 5 minutes. After draining, the fabric was rinsed at 50 C for two to two minutes each time and then dried underneath. Each rinse includes a 2S% catalase solution of 〇·5 g/1 (product of Genencor).

(··) using a liquid ratio of 20.1, in the other bath containing 1 · 〇 g / 湿润 as shown in Table 2, the humectant, 0.4% of the fluorescent brightener of formula (la), and enough The bath was adjusted to acetic acid (8% by weight) at pH 4.5, and the dried fabric obtained according to the step (1) was treated. Let the temperature be at: c speed per minute: the temperature rises to 95. . Target temperature. Then let the 乂 V ° minutes. After draining, at 5°. The fabric was rinsed twice under °, the mother was 10 for the clock and then at 70. [Dry dry. Example 4 Enzymatic Bleaching - Whitening is carried out by a one-step, parent-rich beta, white peony 1 one-step smear exhaustion method: using a liquid ratio of 20:1, the heat-resistant shape is contained in the following Knitted fabric: treated with pre-refined and 0.9g/1 bleaching agent 2.0 g/Ι sodium carbonate buffer as given in Table 1, 3. 〇g/Ι ester acceptor (propylene glycol diacetate), 6.0 ml/1 35% hydrogen peroxide, and 1.7 mg/Ι hydrolase enzyme, straight 呷 I, corresponding to 丨〇^rimagreen 39 201035407

EcoWhite ( 1 χ ) (product of Genencor). The temperature was raised from the ambient temperature to a target temperature of 65 at a rate of 2 ° C per minute. The bath was then held at 65 ° C for 30 minutes and then adjusted to pH 4.5 by the addition of acetic acid (80%). Subsequently, 0.4% of the fluorescent brightener of formula (la) was added to the bath and the treatment was continued for another 20 minutes at a temperature of 65 °C. After draining, the fabric was rinsed twice at 50 C for 1 minute each and then dried at 70 °C. Each rinse included 0.5 g/Ι 25% catalase T100 solution (product of Genencor). Comparative Example 4 Conventional reduction bleaching using sodium dithionite: using a liquid ratio of 20:1 is contained in Table 2 for Comparative Examples! Each of the given components was treated in a bath pre-refined and heat-set at 175 °CT. Make the temperature 2 per minute. The rate of enthalpy increases from ambient temperature to a target temperature of 95 °C. The bath was then held at 95 ° C for 3 〇 minutes. After draining, the fabric was rinsed twice at 5 (TC) for 10 minutes and then dried at 70 ° C. Results according to Ganz (journai 0f c〇l〇r an (j Appearance 1_, Issue 5 (1972)) The method described determines the whiteness of the fabric obtained according to the examples and comparative examples. It is apparent that the whiteness difference of more than 5 units of Ganz is apparent. The results are given in Tables 3 to 6. 40 201035407 Table, 3 · Whiteness treatment _ untreated resistance 6.6 Conventional (Comparative Example 1) - - Bath (Example Enzyme / 1 bath (Example 1A, ' " -------- - ~^白度[甘茨] 底白全白 52 s---- 雠58 231 66 248 70 257 Ο Enzymatic bleaching under hunger will obviously improve the bottom of the 66 fiber, the bleaching effect is better than the use of The effect achieved by the reduction of bleaching is compared with the conventional bleaching-whitening and virginity, and when the whitening-whitening method is used to treat the woven fabric according to the yeast, the whiteness is 40%. Effect (with fire first). A cold two-step bleaching-whitening allows for the highest whitening effect. Table 4: Whiteness-^. ----- λττ έί - Whitening treatment -------- -- Conventional (Comparative Example 2) ------- -----/L Ear-Under J Enzyme/1 bath (Example 2) —-?60 —~-__288 — When the whitening method is used to treat the fabric, the all-white effect is achieved. Sexual whitening is compared with the weaving according to the conventional method. Compared with σ, according to Table 5: Whiteness bleaching-whitening treatment (comparison Example 3) Enzyme/1 bath (Example 3)

201035407 An excellent all-white effect is achieved when the fabric is treated according to the enzyme bleaching-whitening method as compared to the fabric treated according to the conventional method. Table 6: Whiteness Bleaching - Whitening Treatment Whiteness [Gantz] Conventional (Comparative Example 4) 226 Enzyme/1 bath (Example 4) 258 Compared with the fabric treated according to the conventional method, The enzyme bleaching-whitening method achieves an excellent all-white effect when the fabric is treated. [Simple diagram description] No [Main component symbol description] None 42 201035407 Preface 歹 U table < 110〉 Hangsman Advanced Materials Company <12〇> Enzymatic fabric bleaching-whitening method <130> 925016 <;150> EP09154519 <151> 2009-03-06 <160> 2 <170> Patentln version 3.5

<210> 1 <211> 216 <212> PRT <213> Mycobacterium smegmatis perhydrolase <400>

Met Ala Lys Arg lie Leu Cys Phe Gly Asp Ser Leu Thr Trp Gly Trp 1 5 10 15

Val Pro Val Glu Asp Gly Ala Pro Thr Glu Arg Phe Ala Pro Asp Val 20 25 30

Arg Trp Thr Gly Val Leu Ala Gin Gin Leu Gly Ala Asp Phe Glu Val 35 40 45 lie Glu Glu Gly Leu Ser Ala Arg Thr Thr Asn lie Asp Asp Pro Thr 50 55 60

Asp Pro Arg Leu Asn Gly Ala Ser Tyr Leu Pro Ser Cys Leu Ala Thr 65 70 75 80

His Leu Pro Leu Asp Leu Val lie lie Met Leu Gly Thr Asn Asp Thr 85 90 95

Lys Ala Tyr Phe Arg Arg Thr Pro Leu Asp lie Ala Leu Gly Met Ser 100 105 110

Val Leu Val Thr Gin Val Leu Thr Ser Ala Gly Gly Val Gly Thr Thr 115 120 125

Tyr Pro Ala Pro Lys Val Leu Val Val Ser Pro Pro Pro Leu Ala Pro 130 135 140

Met Pro His Pro Trp Phe Gin Leu lie Phe Glu Gly Gly Glu Gin Lys 145 150 155 160

Thr Thr Glu Leu Ala Arg Val Tyr Ser Ala Leu Ala Ser Phe Met Lys 165 170 175 1 201035407

Val Pro Phe Phe Asp Ala Gly Ser Val lie Ser Thr Asp Gly Val Asp 180 185 190

Gly lie His Phe Thr Glu Ala Asn Asn Arg Asp Leu Gly Val Ala Leu 195 200 205

Ala Glu Gin Val Arg Ser Leu Leu 210 215 <210> 2 <211> 651 <212> DNA <213> M. smegmatis perhydrolase <220><221> CDS <222> (1). (648) <400> 2 atg gcc aag cga att ctg tgt ttc ggt gat tcc ctg acc tgg ggc tgg Met Ala Lys Arg lie Leu Cys Phe Gly Asp Ser Leu Thr Trp Gly Trp 15 10 15 gtc ccc Gtg gaa gac ggg gca ccc acc gag egg ttc gcc ccc gac gtg Val Pro Val Glu Asp Gly Ala Pro Thr Glu Arg Phe Ala Pro Asp Val 20 25 30 ege tgg acc ggt gtg ctg gcc cag cag etc gga geg gac ttc gag gtg Arg Trp Thr Gly Val Leu Ala Gin Gin Leu Gly Ala Asp Phe Glu Val 35 40 45 ate gag gag gga ctg age geg ege acc acc aac ate gac gac ccc acc lie Glu Glu Gly Leu Ser Ala Arg Thr Thr Asn lie Asp Asp Pro Thr 50 55 60 gat ccg egg etc aac ggc geg age tac ctg ccg teg tgc etc geg aeg Asp Pro Arg Leu Asn Gly Ala Ser Tyr Leu Pro Ser Cys Leu Ala Thr 65 70 75 80 cac ctg ccg etc gac ctg gtg ate ate atg ctg Ggc acc aac gac acc His Leu Pro Leu Asp Leu Val lie lie Met Leu Gly Thr As n Asp Thr 85 90 95 aag gcc tac ttc egg ege acc ccg etc gac ate geg ctg ggc atg teg Lys Ala Tyr Phe Arg Arg Thr Pro Leu Asp lie Ala Leu Gly Met Ser 100 105 110 gtg etc gtc aeg cag gtg etc acc age Geg ggc ggc gtc ggc acc aeg Val Leu Val Thr Gin Val Leu Thr Ser Ala Gly Gly Val Gly Thr Thr 115 120 125 tac ccg gca ccc aag gtg ctg gtg gtc teg ccg cca ccg ctg geg ccc Tyr Pro Ala Pro Lys Val Leu Val Val Ser Pro Pro Pro Leu Ala Pro 130 135 140 atg ccg cac ccc tgg ttc cag ttg ate ttc gag ggc ggc gag cag aag Met Pro His Pro Trp Phe Gin Leu lie Phe Glu Gly Glu Gin Lys 145 150 155 160 acc act gag Etc gcc ege gtg tac age geg etc geg teg ttc atg aag 2 48 96 144 192 240 288 336 384 432 480 528 201035407

Thr Thr Glu Leu Ala Arg Val Tyr Ser Ala Leu Ala Ser Phe Met Lys 165 170 175 gtg ccg ttc ttc gac gcg ggt teg gtg ate age acc gac ggc gtc gac 576 Val Pro Phe Phe Asp Ala Gly Ser Val lie Ser Thr Asp Gly Val Asp 180 185 190 gga ate cac ttc acc gag gcc aac aat ege gat etc ggg gtg gcc etc 624 Gly lie His Phe Thr Glu Ala Asn Asn Arg Asp Leu Gly Val Ala Leu 195 200 205 gcg gaa cag gtg egg age ctg ctg taa 651 Ala Glu Gin Val Arg Ser Leu Leu 210 215

Claims (1)

201035407 VII, Shen δ Green patent scope: The fabric:: white into white synthetic fabric material method, which is included in the following _~ section ^ measuring whitening strips, so that the fabric material and the Τ Thereby producing a bleached-whitened fabric material: an enzymatic fabric bleaching composition comprising: (1) a perhydrolase enzyme, () an ester of a hydrolase enzyme, Ο (out) hydrogen peroxide source, [1V) surfactant and / or emulsifier, (v) peroxide stabilizer, (Vi) chelating agent, (V11) maintain a pH of about 1 2 3 4 5 to about 8. And (b) at least one fluorescent whitening agent; and optionally (C) an acid or a shading dye for shaded variation of white. The method of claim 1, wherein the perhydrolase enzyme comprises the amino acid sequence of SEQ ID NO: 1, or a variant or homolog thereof. 2. The method of claim 1 or 2, wherein the perhydrolase enzyme is the S54V variant of SEQ ID NO: 1. 3. The method of claim 1 or 2, wherein the perhydrolase enzyme comprises a ratio of hydrolysis to hydrolysis of greater than 1. 4. The method of claim 1 or 2, wherein the ester acceptor is selected from the group consisting of propylene glycol diacetate, ethylene glycol diacetate, triacetin, ethyl hexanoate, and tributyrin Esters such as propylene glycol diacetate. 5. The method of claim 1 or 2, wherein the source of hydrogen peroxide 201035407 is hydrogen peroxide. 7' The method of claim i or 2, wherein the interfacial activity 4J and/or the emulsifier comprises a nonionic surfactant such as a fatty alcohol ethoxylate or an isotridecyl alcohol ethoxylate. 8. The method of claim 2, wherein the over-halide stabilizer is a phosphonic acid. 9. The method of claim 5, wherein the chelating agent is polyacrylic acid. Wherein the fluorescence is increased. 10. The method according to claim 1 or 2, wherein the white agent is selected from the group consisting of: a distyrylbiphenyl derivative of the formula: Wherein Μ is 虱, 钟, nano, unloaded, recorded, or Ci-C6 alkyl or CVC6 mono-substituted, disubstituted, di- or di-substituted ammonium, which may be doped with a ruthenium atom, or The mixture 'and Ri and R2 are each independently hydrogen, CVC6 alkyl halide; the second formula β β-based diacid derivative 201035407 Wherein, as defined above, is defined; a diamine-based hydrazine derivative of the formula: R4 S03M wherein, as defined above, R3 and R4 are, independently of each other, an alkoxy group, a CpCU alkylthio group, a hydrazine-substituted or unsubstituted amine group or an N-heterocyclic ring which may contain other heteroatoms; a diphenylpyrazoline derivative of the formula Wherein, as defined above, and 3 201035407 R5 and R6 are independently of each other hydrogen, Ci-C^alkyl, Crq alkoxy or halogen; diphenyl 11 of the formula: Wherein, as defined above, the coumarin derivative of the formula: CH, (. 21~15), human ^^〇 human 0 is a benzoxazole derivative of the formula: Wherein Β is a group of the formula -CH=CH-, 2,5-thienylene or 1,4-naphthyl, and R7 and R8 are independently of each other hydrogen, <^-(:4 alkyl, Ci -C^ alkoxy or halogen; and 4 201035407 a dicyanostyrylbenzene derivative of the formula: 11. The method of claim 1 or 2, wherein the fluorescent whitening agent is selected from the group consisting of: a distyrylbiphenyl derivative of the formula: Wherein hydrazine is hydrogen, lithium, sodium, potassium, ammonium or a CrCs alkyl group which may be heteroatomically oxygenated or a C2-C6 monosubstituted, disubstituted, trisubstituted or tetrasubstituted Q ammonium group, or a mixture thereof; And a triazolyl indenyl disulfonic acid derivative of the following formula, Where is defined as specified above. 5 201035407 12. The method of claim 1 or 2, wherein the step of the step comprises: hydrolyzing the hydrogen peroxide with hydrogen peroxide after the bleached fabric is produced. 13. If the scope of patent application is 2:1 or 1〇:1. The method of 1 or 2, wherein the liquid ratio is about H. Please find ^ ^ ^ Μ 石丹甲 The method is carried out by a program selected from the group consisting of a batch process, a dye exhaustion procedure, and a discontinuous procedure. 15. The method of claim i or claim 2 wherein the fabric is bleached with a composition of about 6 Torr. 〇 to about 7 〇, for example, 5 at your white temperature, for about 40 minutes to about 60 minutes, such as 50 minutes of processing time. ]如八,图: Benefit <,,, 6