CN101426972A - One-step treatment of textiles - Google Patents

Abstract

The present invention is directed to novel compositions and methods for enzymatic one-step pretreatment of cellulosic, cellulosic-containing (e.g., cotton and cotton-containing) and non-cellulosic textiles, fibers and fabrics. Pretreatment comprises scouring and bleaching, and optionally, desizing of the textiles.

Description

One step of textiles handles

The cross reference of related application

[01] the application's sequence number of examining at present of requiring to submit on April 14th, 2006 is the priority of 60/792,111 U.S. Provisional Patent Application.The application also is that the sequence number of submitting on May 30th, 2006 of examining at present is 10/581, the part continuation application of 014 U.S. Patent application, this U.S. Patent application requires the priority of PCT/US2004/040438 for 371 times at 35 U.S.C. §, the name of this PCT application is called " Perhydrolase (Perhydrolase) ", submit on December 3rd, 2004, this PCT application 35 U.S.C. § require for 119 times on December 3rd, 2003 sequence number that submit to, that abandon now be the priority of 60/526,764 U.S. Provisional Patent Application.

Technical field

[02] the present invention relates to be used for one of textiles destarch, kiering (scouring) and bleaching and go on foot the method and composition that enzyme is handled.

Technical background

[03] in the weaving of textile fabric, yarn and fabric processing, need preliminary treatment or preparation process to think that further use suitably prepares natural material usually, the dyeing, stamp and/or the arrangement stage that need usually in particular for commercial article.These textile treatment steps remove impurity and chromogen the nature existence or add to fiber and/or fabric by spinning and braiding step.

[04] although textile treatment can comprise many different processing and stage, generally include most: destarch---soak via enzyme, alkali or oxidation and remove sizing agent, as starch; Kiering---under temperature, remove degrease, oil, wax, pectic substance (pectic substance), dirt bits, protein and fat by contacting with sodium hydroxide solution near boiling; And bleaching---generally by using oxidant (as hydrogen peroxide, hypochlorite and chlorine dioxide) or removing chromogen and the chromogen of textiles is bleached from textiles by use reductant (as sulfur dioxide or bisulfites).

[05] owing to exist the condition of wide region to change in each step, commercial enzyme weaving processing needs the separation of these pre-treatment step usually.Yet, owing to use the groove that different pH values, temperature conditions and chemistry add that has of several successive, and between the stage separately essential repeatedly cleaning step, with the high energy that causes owing to the high processing temperature more than 95 ℃, this separation of handling step causes increasing heavy fringe cost to disposed of in its entirety technology.Extra cleaning and/or drying steps have increased huge extra cost and waste material to treatment process.

[06] therefore, in the textiles commercial processes that reduces cost and waste material form, various pretreatment stages are combined into step processing compared with normally used commercial process, will produce significant impact.

[07] yet, though carried out research before, the combination of these three usual steps is not satisfied.At present the bleaching technology that uses comprises and uses alkaline hydrogen peroxide bleaching surpassing under 95 ℃ the temperature.Such high temperature and strong bleach system are incompatible fully with amylase required in the destarch operation.Therefore, surpassing on 95 ℃ the temperature, the combination of destarch and bleaching technology causes the degraded and the not satisfied destarch result of destarch enzyme.Substituting destarch technology such as alkalescence or oxidation are soaked and are comprised that use causes the aggressive chemistry medicine of fiber damage.On the other hand, reducing under the temperature, carrying out a step and handle to allow effective enzyme desizing result, causing unacceptably poor bleaching, whiteness value is lower than commerce can accept limit.And, this low temperature technology that does not have the kiering enzyme, the fabric of generation low moisture adsorbability, it is unacceptable for further dyeing, stamp and finishing technique.

[08] US 2002-0007516 discloses a step process, and it uses hydrophobic bleach or the prefabricated peracid related with hydrogen peroxide.Yet this technology still needs chemical substance, and it must extra process waste water, causes increasing the cost of textile treatment device.Similarly, US2003-041387 discloses the use of such bleach system, and it utilizes the peracid as composition adds rather than original position produces.

[09] do not have a kind of dependence to be used for simultaneously cotton and based on the textiles of cotton and the enzymatic compositions of the destarch of non-cotton cellulosic textiles, kiering and bleaching in these systems, they do not provide eco-friendly enzyme method for a this step process of textiles yet.Though perhaps they be the improvement to conventional method, but still leave too many room for improvement.

[10] therefore, still need effective one step of enzymatic textile processing technology, particularly need the combination of destarch in the textile treatment, kiering and bleaching, with respect to traditional textile bleaching technology, it can provide excellent wettable and whiteness benefit, simultaneously with the cost minimization of environment footprint (environmentalfootprint) and textile mills (textile mill), and the fiber damage that provides the fabric intensity of improvement to keep and reduce.

The invention summary

[11] applicant describes the method and composition of the step enzyme processing that is used for textiles at this paper.An aspect is provided for the method for the enzyme bleaching of textiles.Second aspect provides the method for using a step treatment compositions to handle textiles.The 3rd aspect is provided for the composition that step of destarch, kiering and the bleaching of textiles handles.In one aspect, be provided for the composition of the enzyme bleaching of textiles.In one aspect, the processing of textiles is destarch and/or kiering and/or the bleaching for textiles.Can be cellulose or comprise cellulosic textiles that as cotton and mixed cotton, but this processing is not limited to cellulosics by the textiles of handling at method and composition described herein.

[12] in one embodiment; method comprises the enzyme bleaching to textiles: be fit to allow textiles can survey under the time span and condition of whiteness, the textiles that needs are bleached contacts with the enzyme bleaching composition that comprises ester source, acyltransferase and hydrogen peroxide source.The ester source can be any suitable acetic acid esters.The ester source is present in the bleaching liquid, and concentration is about 100ppm to 10, between the 000ppm, between about 1000ppm to 5000ppm or between about 2000ppm to 4000ppm.

[13] acetic acid esters of Shi Heing is selected from propylene-glycol diacetate, ethylene acetate, glycerol triacetate, ethyl acetate, glycerin tributyrate and its analog.The composition of aforesaid acetic acid esters also is admissible.

[14] acyltransferase can be hydrolysis (perhydrolysis) with hydrolysis than greater than any transferase of 1.The concentration of acyltransferase in bleaching liquid is between about 0.005ppm to 100ppm, between about 0.01ppm to 50ppm, between about 0.05ppm to 10ppm.

[15] hydrogen peroxide can add from external source.Perhaps, hydrogen peroxide can generate oxidizing ferment and suitable substrate enzymatic generation in position by hydrogen peroxide.It can be carbohydrate oxidase that hydrogen peroxide generates oxidizing ferment, as glucose oxidase.The substrate that is fit to can be a glucose.The concentration of hydrogen peroxide in bleaching liquid is between about 100ppm to 5000ppm, between about 500ppm to 4000ppm or between about 1000ppm to 3000ppm.

[16] condition of Shi Heing will depend on the enzyme of use and processing method (for example, continuously, in batches, pad volume heap (pad-batch)), but consider to comprise different temperatures, pH value, process time and conditions of similarity.

[17] the pH condition of Shi Heing comprises between the pH value between about 5 to 11, between pH value between about 6 to 10 and the pH value between about 6 to 8.The enzyme bleaching time condition that textiles is fit to is, under the preferable case, and between about 5 minutes to 24 hours, between about 15 minutes to 12 hours, or between about 30 minutes to 6 hours.

[18] temperature conditions of Shi Heing comprises between about 15 ℃ to 90 ℃, between between about 24 ℃ to 80 ℃ or between about 40 ℃ to 60 ℃.

[19] in one embodiment, the method for using a step treatment compositions to handle textiles comprises: allow under the time span and condition of textiles destarch, kiering and bleaching being enough to, the textiles and of needs processing is gone on foot treatment compositions contact.

[20] under the preferable case, a step treatment compositions comprises: i) one or more biological kiering enzymes (bioscouring enzyme); Ii) one or more destarch enzymes; Iii) one or more enzyme bleach systems.One step treatment compositions can further comprise the auxiliary element that one or more are selected from surfactant, emulsifying agent, chelating agent and/or stabilizing agent.

[21] the enzyme bleach system of present embodiment, suitable condition are described identical with first embodiment with time span.

[22] biological kiering enzyme is a pectase, it includes but not limited to pectate lyase, pectinesterase, polygalacturonase etc., as J.R.Whitaker (Microbial pectolytic enzymes, (1990) W.M.Fogarty and C.T.Kelly (ed.) p.133-176.In, Microbial enzymesand biotechnology.Elsevier Science Publishers, Barking, United Kingdom) described, or the combination of pectase and other enzyme such as at, cellulase, protease, lipase and hemicellulase.In one embodiment, pectase is a pectate lyase.

[23] the destarch enzyme is selected from amylase and mannase.A kind of concrete amylase that is applied as the destarch enzyme is α-Dian Fenmei.

[24] one step treatment compositions can further comprise the auxiliary element that is selected from surfactant, emulsifying agent, chelating agent and/or stabilizing agent.Surfactant can be the combination of nonionic surface active agent or nonionic and anionic surfactant.

[25] the chemical bleaching agent can be united use with a step treatment compositions.The chemical bleaching agent (one or more) that is fit to can be selected from oxidative bleaches, sodium peroxide, sodium perborate, potassium permanganate, clorox, calcium hypochlorite and DCCNa.

[26] in a composition embodiment, a step treatment compositions comprises: i) one or more biological kiering enzymes and ii) enzyme bleach system.In one aspect, composition can comprise one or more destarch enzymes.One step treatment compositions can further comprise the auxiliary element that one or more are selected from surfactant, emulsifying agent, chelating agent and/or stabilizing agent.

[27] by following detailed, other targets of the present invention, feature and advantage will become clear.Yet should be appreciated that, although detailed description and specific embodiment have illustrated preferred implementation of the present invention, but they only provide in illustrational mode, this is because by this detailed description, the variations and modifications of carrying out within the scope of the invention and spirit will be conspicuous for a person skilled in the art.

The accompanying drawing summary

[28] Fig. 1 illustrates the bleaching effect of various processing.Picture is the following processing of sample process: A) buffer B) buffer solution+surfactant+PGDA+H ₂O ₂, C) buffer solution+surfactant+BP 3000L and D) and buffer solution+surfactant+PGDA+H ₂O ₂+ AcT+OxAm+BP3000L+ at.

What [29] Fig. 2 showed is to pad through 12 hours with contrast (top two samples) and contrast+enzyme (two samples in bottom) to roll up the picture of piling the sample of handling.

[30] Fig. 3 shows the samples pictures behind the iodine staining just: A) buffer solution; B) buffer solution+surfactant+PGDA+H ₂O ₂C) buffer solution+surfactant+OxAm; D) buffer solution+surfactant+PGDA+H ₂O ₂+ enzymatic mixture; E) commercial bleaching cotton (positive control); F) buffer solution+surfactant+PGDA+H ₂O ₂(padding the volume heap); G) buffer solution+surfactant+PGDA+H ₂O ₂+ enzymatic mixture (padding the volume heap).

[31] Fig. 4 shows the samples pictures after ammoniated ruthenium oxychloride dyes: A) commercial bleaching cotton (positive control); B) buffer solution; C) buffer solution+surfactant+BP 3000L; D) buffer solution+surfactant+PGDA+H ₂O ₂E) buffer solution+surfactant+PGDA+H ₂O ₂+ enzymatic mixture; F) buffer solution+surfactant+PGDA+H ₂O ₂+ (padding the volume heap); G) buffer solution+surfactant+PGDA+H ₂O ₂+ enzymatic mixture (padding the volume heap).

[32] Fig. 5 provides figure like this, and it is presented at the cotton bleaching power of going up the AcT that detects.

[33] Fig. 6 provides figure like this, and it is presented at the bleaching power of the AcT that detects on the linen.

Detailed Description Of The Invention

[34] present, definition and example below only using, mode as a reference describes the present invention. All patents and the publication of this paper reference are included in disclosed all sequences in these patents and the publication, are incorporated herein by reference clearly.

[35] number range comprises the number that limits this scope.

[36] unless otherwise noted, respectively, nucleic acid with 5 ' from left to right write to 3 ' direction; Amino acid sequence is from left to right write to the direction of c-terminus with aminoterminal.

[37] title that provides of this paper is not the restriction to different aspect of the present invention and embodiment, can understand it by reference specification integral body. Therefore, by reference specification integral body the term that and then below defines is more fully explained.

Definition

[38] unless define in addition herein, all technology used herein and scientific terminology have the implication identical with those skilled in the art's common understanding. For example, Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d Ed., John Wiley and Sons, NY (1994); With Hale and Marham, The HarperCollins Dictionary of Biology, Harper Perennial, NY (1991) provides the normal dictionary of many terms of using among the present invention for those of ordinary skills. Although be applied in practice of the present invention with herein described those methods and materials similar or any method and material of equal value, this paper describes preferred method and material. Therefore, by reference specification integral body the term that and then below defines is described more fully. Equally, use such as this paper, unless clearly indicate in addition in the context, singular references " (a) ", " one (an) " and " being somebody's turn to do (the) " comprise that plural number refers to. Except as otherwise noted, respectively, nucleic acid with 5 ' from left to right write to 3 ' direction; Amino acid sequence is from left to right write to the direction of c-terminus with aminoterminal. Should be appreciated that the invention is not restricted to described concrete method, scheme and reagent, because use their background according to those skilled in the art, they can change.

[39] each the greatest measure limit value intention that provides in whole specification comprises the numerical value limit value that each is less, and it is the same in this article to just look like that this less numerical value limit value is clearly write. In whole the specification, each the minimum value limit value that provides comprises the numerical value limit value that each is larger, just looks like that this larger numerical value limit value is clearly write in this article equally. In whole specification, each digital scope that provides will contain each the narrower digital scope that falls in this wider digital scope, as these narrower digital scopes are write in this article clearly.

[40] as used herein, term " bleaching (bleaching) " refers to, process the technique of textile material, described textile material such as fiber, yarn, fabric, clothes and non-woven fabric are to produce more bright color at described fiber, yarn, fabric, clothes or non-woven fabric. For example, as used herein, bleaching refer to by to the removing that in cellulose or other textile material, causes the compound of color, modify or cover up fabric is bleached. Therefore, " bleaching " refers to, under the pH that is fit to and temperature conditions, processes the sufficiently long time of textile, to realize the blast (namely, bleaching) of textile. The bleaching agent that can use the chemical bleaching agent and/or be produced by enzymatic is bleached. The example of the bleaching agent that for example, is fit to include but not limited to ClO₂、H ₂O ₂, peracid, NO₂Deng. In technique of the present invention, method and composition, H₂O ₂With peracid preferably enzymatic produce.

[41] as used herein, term " bleaching agent " comprises any part of energy white goods.

[42] " chemical bleaching agent (one or more) " is the entity that can bleach textile in the situation that does not have enzyme. They can need the existence of bleach-activating. The example that can be used for the chemical bleaching agent that is fit to of technique described herein, method and composition is sodium peroxide, sodium perborate, potassium permanganate, other peracid. In some respects, work as H₂O ₂Be not by the proenzyme position produce the time, it can be considered to the chemical bleaching agent.

[43] term " a step textile process composition " refers to comprise the preparation of the bleaching agent that at least a biological kiering enzyme and at least a enzymatic produce. In some embodiments, processing compositions also comprises at least a destarch enzyme. The bleaching agent that enzymatic produces is preferably peracid. In one aspect, peracid is by in the presence of hydrogen peroxide, and acyltransferase produces the catalytic action of suitable substrate. One step textile process composition will comprise enough enzymes, with the treat liquid that the is provided at this paper regulation enzyme level in the aqueous medium namely. The enzyme that can be used for this paper be wild-type enzyme with and variant. Preferably, variant is designed to oxidation-stabilized, and is for example, stable in the presence of hydrogen peroxide.

[44] phrase " enzyme bleach system " refers to that the energy enzymatic produces enzyme and the substrate of bleaching agent. The bleach system of enzyme can comprise ester source, acyltransferase (or Perhydrolase) and hydrogen peroxide source.

[45] " ester source " refers to comprise the Perhydrolase substrate of ester bond. Comprise that aliphatic series and/or aromatic carboxylic acid use with Perhydrolase with the ester of alcohol. In a preferred embodiment, the ester source is acetic acid esters. In some preferred embodiments, the ester source is selected from one or more in propylene-glycol diacetate, ethylene acetate, glycerol triacetate, ethyl acetate and the glycerin tributyrate. In some preferred embodiments, the ester source is selected from one or more the ester in the following acid: formic acid, acetic acid, propionic acid, butyric acid, valeric acid, caproic acid, sad, n-nonanoic acid, capric acid, dodecylic acid, tetradecanoic acid, hexadecanoic acid, stearic acid and oleic acid.

[46] term " hydrogen peroxide source " refer to join the textile treatment groove from external source (that is, outside or the outside) or generate oxidizing ferment to the generated in-situ hydrogen peroxide of acting on of its substrate by hydrogen peroxide.

[47] term " hydrogen peroxide generates oxidizing ferment (hydrogen peroxide generating oxidase) " refers to that catalysis comprises the molecular oxygen (O as electron acceptor₂) the enzyme of oxidation/reduction reaction. In these reactions, oxygen is reduced to water (H₂O) or hydrogen peroxide (H₂O ₂). The oxidizing ferment that is suitable for this paper is the oxidizing ferment of its substrate Hydrogen Peroxide (rather than water) of effect. The example that is fit to hydrogen peroxide generation oxidizing ferment used herein and substrate thereof is glucose oxidase and glucose. The enzyme (for example, alcohol oxidase, oxidation of glycol enzyme, glycerol oxidase, amino acid oxidase etc.) of other energy Hydrogen Peroxide also is applied with the combination of ester substrate and Perhydrolase of the present invention, to produce peracid. In some embodiments, hydrogen peroxide generation oxidizing ferment is carbohydrate oxidase.

[48] as used herein, term " Perhydrolase " and " acyltransferase " are used interchangeably, and refer to can catalysis to cause the enzyme of the reaction that the peracid that is suitable for bleaching of enough a large amounts forms. In concrete preferred embodiment, very high the crossing of Perhydrolase generation useful in technique described herein, the method and composition is hydrolyzed and hydrolysis ratio. The hydrolysis that exceeds of the enzyme that these are unique makes these enzymes be fit to be used in technique described herein, the method and composition with hydrolysis ratio. In particularly preferred embodiments, Perhydrolase is the Perhydrolase of describing in WO 05/056782. Yet, be not intended to this technique, method and composition are limited to this specific mycobacterium smegmatis (M.smegmatis) Perhydrolase, the specific variants of this Perhydrolase and the specific homologue of this Perhydrolase.

[49] as used herein, it is under the condition that limits and in the time that limits that phrase " is crossed the ratio (perhydrolysis to hydrolysis ratio) of hydrolysis and hydrolysis ", the amount of the peracid that is produced by the Perhydrolase enzymatic and the ratio of the amount of the acid of enzymatic generation. In some preferred embodiments, the analytic approach that provides in WO 05/056782 is used to determine peracid and the sour amount that this enzyme produces.

[50] as used herein, " textiles (textile) " refers to fiber, yarn, fabric, clothes and non-knitting.This term comprises the textiles of being made by natural, synthetic (for example, artificial) and various natural and synthetic mixture.Therefore, term " textiles (one or more) " refers to not processed and processed fiber, yarn, fabric or knitted fabric, non-knitting and clothes.In this manual, term " textiles (one or more) " " fabric (fabric, one or more) " " clothes (garment, one or more) " will be interchangeable, unless stipulate in addition clearly.Term " textiles (one or more) that needs processing " refers to and need maybe may need the textiles of other processing as biological clear-cut finish (biopolishing) by destarch and/or by kiering and/or bleaching.

[51] term " need bleaching textiles (one or more) (textile (s) in need ofbleaching) " refers to be bleached and does not relate to the textiles of other possible processing.These textiless can or can not carry out other processing.Similarly, these textiless can need or can not need subsequent treatment.

[52] product (for example, clothes and other goods) that as used herein, " textile material (textile materials) " be fiber, yarn intermediate, yarn, fabric, made by fabric and the general name of non-woven thing.

[53] as used herein, term " compatible (compatible) " refers to that the component of a step weaving processing compositions does not make the enzymatic activity of Perhydrolase be reduced to Perhydrolase can not be as required effective degree under normal application conditions.Concrete composition material detailed example hereinafter.

[54] as used herein, " Perhydrolase of effective dose (effective amount ofperhydrolase enzyme) " refers to, reaches the amount of the necessary Perhydrolase of enzymatic activity that needs in technology described herein and the method.This effective dose is determined by those of ordinary skill in the art easily, and it is based on many factors, as the concrete enzyme variants of using, the pH value of application, temperature and the similar factor of using, and result's (for example, level of whiteness) of expectation.

[55] as used herein, " oxidizing chemical (oxidizing chemical) " refers to, has the chemicals of the ability of bleaching textiles.Oxidizing chemical exists with amount, pH and the temperature that is suitable for bleaching.This term includes but not limited to hydrogen peroxide and peracid.

[56] as used herein, " acyl group (acyl) " is common name (for example, chloroacetic chloride, the CH of the organic acid group of the carboxylic acid residues behind the removal-OH group ₃CO-Cl is by acetate CH ₃The acyl chlorides that COO-H forms).The name of each carboxyl groups forms with " base (yl) " alternative this acid " acid (ic) ".

[57] as used herein, term " transferase (transferase) " refers to the enzyme that the catalysis functional compound shifts in the substrate scope.

[58] as used herein, term " Enzymatic transformation (enzymatic conversion) " refers to, contacts with enzyme by making substrate or intermediate product, substrate is modified to intermediate product, or intermediate product is modified to end-product.In some embodiments, contact is by directly substrate or intermediate product being exposed to suitable enzyme realization.Therefore, hydrogen peroxide is because the glucose enzymatic is converted into gluconic acid in the presence of oxygen by producing as glucose oxidase.Similarly, for example, in the presence of hydrogen peroxide, ester can generate peracid by the Enzymatic transformation of acyltransferase.

[59] as used herein, phrase " to proteoclastic stability (stability toproteolysis) " finger protein matter (for example, enzyme) is resisted proteoclastic ability.Be not intended to this term is restricted to, use this stability that some specific proteases is come assess proteins.

[60] as used herein, " oxidation stability (oxidative stability) " is meant the ability that protein works under oxidizing condition.Especially, this term finger protein matter is at various concentration H ₂O ₂And/or there is the ability that works under the situation in peracid.Stability under the various oxidizing conditions can be measured by standard method well known by persons skilled in the art and/or method described herein.The change in fact of oxidation stability increases by the enzymatic activity half-life or reduces at least about 5% or confirm (in most cases, increase is preferred) more, this be with the non-existent situation of oxidized compound under enzymatic activity compare.

[61] ability as used herein, that " pH stability (pH stability) " finger protein matter works under specific pH.In general, most of enzymes have its limited pH scope that works.Outside the enzyme that works at intermediate range pH (that is, about pH7), the enzyme that can under very high or low-down pH, work in addition.Stability at various pH can be measured by standard method well known by persons skilled in the art and/or method described herein.The change in fact of pH stability increases by the enzymatic activity half-life or reduces at least about 5% or confirm (in most cases, increase is preferred) more, and this is and compares in the enzymatic activity of enzyme optimal pH.Yet, be not intended to described herein technology, method and/or composition be restricted to any pH level of stability or pH scope.

[62] ability as used herein, that " heat endurance (thermal stability) " finger protein matter works under specified temp.In general, most of enzymes have its finite temperature scope that works.Outside the enzyme that works in intermediate range temperature (that is, room temperature), the enzyme that can work in very high or low-down temperature in addition.Heat endurance can be measured by known method and/or method described herein.The half-life that changes the catalytic activity by mutant in fact of heat endurance increases or reduces at least about 5% or confirm (in most cases more, increase is preferred), described mutant is exposed under the temperature of the optimum temperature that is different from (that is, being higher or lower than) enzymatic activity.Yet, be not intended to technology described herein, method and/or composition be restricted to any temperature stability level or temperature range

[63] as used herein, term " chemical stability (chemical stability) " finger protein matter (for example enzyme) is to the stability of its active chemicals of adverse effect.In some embodiments, these chemicals include but not limited to hydrogen peroxide, peracid, anion surfactant, cationic surfactant, non-ionic surface active agent, chelating agent etc.Yet, be not intended to technology described herein, method and/or composition be restricted to any specific chemicals level of stability or chemicals stability boundary.

[64] as used herein, term " purifying (purified) " and " separating (isolated) " refer to from sample, remove pollutant.For example, not contaminating protein matter and other compound of Perhydrolase by removing in solution or the prepared product, the purifying Perhydrolase.In some embodiments, the Perhydrolase of reorganization is expressed in bacterium or fungal host cells, comes these reorganization Perhydrolases of purifying by removing other host cell component; The percentage thereby the increase of the reorganization Perhydrolase polypeptide in the sample.

[65] as used herein, " protein (protein) " refers to any component of being made up of amino acid and thought protein by those skilled in the art.Term " protein ", " peptide (peptide) " and " polypeptide (polypeptide) " can exchange use at this paper.Wherein peptide is the part of protein, and those skilled in the art know the application in the text of this term.

[66] as used herein, similar protein is considered to " related protein (related proteins) " on the function and/or on the structure.In some embodiments, these protein sources comprise the difference (for example, bacterioprotein and mycoprotein) between the organism classification in different genus and/or kind.In some embodiments, these protein sources comprise the difference (for example, bacterial enzyme and fungal enzyme) between the organism classification in different genus and/or kind.In other embodiments, related protein is to be provided by identical kind.In fact, be not intended to technology described herein, method and/or composition are restricted to related protein from any particular source (one or more).In addition, term " related protein " comprises tertiary structure homologue and primary sequence homologue.In further embodiment, this term comprise can immunology on the protein of cross reaction.In the most particularly preferred embodiment, the useful relevant Perhydrolase protein of this paper has very high hydrolysis and hydrolysis ratio excessively.

[67] as used herein, term " derivative (derivative) " is meant by the arbitrary one or both ends in C-and N-end and adds one or more amino acid, in amino acid sequence one perhaps many different loci place replace one or more amino acid, and/or appoint one or both ends or lack one or more amino acid in one or more site of amino acid sequence at protein, and/or insert one or more amino acid, and the protein that goes out by protein derived in one or more site of amino acid sequence.The preparation of the protein derivatives preferably dna sequence dna by modifying the coding native protein, the dna sequence dna that this dna sequence dna is transformed into suitable hosts and expresses this modification is finished to form derived protein.

[68] relevant (with deriving) protein comprises " variant proteins (variant proteins) ".In some preferred implementations, variant proteins is different from parental generation protein, as wild-type protein; And variant proteins differs from one another, and difference is the amino acid residue of minority.The number of different aminoacids residue can be one or more, preferably 1,2,3,4,5,10,15,20,30,40,50 or more amino acid residue.Amino acid whose numbers different between the variant are between 1 to 10.In some respects, related protein and specific variant proteins have at least 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 97%, 98% or 99% amino acid sequence identity, in addition, related protein or variant proteins refer to as used herein, are different from the protein of another related protein or parental generation protein on the number of important area (prominent regions).For example, in some embodiments, variant proteins has 1,2,3,4,5 or 10 corresponding important area that is different from parental generation protein.

[69] known in the art several are suitable for producing the method for the variant of enzyme described herein, and these methods include but not limited to site saturation mutagenesis, scanning mutagenesis, insertion mutagenesis, random mutagenesis, direct mutagenesis and orthogenesis and various other recombination method.

[70] in particularly preferred embodiments, homologous protein is carried out engineered, the enzyme that has required activity (one or more) with generation.

[71] as used herein, term " similar sequence (analogous sequence) " refers in protein, and the sequence with similar function, tertiary structure and/or the conserved residues of destination protein matter (that is, normally initial destination protein matter) is provided.For example, in the epitope regions that contains α spiral or β lamellar structure, substituted amino acid is preferably kept identical ad hoc structure in similar sequence.This term also refers to nucleotide sequence and amino acid sequence.In some embodiments, develop similar sequence, like this, substituted amino acid causes demonstrating variant enzyme similar or improved function.In some preferred implementations, the purpose fragment the part or its near, amino acid whose tertiary structure and/or conserved residues in the destination protein matter are positioned.Therefore, contain under the situation of α spiral for example or β lamellar structure in purpose fragment or part, substituted amino acid preferably keeps this ad hoc structure.

[72] as used herein, " homologous protein (homologous protein) " refers to have with the destination protein matter Perhydrolase of another source (for example, from) protein (for example Perhydrolase) of similar action and/or structure.Homology does not mean that one fixes on last being correlated with of evolving.Therefore, intention is that this term comprises the same or analogous enzyme (one or more) (that is, aspect the 26S Proteasome Structure and Function) that obtains from different kinds.In some preferred implementations, need identify the homologue that similar level Four, three grades and/or primary structure are arranged with destination protein matter, because use similar fragment from homologue to replace the destructiveness that fragment in the destination protein matter or part will reduce this variation.In some embodiments, homologous protein has induced the immune response (one or more) similar with destination protein matter.

[73] as used herein, " wild type (wild-type) " and " natural (native) " protein is those protein of natural discovery.Term " wild-type sequence (wild-type sequence) " and " wild type gene (wild-type gene) " can exchange application at this paper, refer to the sequence intrinsic in host cell or the sequence of natural generation.In some embodiments, wild-type sequence is meant aim sequence, and it is the starting point of protein engineering project.The gene of protein of natural generation of encoding can obtain according to conventional method well known by persons skilled in the art.Method generally includes, and the label probe of the sequence in synthetic zone with the coding destination protein matter of inferring is prepared genomic library and by hybridizing the genes of interest that screens in the library with probe from the organism of expressing this protein.Positive hybridization clone is mapped and is checked order then.

[74] can with any appropriate method as known in the art determine between sequence the homology degree (referring to, for example, Smith and Waterman, Adv.Appl.Math., 2:482[1981]; Needleman and Wunsch, J.Mol.Biol., 48:443[1970]; Pearson and Lipman, Proc.Natl.Acad.Sci.USA 85:2444[1988]; GAP, BESTFIT, FASTA and TFASTA among program such as the Wisconsin GeneticsSoftware Package (GeneticsComputer Group, Madison, WI); With Devereux etc., Nucl.Acid Res., 12:387-395[1984]).

[75] for example, PILEUP is a useful program of determining the sequence homology level.PILEUP uses gradual paired comparisons (progressive pairwise alignment) to create out the multisequencing comparison by one group of correlated series.It also can draw tree graph, demonstrates the cluster relation that is used for creating this comparison.The method for simplifying of the progressive comparison method of PILEUP application Feng and Doolittle (Feng andDoolittle, J.Mol.Evol., 35:351-360[1987]).This method and Higgins similar to the method that Sharp describes (Higgins and Sharp, CABIOS 5:151-153[1989]).Useful PILEUP parameter comprises room weight (gap weight) value 3.00 of acquiescence, room length weight (the gap length weight) value 0.10 and the terminal room (weighted end gaps) of weighting of acquiescence.Another example of appropriate algorithm is the BLAST algorithm, by description (Altschul et al., J.Mol.Biol., 215:403-410, [1990] such as Altschul; With Karlin et al., Proc.Natl.Acad.Sci.USA90:5873-5787[1993]).Useful especially blast program be the WU-BLAST-2 program (referring to Altschul et al., Meth.Enzymol.,, 266:460-480[1996]).Parameter " W ", " T " and " X " determine the sensitivity and the speed of comparison.The default value that blast program uses is a character length (W) 11, BLOSUM62 matrix (referring to Henikoff and Henikoff, Proc.Natl.Acad.Sci.USA 89:10915[1989]) comparison (B) 50 that keep the score, desired value (E) 10, M ' 5, N '-4 and two chains of comparison.

[76] in the content of relevant at least two nucleic acid or polypeptide, phrase " similar basically (substantially similar) " and " substantially the same (substantially identical) " typically mean, polynucleotides or polypeptide comprise and compare and have at least about 40% homogeneity with reference to (that is wild type) sequence, more preferably at least about 50% homogeneity, even more preferably at least about 60% homogeneity, preferably at least about 75% homogeneity, more preferably at least about 80% homogeneity, even more preferably at least about 90% homogeneity, more preferably about again 95% homogeneity, most preferably about 97% homogeneity, sometimes up to about 98% and the sequence of about 99% sequence homogeneity.Can use known procedure such as BLAST, ALIGN and CLUSTAL, use canonical parameter determine sequence homogeneity (referring to, Altschul for example, et al., J.Mol.Biol.215:403-410[1990]; Henikoff et al., Proc.Natl.Acad.Sci.USA 89:10915[1989]; Karin et al., Proc.Natl.Acad.Sci USA 90:5873[1993]; With Higgins et al., Gene 73:237-244[1988]).The software of implementing the BLAST analysis can openly obtain from National Center forBiotechnology Information.Also can use FASTA search database (Pearson et al., Proc.Natl.Acad.Sci.USA 85:2444-2448[1988]).Two substantially the same indications of polypeptide are that first polypeptide can have the immunology cross reaction with second polypeptide.Typically, difference is that the polypeptide that conservative amino acid replaces has the immunology cross reactivity.Therefore, only on conservative replaces when variant, polypeptide and second polypeptide are substantially the same so at two peptides for example.Two another substantially the same indications of nucleotide sequence are two molecule hybridization (for example, in the paramount stringency scope of moderate) each other under stringent condition.

[77] at least a portion (for example, preferably about 75% or more, more preferably about 90% or more) of term " side by side " or " simultaneously " or " step " intention demonstration destarch, kiering and bleaching is carried out in single operation.This term be not intended to refer to the textiles handled with this method and composition can not be processed more than once.But this term refers to for each cycle of treatment, as in other local various ingredients of describing in detail of the application, is used to machining textile at one time.Similarly, the component of processing can once add one, adds all simultaneously or with the group adding, need only at least a portion that all components is present in cycle of treatment.The part of the cycle of treatment that all components exists can change according to the total length of cycle of treatment.

[78] also in an operation carry out in some embodiments by biological kiering (bioscouring) of intention expression at least a portion and enzymatic bleach for term " side by side ".This has remarkable advantages: no longer need flushing and other processing of enforcement usually between kiering of carrying out respectively and blanching step.Therefore, for each processing, reduced the demand of water, time and energy in a large number and to the demand of distinct device.And, according to the type for the treatment of processed fabric with the character of the impurity that exists, can obtain the destarch effect man-hour carrying out of the present invention adding thereon.Therefore, in these situations, do not need to carry out other destarch and handle.Although preferably all destarch and blanching step are united implementation, persons of ordinary skill in the art will recognize that the some parts of destarch can separate implementation with blanching step, and do not deviate from spirit of the present invention.

[79] as used herein, " purifying preparation (the purified preparation) " of polypeptide (as enzyme) or " pure substantially preparation (substantially pure preparation) ", be meant with the polypeptide of its abiogenous other protein, lipid and separate nucleic acid.Preferably, also for example antibody or gel-type vehicle (for example polyacrylamide) separate polypeptide with the material that also is used for purified polypeptide.Preferably, at least 10%, 20%, 50%, 70%, 80% or 95% of the dry weight of polypeptide formation purifying preparation.In some embodiments, enzyme can be used as the use of purifying preparation or provides.

[80] term used herein " peptide (peptides) ", " protein (proteins) " and " polypeptide (polypeptides) " can exchange use." enzyme (Enzymes) " is a type of protein, and it can the catalysis biological chemical reaction.In this technology, method and composition, enzyme mainly is the enzyme that can decompose (that is, degraded) various natural materials, and described natural materials for example but be not limited only to protein and sugar.

[81] term " slurries (size) " or " slurries (sizing) " refer to use in industrial textile passes through to increase the wear resistence of yarn and intensity to improve the compound of knitting property.Slurries are made by for example starch or starchy compounds usually.

[82] as used herein, term " destarch (desize) " or " destarch (desizing) " refer to remove slurries from textiles the process of---generally being starch---, and this carried out before using specific arrangement, dyeing or bleaching usually.

[83] as used herein, " destarch enzyme (one or more) " refers to be used for the enzyme that enzymatic is removed slurries.Exemplary enzyme is amylase, cellulase and mannase.

[84] reaction as used herein, that term " is crossed hydrolysis (perhydrolyzation) " or " crossing hydrolysis (perhydrolyzed) " refers to be produced by the ester substrate acetate in the presence of hydrogen peroxide.In a preferred embodiment, cross hydrolysis reaction---acyltransferase---catalysis by enzyme.

[85] as used herein, term " peracetic acid (peracetic acid) " refers to the peracid of deriving from the ester group of donor molecule (donormolecule).Generally speaking, peracid is derived by carboxylic acid ester, and described carboxylic acid ester has formed the acid product excessively of an oxygen atom that can transmit it of high response with hydroperoxidation.The ability of this just transfer oxygen atom plays as bleaching agent peracetic acid.

[86] as used herein, term " kiering (scouring) " refers to remove naturally occurring impurity in cotton yarn or other textiles, for example, and a lot of non-cellulose compounds (for example, pectin, protein, wax and dirt bits etc.).In some embodiments, except natural non-cellulosic impurity, kiering can be removed the retained material of introducing by making, as spinning, winder (coning) or sizing lubricant (slashing lubricant).

Therefore [87] term " biological kiering enzyme (one or more) " is meant the enzyme (one or more) that can remove the impurity that at least a portion finds in cotton yarn or other textiles.

[88] term " dirt bits (motes) " is meant undesired impurity, for example cottonseed fragment, leaf, stem and plant other parts, itself in addition afterwards, adhere to fiber in mechanical ginning processing (mechanical ginningprocess).

[89] as used herein, term " grey cloth (greige (pronunciation gray)) " textiles refers to the textiles that the not any bleaching of process, dyeing or arrangement are handled after production.For example, any woven fabric or knitted fabric that leaves loom and be not organized (destarch, kiering etc.), bleach or dye is called the grey cloth textiles.Hereinafter the textiles that uses in the example is the grey cloth textiles.

[90] as used herein, term " dyeing (dyeing) " refers to, particularly applies color in the coloring solution to textiles for example by being immersed in.

[91] term " non-cotton cellulosic (non-cotton cellulosic) " fiber, yarn or fabric refer to mainly by based on cellulosic composition rather than cotton fiber, yarn or the fabric that constitutes.The example of these compositions comprises linen, ramie, jute, flax, artificial silk, Lyocell fiber, cellulose acetate and other analogous composition from the non-cotton cellulosic goods.

[92] term " protease (protease) " refers to from the microorganism for example protein or the polypeptide structure territory of fungi, protein of bacteria or polypeptide, or from the protein or the polypeptide structure territory of protein or the polypeptide of plant or animal, and it has the ability at one or more diverse location catalyze cleavage peptide bonds of protein sugar skeleton.

[93] as used herein, term " acyltransferase (acyl transferase) " has referred to that fracture ester and other need the enzyme of the function of the oil base component of removing in textiles processing (for example, kiering).In the composition background, acyltransferase refers to that the suitable compound (for example, propylene-glycol diacetate) of catalysis is converted into the enzyme of the various compositions that comprise peracetic acid.

[93] as used herein, term " at (cutinase) " refers to the enzyme of plant, bacterium or the fungal source of use in weaving processing.At is the enzyme of steatolysis, can the hydrolysis substrate cutin.Can rupture fatty acid ester and other of at needs the oil base component of removing in textiles processing (for example, kiering)." at " refers to have the enzyme of significant plant cutin hydrolysing activity.Especially, at has hydrolysing activity to the biological polyester polymers cutin of finding on leaves of plants.The at that is fit to can be separated with bacterial origin from many different plants, fungi.The example of at is provided at: Lipases:Structure, Mechanism and Genetic Engineering, VCH Publishers, edited by Alberghina, Schmid ﹠amp; Verger (1991) pp.71-77; Upases, Elsevier, edited by Borgstrom ﹠amp; Brockman (1984) pp.471-477; With Sebastian et al., J.Bacteriology, vol.169, no.1, pp.131-136 (1987).

[95] as used herein, term " pectate lyase (pectate lyase) " is meant a class pectase.The pectase that " pectase " expression limits according to field like this: pectase is that one group of cutting pectin substance is mainly poly (1 in this field, 4-α-D galacturonide) and the enzyme of the glycosidic bond of its derivative (referring to list of references Sakai et al., Pectin, pectinase andprotopectinase:production, properties and applications, pp 213-294in:Advances in Applied Microbiology vol:39,1993).Preferably, the useful pectase of this paper is the α-1 that cuts pectic acid at random in---being also referred to as polygalacturonase---by trans elimination catalysis, the pectase of 4-glycosidic bond, as polygalacturonase lyases (EC4.2.2.2) (PGL), it is also referred to as poly (1,4-α-D galacturonide) lyase, is also referred to as pectate lyase.

[96] term " pectin (pectin) " expression pectate, polygalacturonase and pectin, it can esterifiedly be higher or lower degree.

[97] as used herein, and term " α-Dian Fenmei (α-amylase) " referring to a kind of enzyme, the α of its cutting amylose-(1-4) glycosidic bond produces maltose molecule (disaccharides of phlorose).Amylase is the digestive ferment of finding in saliva, and it is also produced by various plants.Amylase is decomposed into littler unit with long-chain carbohydrate (as starch).When with the contrast of non-oxide stable alpha-amylase, particularly when with oxidation-stabilized α-Dian Fenmei during from non-oxide stable α-Dian Fenmei contrast that it is derived, the α-Dian Fenmei of " oxidation-stabilized " is the α-Dian Fenmei that the opposing method for oxidation is degraded.

[98] as used herein, " microorganism (microorganism) " refers to bacterium, fungi, virus, protozoan and other microorganism or microcosmic organism.

[99] as used herein, " derivative (derivative) " is meant protein, it derived from protein precursor (for example, native protein), this is by adding one or more amino acid to one or two of C-and/or N-end, replace one or more amino acid of amino acid sequence or the site that some are different, lack one or more amino acid in any one or both ends of protein or in one or more sites of amino acid sequence, or insert one or more amino acid in one or more sites of amino acid sequence and realize.Enzyme can be the derivative of known enzyme, as long as the function of the enzyme that their enforcement conducts are not derived is to useful necessary degree in this technology, method and composition.

[100] as used herein, material (for example, polynucleotide or protein) " derived from (derived from) " microorganism refers to this substance source microorganism since then.

The destarch enzyme

[101] any suitable destarch enzyme can be used for the present invention.Preferably, the destarch enzyme is an amylolytic enzyme.Mannase and glucoamylase also find can be used for this paper.More preferably, the destarch enzyme is α-or the combination of beta amylase and they.

Amylase

[102] be fit to the α of background of the present invention-and beta amylase comprise those bacteriums or fungal source.The mutant of these diastatic chemistry or genetic modification is also included within this category.Preferably α-Dian Fenmei comprises, for example can be from the α-Dian Fenmei of bacillus kind acquisition.Useful amylase includes, but are not limited to: Optisize 40, Optisize 160, Optisize HT 260, OptisizeHT 520, Optisize HT Plus, Optisize FLEX (all from Genencor Int.Inc.), Duramyl ^TM, Termamyl ^TM, Fungamyl ^TMAnd BAN ^TM(all can be from Novozymes A/S, Bagsvaerd, Denmark obtains).Other preferred amylolytic enzyme is a CGTases (cyclodextrin glucanotrasferase enzyme, EC 2.4.1.19), for example those obtain to plant or thermophilic anaerobic rod Pseudomonas (Thermoanaeno-bacterium) from bacillus kind, thermophilic anaerobic bacillus (thermoanaerobactor).

[103] activity of Optisize 40 and Optisize 160 is represented with the product of RAU/g.One RAU is under standard conditions, in one hour 1 gram starch is converted into the amount of the enzyme of soluble sugar.The activity of Optisize HT 260, Optisize HT 520 and Otpsize HT Plus is represented with TTAU/g.One TTAU is under standard conditions, per hour 100mg starch is hydrolyzed to the amount of the required enzyme of soluble sugar.The activity of Optisize FLEX is determined with TSAU/g.One TSAU is under standard conditions, in one minute 1mg starch is converted into the amount of the required enzyme of soluble sugar.

[104] depend on technology type, diastatic consumption difference.The dosage that identical enzyme is littler needs more time than bigger dosage.Yet the diastatic amount of destarch there is not the upper limit, except the regulation of the physical characteristic that may be subjected to solution.Excessive enzyme can not damage fabric; It allows shorter process time.Based on enzyme aforementioned and that use, advise the following minimum dose that is used for destarch:

The amylase product	Minimum dose (every liter of desizing liquid)	Typical scope (every liter of desizing liquid)
			Optisize 40	1,000 RAU	2,000-70,000 RAU
Optisize 160	1,000 RAU	2,000-70,000 RAU
			Optisize HT 260	1,000 TTAU	3,000-100,000 TTAU
Optisize HT 520	1,000 TTAU	3,000-100,000 TTAU
			Optisize HT Plus	1,000 TTAU	3,000-100,000 TTAU
Optisize FLEX	5,000 TSAU	13,000-65,000 TSAU

[105] derive in the enzyme that the destarch enzyme also can preferably be listed from above, wherein add, lack or replace one or more amino acid, comprise hybridization polypeptide (hybrid polypeptide), as long as the polypeptide that obtains is showed the destarch activity.Utilize traditional method of mutagenesis to produce and utilize that for example high pass is crossed triage techniques such as the agar plate screening technique is differentiated these useful variants in the present invention's practice.

[106] the destarch enzyme adds in the aqueous solution (being treatment compositions) so that the textile material destarch is effectively measured.Usually, with the destarch enzyme for example α-Dian Fenmei join in the treatment compositions in following amount: by the zymoprotein of fabric weight from 0.00001% to 2%, preferably, zymoprotein by fabric weight from 0.0001% to 1%, more preferably, by the zymoprotein of fabric weight from 0.001% to 0.5%, even more preferably, by the zymoprotein of fabric weight from 0.01% to about 0.2%.

Biological kiering enzyme

Pectase

[107] any capable degraded for example the pectin degrading enzymatic compositions of the pectin fraction of plant cell wall can be used for carrying out the present invention.The pectase that is fit to comprises those of fungi or bacterial origin ad lib.In the pectase of chemistry or genetic modification is also contained in.Preferably, the pectase that uses among the present invention is that reorganization produces or natural source.They can be the single component enzymes.

[108] pectase can be classified: according to the pectin of their preferred substrate, high methyl-esterification or pectin and polygalacturonase (pectate) and their reaction mechanism, β-elimination or the hydrolysis of low methyl-esterification.Pectase can mainly be inscribe-effect---site at random in chain cuts off polymer, obtains the mixture of oligomer, or they can be circumscribed-effects---attack and produce monomer or dimer from an end of polymer.Several pectinase activities that act on the smooth domain of pectin are included in the enzyme classification that is provided by Enzyme Nomenclature (1992), for example, pectate lyase (EC 4.2.2.2), colloid lyase (EC 4.2.2.10), polygalacturonase (EC 3.2.1.15), circumscribed-polygalacturonase (EC 3.2.1.67), circumscribed-the polygalacturonase lyase (EC 4.2.2.9) and circumscribed-poly-α-galacturonic acid enzyme (EC 3.2.1.82).In a preferred embodiment, method of the present invention is utilized pectate lyase.

[109] enzymatic activity of pectate lyase refers to cut α-1 in the pectic acid (being also referred to as polygalacturonase), 4-glycosidic bond at random by trans elimination catalysis as used herein.Pectate lyase is also referred to as polygalacturonase lyase and poly (1, the 4-D-galacturonic acid) lyase.Be purpose of the present invention, the enzymatic activity of pectate lyase is to be that the increase of the absorbance of polygalacturonase sodium solution under 235nm of the 0.1%w/v in 10 the 0.1M glycine buffer determines that activity (sees by measuring pH value, Collmer et al., 1988, (1988) .Assaymethods for pectic enzymes.Methods Enzymol 161,329-335).Enzymatic activity is typically expressed as x mol/min promptly, the amount of the enzyme that the product of per minute catalysis x mole forms.The another kind of detection measured the increase of viscosity that pH value is the polygalacturonase sodium solution of the 5%w/v in 10 the 0.1M glycine buffer, as (the APSU unit) by the measurement of vibration viscosimetry.Be appreciated that any pectate lyase can be used to put into practice the present invention.

[110] comprise the limiting examples of the pectate lyase of use in the present invention, comprise the pectate lyase that comes as Erwinia (Erwinia), pseudomonas (Pseudomonas), Bacillus (Bacillus), klebsiella (Klebsiella) and Xanthomonas (Xanthomonas) clone from different bacteriums genus.Being fit to pectate lyase used herein is from hay bacillus (Bacillus subtilis) (Nasser, et al. (1993) FEBS Letts.335:319-326) and certain YA-14 of Bacillus (Kim, et al. (1994) Biosci.Biotech.Biochem.58:947-949).Generation is from bacillus pumilis (Dave and Vaughn (1971) J.Bacteriol.108:166-174), bacillus polymyxa (B.polymyxa) (Nagel and Vaughn (1961) Arch.Biochem.Biophys.93:344-352), bacillus stearothermophilus (B.stearothermophilus) (Karbassi and Vaughn (1980) Can.J.Microbiol.26:377-384), other pectate lyase of Bacillus certain (Hasegawa and Nagel (1966) J.Food Sci.31:838-845) and certain RK9 of Bacillus (Kelly and Fogarty (1978) Can.J.Microbiol.24:1164-1172) also is described and considers and uses in this composition and method.Above any one, and do not rely on bivalent cation and/or thermally-stabilised pectate lyase can in the present invention's practice, use.

[111] in a preferred embodiment, pectate lyase comprises, for example, and those disclosed in WO04/090099 (Diversa) and WO 03/095638 (Novo).

[112] according to the inventive method, the effective dose of pectolytic enzyme to be used depends on multiple factor, but according to the present invention, the concentration of pectolytic enzyme in aqueous medium can be by fabric weight from about 0.0001% to about 1% milligram zymoprotein, preferably, by the zymoprotein of fabric weight 0.0005% to 0.2%, more preferably, by the zymoprotein of fabric weight 0.001% to about 0.05%.

At

[113] can use any at of use in the present invention that is fit to, it comprises, for example derived from the at of special humicola lanuginosa (Humicolainsolens) at strain DSM 1800, as at U.S. Patent number 4,810, described in the embodiment 2 of 414 (being incorporated herein by reference), or in a preferred embodiment, at U.S. Patent number 5,512, the microorganism at of describing in 203 from pseudomonas mendocina (Pseudomonas mendocina), their variant and/or equivalent.The variant that is fit to for example is described among the WO 03/76580.

[114] the bacterium at of Shi Heing can derive from pseudomonas (Pseudomonas) or acinetobacter (Acinetobacter), preferably, derive from Pseudomonas stutzeri (P.stutzeri), Pseudomonas alcaligenes (P.alcaligenes), pseudomonas pseudoalcaligenes (P.pseudoalcaligenes), pseudomonas aeruginosa (P.aeruginosa) or Acinetobacter calcoaceticus (A.calcoaceticus), most preferably, derive from pseudomonas stutzeri strain Thai IV17-1 (CBS 461.85), PG-1-3 (CBS 137.89), PG-1-4 (CBS 138.89), PG-II-11.1 (CBS 139.89) or PG-II-11.2 (CBS 140.89), pseudomonas aeruginosa PAO (ATCC 15692), Pseudomonas alcaligenes DSM 50342, pseudomonas pseudoalcaligenes IN II-5 (CBS 468.85), pseudomonas pseudoalcaligenes M-1 (CBS 473.85) or Acinetobacter calcoaceticus GrV-39 (CBS 460.85).Derive from the at of plant for use, known at is present in the pollen of a lot of plants, and these at are useful in this technology, method and composition.At also can derive from fungi, for example, and some kind of colter mould (Absidia); Some kind of Acremonium; Some kind of Agaricus; Anaerobic fungi belongs to (Anaeromyces) some kind; Some kind of aspergillus comprises microorganism Aspergillus aculeatus (A.auculeatus), aspergillus awamori (A.awamori), aspergillus flavus (A.flavus), smelly aspergillus (A.foetidus), A.fumaricus, Aspergillus fumigatus (A.fumigatus), aspergillus nidulans (A.nidulans), aspergillus niger (A.niger), Aspergillus oryzae (A.oryzae), Aspergillus terreus (A.terreus) and aspergillus versicolor (A.versicolor); Some kind of Aureobasidium (Aeurobasidium); Some kind of Cephalosporium (Cephalosporum); Some kind of Chaetomium (Chaetomium); Some kind of Coprinus (Coprinus); Some kind of Dactyllum; Some kind of Fusarium (Fusarium) comprises F.conglomerans, fusarium decemcellulare (F.decemcellulare), fusarium javanicum (F.javanicum), flax wilt(Fusarium lini) sickle-like bacteria (F.lini), Fusarium oxysporum (F.oxysporum) and Fusarium solani (F.solani); Some kind of Gliocladium (Gliocladium); Some kind of detritus Pseudomonas comprises special humicola lanuginosa (H.insolens) and H.lanuginosa; Some kind of Mucor (Mucor); Some kind of Neurospora (Neurospora) comprises Neurospora crassa (N.crassa) and neurospora sitophila (N.sitophila); Some kind of Neocallimastix; Some kind of Orpinomyces; Some kind of Penicillium notatum; Show the flat lead fungi of hair and belong to (Phanerochaete) some kind; Some kind of Phlebia; Some kind of Piromyces; Some kind of pseudomonas; Some kind of the mould Pseudomonas of wine (Rhizopus); Some kind of Schizophyllum (Schizophyllum); Some kind of Trametes (Trametes); Some kind of trichoderma (Trichoderma) comprises trichoderma reesei (T.reesei), trichoderma reesei (long shoot (longibrachiatum)) and Trichoderma viride (T.viride); And some kind of Zygorhynchus (Zygorhynchus).Similarly, can envision at and can be found in the bacterium, as some kind of Bacillus; Some kind of Cellulomonas (Cellulomonas); Some kind of fusobacterium (Clostridium); Some kind of myceliophthora (Myceliophthora); Some kind of pseudomonas comprises pseudomonas mendocina and pseudomonas putida (P.putida); Some kind of hot zygosaccharomyces (Thermomonospora); Thermophilic fungal belongs to (Thermomyces) some kind, comprises T.lanuginose; Some kind of streptomyces (Streptomyces) comprises streptomyces olivochromogenes (S.olivochromogenes); Be found in the fiber degradation rumen bacteria, as producing in the thread bacillus of butanedioic acid (Fibrobacter succinogenes); Be found in the yeast, described yeast comprises some kind of Mycotoruloides (Candida), comprises antarctic candida (C.Antarctica), candida rugosa (C.rugosa), torresii; Candida parapsilosis (C.parapsllosis); Candida sake bacterium (C.sake); Candida zeylanoides bacterium (C.zeylanoides); Little Pichia pastoris (Pichiaminuta); Rhodotorula glutinis (Rhodotorula glutinis); Saccharomyces muciparus (R.mucilaginosa); And Sporobolomycesholsaticus.

[115] at preferably is added to aqueous enzyme solutions in following amount: by the zymoprotein of fabric weight from 0.00001% to 2%, preferably, zymoprotein by fabric weight from 0.0001% to 1%, more preferably, zymoprotein by fabric weight from 0.005% to 0.5%, even more preferably, by the zymoprotein of fabric weight from 0.001% to 0.5%.

Cellulase

[116] cellulase also is can consider to be used for method and composition described herein to be used for biological kiering.Cellulase by comprise inscribe-and circumscribed-activity and cellobiose hydrolysis ability be categorized as a series of enzyme families.The cellulase that uses in the present invention practice can be derived from the known microorganism that can produce cellulolytic enzyme, for example detritus Pseudomonas, thermophilic fungal genus, Bacillus, trichoderma, Fusarium, myceliophthora, show the flat lead fungi genus of hair, rake teeth Pseudomonas (Irpex), Scytalidium (Scytalidium), Schizophyllum (Schizophylium), Penicillium notatum, aspergillus or Geotrichum (Geotricum) certain.The known kind that can produce cellulolytic enzyme comprises special humicola lanuginosa, Fusarium oxysporum (Fusarium oxysporum) or trichoderma reesei.Be disclosed in U.S. Patent number 4,435,307 in the cellulase limiting examples that is fit to; European Patent Application No. 0 495 257; PCT number of patent application WO 91/17244; In European Patent Application No. EP-A2-271 004, all these are introduced into this paper as a reference.

[117] cellulase also is used for the biological clear-cut finish of textiles.Cotton can the processing by the enzyme that is known as " biological clear-cut finish " based on cellulosic natural fabric with other improved.This processing gives fabric the more smooth and outward appearance of gloss more.This processing is used to remove the fiber of the shallow bid of " microtriche (fuzz) "-produce from the yarn surface.In the textiles trade, the ball of microtriche is called " fiber bobbles (pill) ".After biological clear-cut finish, microtriche and fiber bobbles are reduced.Other benefit of removing microtriche is more soft, more smooth feel and good colour brightness (colorbrightness).

[118] in the embodiment of method of the present invention, the operable concentration range of cellulase is from the zymoprotein by fabric weight from 0.0001% to 1%, preferably, by the zymoprotein of fabric weight from 0.0001% to 0.05%, particularly by the zymoprotein of fabric weight from 0.0001% to about 0.01%.

[119] mensuration of cellulase activity (ECU)

The activity that cellulose decomposes can be passed through the ability of the viscosity of measurement enzyme reduction carboxymethyl cellulose (CMC) solution and determine with inscribe-cellulase unit (ECU).ECU detects the ability that reduces the viscosity of carboxymethyl cellulose (CMC) solution by measuring samples, quantizes to be present in the amount of the catalytic activity in the sample.This at the vibration viscosity apparatus (for example detects, derive from Sofraser, the MIVI 3000 of France) carries out in, condition is 40 ℃, the phosphate buffer of pH 7.5,0.1M, 30 minutes time, uses the relative enzyme standard items (Hercules 7 LED), the about 0.15ECU/ml of enzyme concentration that reduce CHIC substrate viscosity.The main standard product are defined as 8200ECU/g.

[120] ECU are the amounts that reduce the enzyme of half viscosity under these conditions.

Other biological kiering enzyme

[121] the invention is not restricted to use the enzyme that is used for biological kiering of above-mentioned discussion.Other enzyme can be separately or mutually combination or with those above-mentioned being used in combination of listing.For example can use protease in the present invention.The protease that is fit to comprises those of animal, plant or microbial source, preferably, is those of microbial source.Protease can be serine protease or metalloproteinases, preferably, is the protease of alkaline microbial protease or tryptose enzyme.The example of protease comprises aminopeptidase, and it comprises prolyl aminopeptidase (3.4.11.5), X-pro aminopeptidase (3.4.11.9), bacterium LAP (3.4.11.10), thermophilic aminopeptidase (3.4.11.12), lysyl aminopeptidase (3.4.11.15), tryptophanyl aminopeptidase (3.4.11.17) and Peptidase MSTN (3.4.11.18); The serine endopeptidase, it comprise chymotrypsin (3.4.21.1), trypsase (3.4.21.4), Cucumisin (cucumisin) (3.4.21.25), brachyurin (3.4.21.32), cerevisin (cerevisin) (3.4.21.48) and subtilopeptidase A (3.4.21.62); The cysteine endopeptidase, it comprises papain (3.4.22.2), ficain (3.4.22.3), chymopapain (3.4.22.6), asclepain (3.4.22.7), actinidain (3.4.22.14), caricain (3.4.22.30) and ananain (3.4.22.31); Aspartic acid peptide chain restriction endonuclease, it comprise pepsin A (3.4.23.1), aspergillus pepsinogen I (Aspergillopepsin I) (3.4.23.18), Penicillopepsin (Penicillopepsin) (3.4.23.20) and sugared pepsin (Saccharopepsin) (3.4.23.25); With the metal endopeptidase, comprise Bacillolysin (3.4.24.28).

[122] limiting examples of subtilopeptidase A comprises: subtilopeptidase A BPN ', subtilopeptidase A amylosacchariticus, subtilopeptidase A 168, subtilopeptidase A mesentericopeptidase, subtilopeptidase A Carlsberg, subtilopeptidase A DY, subtilopeptidase A 309, subtilopeptidase A 147, hot enzyme (thermitase), aqualysin, bacillus PB92 protease, Proteinase K, protease TW7 and protease TW3.

[123] commercially available protease comprises: Alcalase ^TM, Savinase. ^TM, Primase. ^TM, Duralase. ^TM, Esperase ^TM, Kannase ^TMAnd Durazym ^TM(NovoNordisk A/S), Maxatase. ^TM, Maxacal. ^TM, Maxapem ^TM, Properase ^TM, Purafect ^TM, Purafect OxP ^TM, FN2. ^TMAnd FN3 ^TM(Genencor InternationalInc.).

[124] also available in the present invention is ease variants, those disclosed: EP 130 in following patent or disclosed patent application for example, 756 (Genentech), EP 214,435 (Henkel), WO 87/04461 (Amgen), WO 87/05050 (Genex), EP 251,446 (Genencor), EP 260,105 (Genencor), Thomas, et al., (1985), Nature.318.p.375-376, Thomas, et al., (1987), J.MoI.Biol., 193, pp.803-813, Russel, etal., (1987), Nature, 328, p.496-500, WO 88/08028 (Genex), WO 88/08033 (Amgen), WO 89/06279 (Novo Nordisk A/S), WO 91/00345 (NovoNordisk AJS), EP 525 610 (Solvay) and WO 94/02618 (Gist-Brocades N.V.), all these are introduced into this paper as a reference.

[125] protease activities can be as at " Methods of Enzymatic Analysis ", thirdedition, and 1984, Verlag Chemie, Weinheim measures described in the vol.5.

In other specific embodiment of the present invention, can consider that [126] lipase is used from the biological kiering of textiles separately or with other biological kiering enzyme one of the present invention.The lipase (being also referred to as carboxylic ester hydrolases) that is fit to includes, but not limited to those of bacterium or fungal source, comprises triglyceride lipase (3.1.1.3) and phospholipase A ₂(3.1.1.4.).The lipase of Shi Yonging comprises in the present invention, but be not limited to, be derived from the lipase of Humicola (different name thermophilic fungal genus), for example be derived from H.lanuginosa (dredging the thermophilic hyphomycete of continuous shape (T.lanuginosus))---as patent or disclosed patent application EP 258,068 and EP 305, described in 216, or from described in special humicola lanuginosa such as the WO 96/13580; Pseudomonas lipase, (EP 218 from Pseudomonas alcaligenes or pseudomonas pseudoalcaligenes for Tathagata, 272), Pseudomonas cepacia (P.cepacia) (EP 331,376), Pseudomonas stutzeri (GB 1,372,034), Pseudomonas fluorescence (P.fluorescens), certain bacterial strain of pseudomonas SD 705 (WO 95/06720 and WO 96/27002), P.wisconsinensis (WO 96/12012); Bacillus lipase is as from hay bacillus (B.Subtilis) (Dartois, et al., Biochem.Biophys.Acta, 1131:253-360,1993); Bacillus stearothermophilus (B.stearothermophilus) (JP64/744992) or bacillus pumilus (B.pumilus) (WO91/16422), all lists of references are introduced into this paper as a reference.Those that other example is a lipase Variant as describing in WO 92/05249, WO 94/01541, EP 407 225, EP 260 105, WO95/35381, WO 96/00292, WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202, all these are introduced into this paper as a reference.The preferred commercial lipase that gets comprises Lipolase ^TMWith Lipolase Ultra ^TM, Lipozyme ^TM, Palatase ^TM, Novozym ^TM435 and Lecitase ^TM(all can obtain) from Novo Nordisk A/S.The activity of lipase can as " Methods of Enzymatic Analysis ＂, Third Edition, 1984, Verlag Chemie, Weinhein measures described in the vol.4.

[127] be understandable that any enzyme that shows biological kiering activity can be used for practice of the present invention.Just can use biological kiering enzyme, or from the biological kiering enzyme of above-listed enzyme from other organism---wherein add, lack or replace one or more amino acid, comprise the hybridization polypeptide, as long as resulting polypeptide shows biological kiering activity.Utilize traditional method of mutagenesis to produce and for example utilize high pass to cross triage techniques such as agar plate screening technique and differentiate and can be used for putting into practice this class variant of the present invention.For example, the activity of pectate lyase can be applied in the hole of the 4mm that stamps out in the agar plate (for example, LB agar) and measures by detecting solution, contains 0.7%w/v polygalacturonase sodium (Sigma P 1879) in described hole.This agar plate descended incubation 6 hours at an actual temp (for example, 75 ℃) then.This agar plate is immersed in (i) 1M CaCl then ₂In 0.5 hour; Or (ii) in the 1% alkyl trimethyl ammonium bromine (MTAB, Sigma M-7635) that mixes 1 hour.Two kinds of steps cause polygalacturonate to precipitate in agar.The pectate lyase activity can detect by the outward appearance in the clear zone in the background of the polygalacturonate that precipitates.Use the dilution of the standard items preparation of pectate lyase, the sensitivity of calibration analyte.

Bleaching agent

[128] in an embodiment of the invention, bleaching agent is used for handling the present invention's textiles.The present invention does not limit and uses bleaching agent or use any specific bleaching agent.Similarly, the present invention does not limit and only uses a kind of bleaching agent.Exemplary bleaching agent of the present invention is, for example hydrogen peroxide, urea peroxide, sodium carbonate peroxide (sodium carbonate peroxide), sodium peroxide, sodium perborate, clorox, calcium hypochlorite and DCCNa.In preferred embodiment, hydrogen peroxide is used as bleaching agent.In another embodiment, the agent of the independent inclusive NAND enzymatic bleach of enzymatic living beings bleaching agent is used together.The unrestricted example of enzymatic living beings bleaching agent is peroxidase (Colonna, et ai.Recent biological developemtns in the useof peroxidases, Tibtech, 17:163-168,1999) and oxidoreducing enzyme (for example, glucose oxidase) (Pramod, Liquid laundry detergents containing stabilizedglucose-glucose oxidative system for hydrogen peroxide generation, US5288746).

[129] in this composition and method, use Perhydrolase and other chemical bleaching agent (one or more), zinc or aluminium salt as SODIUM PERCARBONATE (sodium percarbonate), sodium perborate, sodium sulphate/hydrogen peroxide adduct and sodium chloride/hydrogen peroxide adduct and/or photosensitive bleaching dyestuff such as sulfonated phthalocyanine dye use together, further improve bleaching effect.In other embodiment, Perhydrolase of the present invention and bleach boosters (for example, TAED, NOBS) use together.

The bleach system of enzyme

[130] crossing the key component that hydrolysis produces peracid by enzymatic is enzyme, ester substrate and hydrogen peroxide.

Hydrogen peroxide

[131] hydrogen peroxide can directly add in batches, or " original position " produces constantly.Acyltransferase also can with any other appropriate H ₂O ₂Use together in the source, comprises the H that produces by chemistry, electrochemistry and/or Enzymology method ₂O ₂The example in chemistry source is above-mentioned percarbonate and peroxy-borate, and the example in electrochemistry source is a fuel cell of supplying with oxygen and hydrogen, and the enzymatic example comprises from utilizing glucose and glucose oxidase enzyme reaction to produce H ₂O ₂Establishing an equation down provides the example of the coupling system that uses with the present invention.

Glucose oxidase

Glucose+H ₂O------------------------------------------gluconic acid+H ₂O ₂

+

Perhydrolase

H ₂O ₂+ ester substrate----------------------------------------alcohol+peracid

[0227] is not intended to limit the invention to any concrete enzyme, because and suitable substrates generation H ₂O ₂Any enzyme all useful in the method for the invention.For example, useful in the present invention from the LO that lactic acid bacteria (Lactobacillus) is planted, known described LO generates H by lactic acid and oxygen ₂O ₂In fact, an advantage of method of the present invention is, the generation of acid (for example, gluconic acid in the above example) is reduced to the pH scope of effective bleaching (that is, in the pKa value or be lower than the pKa value) of peracid with the pH of alkaline solution.Other enzyme (for example, alcohol oxidase, oxidation of glycol enzyme, glycerol oxidase, amino acid oxidase etc.) that can produce hydrogen peroxide also can be used in combination with ester substrate and Perhydrolase of the present invention, produces peracid.In some preferred implementations, the ester substrate is selected from one or more in the following acid: formic acid, acetate, propionic acid, butyric acid, valeric acid, sour, sad, n-nonanoic acid, capric acid, dodecylic acid, tetradecanoic acid, hexadecanoic acid, octadecanoid acid and oleic acid.Therefore, as described herein, for textile bleaching, the invention provides than present application the clear and definite advantage of method and composition.

Acyltransferase

[133] find that in the present invention useful acyltransferase describes in WO 05/056782.

[134] application of the enzyme that obtains from microorganism is long-standing.In fact, many known biocatalysts are arranged in this area.For example, U.S. Patent number 5,240,835 (being incorporated herein by reference at this) provide description active to the transacylase that obtains from C.oxydans and that produce.In addition, U.S. Patent number 3,823,070 (being incorporated herein by reference at this) provides produced the coryneform description of some aliphatic acid by normal paraffin hydrocarbons.U.S. Patent number 4,594,324 (being incorporated herein by reference at this) provide the description to the pod membrane methyl coccus (Methylcoccus capsulatus) of oxyalkylene.Other biocatalyst be known in the art (referring to, for example, U.S. Patent number 4,008,125 and 4,415,657; Both all incorporate into herein as a reference).EP 0 280 232 has described the C.oxydans enzyme has been used in the reaction between the ester of two pure and mild acetate, produces monoacetate.Other reference file descriptor with the C.oxydans enzyme in the past chiral diol prepare the chiral hydroxyl group carboxylic acid.About the active of C.oxydans transacylase and the details of cultivating C.oxydans, preparation and this enzyme of purifying are provided at U.S. Patent number 5,240, in 835 (being incorporated herein by reference as mentioned above).Therefore, mainly to use the ester exchange reaction ability of acetic acid esters be known to this enzyme.Yet, determine that it is very unexpected that this endonuclease capable carried out hydrolysis.More surprisingly, these enzymes demonstrate very high efficient in crossing hydrolysis.For example, under the situation of glycerin tributyrate and water existence, this enzyme produces butyric acid, and under the situation that glycerin tributyrate, water and hydrogen peroxide exist, this enzyme mainly produces peracetic acid and considerably less butyric acid.This high hydrolysis and the hydrolysis ratio crossed is the peculiar property that the enzyme of Perhydrolase type of the present invention shows, and the unique property that do not show of lipase, at and the esterase of description before being.

[135] Perhydrolase of the present invention has activity in wide pH and temperature range, and the substrate of accepting wide region is used for acyl group and shifts.Acceptor comprises water (hydrolysis), hydrogen peroxide (crossing hydrolysis) and alcohol (classical acyl group shifts).Measure in order to carry out hydrolysis, make enzyme in the buffer solution of selecting, under the temperature of appointment and the substrate ester, under the situation that hydrogen peroxide exists, carry out incubation.The typical substrate that is used to measure hydrolysis comprises ester such as ethyl acetate, glycerol triacetate, glycerin tributyrate and other substrate.In addition, the nitrobenzophenone ester of this wild-type enzyme hydrolysis short chain acids.The latter is the substrate that makes things convenient for of measuring enzyme concentration.By analytical method described herein, can measure peracid and acetate.The hydrolysis of nitrobenzophenone ester has also been described.

[136] though the main example that uses in development process of the present invention is the mycobacterium smegmatis Perhydrolase, any Perhydrolase that obtains from any source that ester mainly can be changed into peracid under the situation that hydrogen peroxide exists is all in the present invention available.

[137] in an embodiment of this method, the operable concentration range of Perhydrolase is 0.0001-100ppm in wash liquid; 0.0001-50ppm preferably; 0.0001-25ppm more preferably; 0.0001-10ppm preferably.In another embodiment of this method, the operable concentration of Perhydrolase is every gram fabric 0.0001-1%; More preferably, every gram fabric 0.0001-0.1% or every gram fabric 0.0001-0.01%.

Substrate

[138] in preferred implementations more of the present invention, comprise that the ester of aliphatic series and/or aromatic carboxylic acid and alcohol is used with the Perhydrolase of the present composition.In some preferred implementations, the ester substrate is selected following one or more: formic acid, acetate, propionic acid, butyric acid, valeric acid, sour, sad, n-nonanoic acid, capric acid, dodecylic acid, tetradecanoic acid, hexadecanoic acid, octadecanoid acid and oleic acid.Therefore, in some preferred implementations, the composition that provides comprises at least a Perhydrolase, at least a hydrogen peroxide source and at least a ester acid.In other embodiments, glycerol triacetate, glycerin tributyrate and other ester are as the acry radical donor that is used to form peracid.

Process conditions

[139] whether comprising mode that the aqueous solution of enzyme (one or more) and bleach system contacts with textile material, will to rely on processing scheme be continuous, semicontinuous, discontinuous volume heap, (or Continuous Flow) in batches of padding.For example, to the continuous or discontinuous volume heap technology of padding, aqueous enzyme solutions preferably is contained in the saturated tank (saturator bath), and when passing this groove, textiles is applied successively to this textile material, textile material absorbs a certain amount of working fluid usually in this process, for example, 0.5 of its deadweight to 1.5 times.In batch operation, be that fabric is exposed to a period of time in the enzyme solutions under the 5:1 to 50:1 at liquid with the fabric ratio, scope was from about 2 minutes to 24 hours.These are General Parameters.In some embodiments, the denseer solution of enzyme and other compound can shorten the time in the application of the invention.Those skilled in the art can determine the most suitable its parameter of needs separately.

[140] method disclosed herein can be carried out under than the lower temperature of traditional kiering, destarch and bleaching technology.In one embodiment, the method is being carried out below 95 ℃, preferably, and between about 15 ℃ to 95 ℃.In preferred embodiment, method of the present invention is being carried out between about 24 ℃ to 80 ℃.In preferred embodiment, method of the present invention is being carried out the result who obtains satisfaction between about 40 ℃ to about 60 ℃.

[141] method of the present invention can carried out under the pH scope of more approaching neutrality mutually than traditional kiering, destarch and bleaching technology.Though it is useful that the method is found between about 5 to 11 in the pH value, preferred pH value is lower than 9.In one embodiment, the pH value of the inventive method implementation is between about 6 to 9, preferably between 6 to 8.In preferred embodiment, the pH value that the inventive method is carried out is between about 7.5 to 8.5.In further preferred embodiment, the pH value is about 8.0.

[142] those of ordinary skills know, the process conditions of using in the present invention carries out can be selected, so that meet the particular device or the particular type of the technology of required use.For example, the textiles that needs to handle preferably keeps in touch with treatment fluid, its temperature is from about 15 ℃ to about 90 ℃, preferably from about 24 ℃ to about 80 ℃, most preferably from about 40 ℃ to about 60 ℃, and the suitable time of handling textiles be at least about 2 minutes to 24 hours, more preferably from about 30 minutes to about 12 hours, preferably from about 30 minutes to about 6 hours, most preferably from about 30 minutes to about 90 minutes.Certainly, those of ordinary skills know that reaction condition such as time and temperature will change according to the fabric of the equipment that uses and/or technology and processing.

[143] preferred embodiment for the treatment of the technology type that uses with the present invention includes, but not limited to spray (Jet), dye gigging agent/capstan winch (Jigger/Winch), writing that surpasses all the others dyeing (Pad-Roll) and compregnate gas steaming (Pad-Steam) type and continuous bleaching class.Group technology of the present invention can use steam or cold bleaching principle as batch, semicontinuous or continuous processing carries out.As an example, this technology can comprise following steps: a) as described herein, fabric is immersed kiering and bleaching cistern, extrude excessive liquid subsequently, so that keep the amount of carrying out the necessary liquid of reaction (usually between dry fabric weight 60% and 120% between), b) make the processing of infiltration fabric steam, so that make fabric reach required reaction temperature, usually between about 20 ℃ to 80 ℃, and c) passes through at J-Box, U-Box, in carpet knitter (carpet machine) or its analog fabric rolled or pleating, keep the long enough time durations, so that kiering and bleaching take place.

[144] mention as other places, destarch can be the result of expectation.Therefore for the fabric of certain type, the final products that fabric desizing is handled to obtain desired qualities can be favourable and/or essential.In such a case, the present invention can be used as the combination of destarch, bleaching and boiling, or the combination of destarch and bleaching process, or the combination of destarch and boiling.

[145] method of the present invention comprises providing and does not put the textiles composition in order to Treatment Solution, as described.The textiles component can comprise fiber, yarn, fabric, and it comprises woven fabric, braided fabric, clothes and non-woven thing.For unfinished, the textiles component is intended that not by destarch, kiering, bleaching, dyeing, stamp or other material of arrangement step such as durable impression is provided.Certainly, those of ordinary skills know that the textiles among the present invention is those textiless that do not pass through ready-made clothes or comprise other production technology of cutting out and sewing of material.

[146] this technology can use any textile material to comprise cellulose and synthetic material, described cellulose is as cotton, flax, ramee, hemp, artificial silk, Lyocell fibers, cellulose acetate and Triafol T, described synthetic material comprises, but be not limited to polyester, nylon, spandex, Lycra, acrylic resin and various other mixture natural and synthetic material.Be purpose of the present invention, natural material can comprise protein fibre such as wool, silk, goat cashmere, also has the described cellulose in this paper place.

[147] this technology can be used for bleaching, to several types may be easily by the synthetic textiles of basic hydrolysis and degraded and their mixture, include but are not limited to, polyester, artificial silk, acetate, nylon, cotton/polyester, cotton/Lycra etc. do not have perceptible fiber or fabric damage.

[148] method of the present invention further can comprise the step that singeing and mercerising are handled after treatment step.Although destarch can be used with independent step, in a preferred embodiment, the destarch step be included in the step processing of the present invention, so bleaching, destarch and kiering is combined as a step via comprise destarch enzyme (one or more) in treatment trough.

[149] certain, in a preferred application, technology of the present invention is included in cleaning step or a series of cleaning step after the step processing method provided herein.The textiles of clean is known and within technical staff's technical merit.Wash phase appears at each destarch, kiering and blanching step usually---when existing---and afterwards, and after treatment step of the present invention.In addition, no matter its order and/or combination, in a preferred embodiment, treatment step can comprise one, and to soak or prewet step even or consistent moistening to guarantee in textiles.

[150] method of the present invention provides wettable preferably for the textiles component of handling through the method.The wettable of textiles is important to any dyeing and the arrangement of textiles.Wettable cause dyeing or finishing agent to the infiltration preferably of textiles, and textile dyeing preferably and/or arrangement result.Therefore, the wettable of textiles is the index how many effects treatment process has.Higher wettable means more effective and better treatment process, that is, and and shorter infiltrating time length.Traditional textiles peroxide bleaching only provide acceptable moistening character when temperature surpasses 95 ℃, and lower bleaching temperature (70 ℃) obtains the wettable performance greater than about 40%.Yet technology of the present invention provides the fabric with about below 10%, preferred about wettable index enhancing 5% below, and the wettable index definition of this paper is:

[(70 ℃ wettables)-(95 ℃ wettables)]/(95 ℃ wettables) are represented with the percentage form.Another selectable trap detects, for example, AATCC detection method 79-1995, it is wetting to be used for after handling fast detecting.

[151] be purpose of the present invention, detect by AATCC detection method 82-1996 that it is included in loosen collagen fibre in the cupri ethylene diamine (CP) based on the fibre damage of flowability.The representational fiber sample of the about 1.5mm of cutting is dissolved in it among the CP in sample bottle with several glass marbles---and described CP is limited by equation CP=120 * example weight * 0.98, is placed under the nitrogen and by shaking dissolving in about 2 hours.Adding additional C P---described CP is according to equation CP=80 * example weight * 0.98 qualification, and shakes in addition under nitrogen 3 hours.Solution is placed in and at the uniform velocity stirs down to prevent the separation of disperse system.Then, solution is measured on 25 ℃ of constant temperature baths with the Oswald Canon Fenske viscosity apparatus after calibrating, to determine the delivery time.Calculate from formula F=100/ctd then mobile, c=viscosity constant wherein, t=delivery time, the density 1.052 of d=solution.

Auxiliary element

[152] Treatment Solution of the present invention also can comprise various auxiliary elements, and this paper is also referred to as auxiliary chemicals.Such composition includes, but not limited to sequestering agent or chelating agent, wetting agent, emulsifying agent, pH value controlling agent (for example, buffer solution), bleaching catalyst, stabilizing agent, dispersant, antifoaming agent, washing agent and their mixture.Be appreciated that such auxiliary element is except that enzyme of the present invention, hydrogen peroxide and/or hydrogen peroxide source with comprise the ester moiety material.Wetting agent is selected from surfactant usually and particularly is selected from non-ionic surface active agent.The level of the wetting agent that uses generally include this bath about 0.1 to about 20g/L, more preferably about 0.5 to about 10g/L, further preferably about 0.5 to about 5g/L.The a variety of causes of use stabilizing agent comprises buffer capacity, sequester, dispersion and additionally strengthens the performance of surfactant.But stabilizing agent can slow down the speed of peroxide breakdown and can and cause the metal impurities combination of fiber infringement or with its neutralization with the catalysis peroxide breakdown.Along with inorganic or organic class is fully realized and silicate and organophosphorus ester acquisition approval the most widely, stabilizing agent is fully realized, the level of using in the present invention be this bath about 0.01 to about 30g/L, further preferably about 0.01 to about 10g/L, most preferably about 0.01 to about 5g/L.

Surfactant

[153] be fit to nonrestrictive the comprising of surfactant that the present invention puts into practice use, and nonionic (see, for example, U.S. Patent number 4,565,647, it is introduced into this paper as a reference); Anion; CATION; And zwitterionic surfactant (see, for example, U.S. Patent number 3,929,678, it is introduced into this paper as a reference); Its concentration that usually exists is between by weight from about 0.2% to about 15%; Preferably by weight from about 1% to about 10%.Anion surfactant is nonrestrictive to be comprised, linear alkyl benzene sulfonate, alpha-alkene sulfonate, alkyl sulfate (aliphatic alcohol sulfate), alcohol ethoxy sulfate, secondary alkyl sulfonate, α-thia fatty acid methyl esters, alkyl or alkene butanedioic acid and soap.Non-ionic surface active agent comprises without limitation, the N-acyl group N-alkyl derivative (glucamide (glucamides)) of alcohol ethoxylate, nonyl phenol ethoxylate, alkyl poly glucoside, alkyl-dimethyl amine oxide, ethoxylated fatty acid single ethanol amide, fatty monoethanol amide, polyhydroxy alkyl fatty acid amide and aminoglucose.The preferred surfactant that uses in the embodiments of the present invention is non-ionic surface active agent or nonionic and anion mixture.

Chelating agent

[154] chelating agent also can use, and can be selected from aminocarboxylic acid ester, amido phosphonate, polyfunctional group replacement aromatic chelating agent and its mixture, and all these limit hereinafter.

[155] can be used as the aminocarboxylic acid ester of optional chelating agent, comprise ethylenediamine tetraacetate, N-hydroxyethyl-ethylenediamine triacetate, nitrilotriacetate, ethylenediamine tetrapropionic acid ester, teiethylene tetramine-hexacetic acid ester, do not contain more than the alkyl of about 6 carbon atoms or the phosphonate ester of alkenyl.

[156] aromatic chelator that replaces of polyfunctional group also is useful in the composition of this paper.See the U.S. Patent number 3,812,044 that licensed to Connor etc. on May 21st, 1974.The form of the acid of preferred this compounds is that the dihydroxy disulfobenzene is as 1,2-dihydroxy-3,5-disulfobenzene diethylenetriamine pentaacetic acid ester and ethanol Diglycocol (ethanoldiglycine), alkali metal, ammonium and their substituted ammonium salt and their mixture.

[157] when allowing the phosphorus total amount of low concentration at least, amino phosphonates do also is suitable as chelating agent and uses in composition of the present invention.

[158] preferred biodegradable chelating agent used herein is EDDS ester (" EDDS "), its [S, S] isomers particularly, and as licensing to the United States Patent (USP) 4,704 of Hartman and Perkins on November 3rd, 1987, described in 233.

[159] when existing, the concentration that chelating agent uses is from about 0.01 to about 10g/L, more preferably from about 0.1 to about 5g/L, most preferably from about 0.2 to about 2g/L.

Commercial Application of the present invention

[160] the present invention has many practical applications industrial, and is desired as this paper, and this specification is intended that exemplary but not comprising property.

[161] in one embodiment, the present invention has the application of expection in industrial textile: main in the processing of fiber, yarn, fabric, clothes and non-woven thing.The main application comprises: a step enzyme of textiles is handled, and comprises the kiering and the bleaching of textiles.The destarch of textiles also can be finished simultaneously with kiering, bleaching and kiering-bleaching.

The dosage of the enzyme component that [162] gives in the composition (that is concentration) depends on given activity, process conditions and required result.Those skilled in the art can determine dosage level.

[163] composition as herein described and method, than the processing of tradition based on chemicals, for example alkaline kiering, bleaching etc. provide effective textile treatment to reduce loss of strength simultaneously.Be not bound by theory, can believe, when comparing based on the processing of chemicals with tradition, this composition and method are still less damaged fiber, and therefore reduce loss of strength.Loss of strength can be passed through technical measurement well known in the art, as ASTM D 5034 (grabbing sample experiment (Grab test)), ASTMD 5035 (fabric galley proof strength test (Strip test)), ASTM D 3787 (ball burst testing (Ball burst test)), and/or ASTM D 3786 (the hydraulic method top resistance to spalling of knitwear and non-woven fabric).

[164] in the experiment disclosure below, use following abbreviation: eq (equivalent); M (mole); μ M (micromolar); N (just); Mol (mole); Mmol (mM); μ mol (micromole); Nmol (nanomole); G (gram); Mg (milligram); Kg (kilogram); μ g (microgram); L (liter); Ml (milliliter); μ l (microlitre); Cm (centimetre); Mm (millimeter); μ m (micron); Nm (nanometer); ℃ (degree centigrade); H (hour); Min (minute); Sec (second); Msec (millisecond); Ci (Curie); MCi (millicurie); μ Ci (micromicrocurie); TLC (thin-layer chromatography (thin layerachromatography)); Ts (tosyl); Bn (benzyl); Ph (phenyl); Ms (mesyl); Et (ethyl); Me (methyl).

Embodiment

[165] the following examples have described in further detail the present invention, and embodiment is intended to limit the desired scope of the invention.Accompanying drawing is intended to be considered the intact part of description of the present invention and specification.The list of references of all references is incorporated as reference especially at this, is used for all the elements described herein.Provide the following examples that invention required for protection is described for example rather than limit it.

Embodiment 1

Cotton step enzymatic preliminary treatment

[166] present embodiment has exemplified cotton and has contained the embodiment that one of cotton fiber and fabric goes on foot enzymatic preliminary treatment (destarch, kiering and bleaching).

[167] test from Testfabrics (West Pittiston, the military careless sateen of 428R type PA) (Army card cotton sateen) greige goods fabric and from the 428U type of Testfabrics, destarch but carry out on the unbleached military careless sateen fabric.

[168] enzyme of Shi Yonging is:

The acyltransferase variant S51A98T (Genencor of 1ppm; WO 05/056782);

The Purastar OxAm 4000E (α-Dian Fenmei that Genencor is oxidation-stabilized) of 1g/L;

The Optisize 160 of 2ml/L (the conventional α-Dian Fenmei of Genencor);

The Bioprep 3000L of 6ml/L (Novozymes pectate lyase);

At (the Genencor of 4ppm; At U.S. Patent number the 5th, 512, pseudomonas mendocina at described in 203 or the variant described in WO 03/76580 with sudden change F180P/S205G).

[169] other compound of Shi Yonging is:

The Triton X-100 of surfactant: 0.25g/L;

The propylene-glycol diacetate of 3000ppm;

The hydrogen peroxide of 2000ppm;

0.01% ammoniated ruthenium oxychloride dyestuff in the phosphate buffered solution of pH 6.8,50mM;

(iodine solution prepares by following method: the KI of 10g is dissolved in the DI water of 100ml iodine solution, adds the iodine of 0.65g then and stirs this solution until dissolving fully.In this solution, add DI water to 800ml, add ethanol then) to 1L.

[170] for detecting destarch, kiering and bleaching effect of Combination,, use three 4 inches * 3 inches military careless cotton sateen greige goods fabric sample (428R type) to carry out from Testfabrics in the experiment shown in the table 1.The experiment of all scrutinies (1-19) was carried out 60 minutes under the condition of 50 ℃ and pH 8 in Launder-O-meter.Fabric is soaked in pads volume heap experiment in the reaction solution after 5 minutes, with it by cylinder and at room temperature (24 ℃) incubation 24 hours down.After these were handled, all fabric samples thoroughly clean with entering water, and were air-dry before evaluation then.Commercially available bleaching from the military careless sateen of Testfabrics in all handling as positive control.

[171] table 1

Numbering	Handle
			1	Buffer solution
2	Buffer solution+surfactant
		3	Buffer solution+surfactant+PGDA
4	Buffer solution+surfactant+PGDA+H 2O 2
		5	Buffer solution+surfactant+OxAm
6	Buffer solution+surfactant+BP 3000L
		7	Buffer solution+surfactant+at

8	Buffer solution+surfactant+PGDA+H 2O 2+BP 3000L
		9	Buffer solution+surfactant+PGDA+H 2O 2+ at
10	Buffer solution+surfactant+PGDA+H 2O 2+AcT
		11	Buffer solution+surfactant+PGDA+H 2O 2+ AcT+OxAm+BP 3000L+ at
12	Buffer solution+PDGA+H 2O 2+AcT
		13	Buffer solution+PDGA+H 2O 2+OxAm
14	Buffer solution+PDGA+H 2O 2+BP 3000L
		15	Buffer solution+PDGA+H 2O 2+ at
16	Buffer solution+PDGA+H 2O 2+ AcT+OxAm+BP 3000L+ at
		17	Buffer solution+PDGA+H 2O 2
18	Buffer solution+surfactant+PGDA+H 2O 2(padding the volume heap)
		19	Buffer solution+surfactant+PGDA+H 2O 2+ AcT+OS 160+BP 3000L (padding the volume heap)
428R	Greige goods fabric
		428U	Destarch from Testfabrics
428	Commercially available bleaching from Testfabrics

[172] bleaching effect is by using the Minolta spectrophotometric determination CIEL of model C R-2000 ^*Value quantizes, CIE L ^*The value representation whiteness.Higher CIE L ^*Value shows better bleaching.

[173] residual starch that uses iodine test to detect to remain in after each is handled in the fabric is to measure the destarch effect.Downcut 5 3/8 inch fabric disk and every disk is put into about one minute of the iodine solution of 2ml from each sample.This disk dabs with cold water flush and with filter paper rapidly then.Use reflectometer (Reflectometer) to measure the CIE L of disk at once ^*Value.High more CIE L ^*Value shows that the residual starch in the fabric is few more, shows good more destarch performance.[174] kiering effect quantizes by the visual evaluation of water drop test, ammoniated ruthenium oxychloride dyeing and dirt bits.The water that water drop test is passed through to drip 10 μ l is measured water droplet then and is undertaken by the time that fabric absorbs on the fabric face of handling.Similarly, all fabrics of handling dyeed 5 minutes with 0.01% ammoniated ruthenium oxychloride dye solution, with the amount of remaining colloid in the fabric after the quantification treatment.Then, the fabric of cleaning down dyeing, and measuring CIE L ^*Air-dry before the value.Low more CIE L ^*Value shows high more colloid combination, and this is relevant with low more kiering performance.(PSU) quantize removing of dirt bits by panel score element (panel score unit), wherein 0 shows there are not the dirt bits, and 5 show a large amount of dirt bits.The result is displayed in Table 2.

Table 2

	CIE L *Bleaching	Water droplet destarch second	CIE L *Destarch	CIE L *Kiering	PSU kiering (the dirt bits are removed)
						1	85.5	8	48.4	33.0	5
2	86.1	1	51.0	35.3	5
						3	85.9	1	46.6	31.4	5
4	89.1	1	49.7	31.2	4
						5	86.4	1	52.8	45.6	5
6	86.2	1	55.6	34.4	5
						7	86.0	1	47.6	33.6	5
8	89.4	1	54.4	33.0	3
						9	89.5	1	49.9	31.4	3
10	91.8	1	47.5	35.3	1
						11	91.6	1	55.5	45.1	1
12	89.1	24	48.2	28.8	4
						13	91.8	16	49.5	29.0	2
14	89.8	1	48.7	41.9	4
						15	89.4	18	54.9	27.7	4
16	89.5	11	48.4	28.3	4
						17	91.4	1	53.3	40.5	1
18	87.7	1	47.4	28.4	4
						19	90.1	1	54.4	36.0	1
428R	86.1	300+	51.0	30.4	5
						428U	NA	NA	NA	49.8	NA
428	94.3	1	62.4	77.6	0

[175] as shown in table 2 and Fig. 1-4; in the presence of hydrogen peroxide and propylene-glycol diacetate, the military careless sateen fabric that uses acyltransferase, α-Dian Fenmei, pectate lyase to handle simultaneously shows destarch, kiering (the dirt bits are removed) and the bleaching effect of significant quantity.

Embodiment 2

Cotton bleaching

[176] in the present embodiment, the experiment of estimating the Perhydrolase that is used to bleach COTTON FABRIC among the present invention has been described.

[177] in these experiments, in Launder-O-meter, under 55 ℃, every six cotton sample product are carried out 60 minutes processing.In these experiments, 3 (3 " * 3 ") 428U types and 3 (3 " * 3 ") 400U type substrates are used in each experiment.To from two kinds of the Testfabrics 100% dissimilar COTTON FABRIC of not bleached (428U type (destarch but unbleached military careless sateen) and 400U type (destarch but unbleached cotton print (cotton printcloth))) detect.Liquor ratio is about 26 to 1 (～7.7g fabric /～200ml volume of liquid).Use ethyl acetate (3% (v/v)), hydrogen peroxide (1500ppm) and Triton X-100 (0.001%), in the sodium phosphate buffer (100mM) of pH7 and pH 8, and in the buffer solution of the sodium carbonate (100mM) of pH9 and pH10, the Perhydrolase of 12.7mgP/ml is detected.

[178] use Chroma Meter CR-200 (Minolta), by getting 4 CIE L of each sample before and after treatment ^*a ^*b ^*Value quantizes bleaching effect with total color difference, and the total color difference of the sample after the processing calculates according to following formula:

(wherein, △ L, △ a, △ b are respectively CIE L ^*, CIE a ^*With CIE b ^*Value poor before and after treatment).

[179] higher △ E value shows better bleaching effect.The result (sees, shows that Fig. 5) Perhydrolase all demonstrates the bleaching effect of obvious raising for 8 times to two types 100% COTTON FABRIC under test condition, at pH 7 and pH.

[180] also observe, on the substrate that enzyme is handled, a large amount of dirt bits (for example, painted spot) disappear.

Embodiment 3

The linen bleaching

[181] in this embodiment, the experiment of assessment Perhydrolase of the present invention to the bleaching power of linen described.Used and above-mentioned cotton detection (embodiment 2) identical method and the condition that be used for, to detect the linen sample.As implied above, experiment uses the linen fabric to carry out (linen goods, L-53 type in Launder-O-meter; Testfabrics).

[182] in these experiments, use Perhydrolase and ethyl acetate (3%v/v), hydrogen peroxide (1200ppm) and the Triton X-100 (0.001%) of 12.7mgP/ml, in the sodium phosphate buffer of pH 7 and pH8,3 (4 " * 4 ") linen samples are handled.As above embodiment 2 is described, calculates bleaching effect.Fig. 6 provides figure, and it is illustrated in the bleaching effect of the Perhydrolase of the present invention of pH 7 and 8 times detections of pH to linen.

[183] be appreciated that, embodiment described herein and embodiment only are the purposes in order to exemplify, those skilled in the art will expect various modifications or change with regard to these embodiment and embodiment, and these various modifications or change the spirit and scope will be included in the application and the scope of claims in.For all purposes, all publications, patent and patent application that this paper quotes all are incorporated herein by reference with it.

Claims (63)

1. enzyme bleaching composition comprises:

I) ester source;

Ii) acyltransferase;

Iii) hydrogen peroxide source.

2. the described composition of claim 1 further comprises biological kiering enzyme.

3. the described composition of claim 1 further comprises the destarch enzyme.

4. the described composition of claim 1, wherein said ester source is an acetic acid esters.

5. the described composition of claim 1, wherein said ester source is selected from propylene-glycol diacetate, ethylene acetate, glycerol triacetate, ethyl acetate and glycerin tributyrate.

6. the described composition of claim 1, wherein said acyltransferase performance greater than 1 cross hydrolysis and hydrolysis ratio.

7. the described composition of claim 1, wherein said hydrogen peroxide source comprise the substrate that hydrogen peroxide generates oxidizing ferment and is fit to.

8. the described composition of claim 7, wherein said oxidizing ferment is a carbohydrate oxidase.

9. a step treatment compositions comprises: i) one or more biological kiering enzymes; Ii) one or more destarch enzymes; Iii) enzyme bleaching composition.

10. the described composition of claim 9 further comprises the auxiliary element that one or more are selected from surfactant, emulsifying agent, chelating agent, dispersant and/or stabilizing agent.

11. the described composition of claim 9 further comprises bleach-activating.

12. the described composition of claim 9 further comprises the chemical bleaching agent.

13. the described composition of claim 12, wherein said chemical bleaching agent is selected from oxidative bleaches, sodium peroxide, clorox, calcium hypochlorite and DCCNa or their combination.

14. the described composition of claim 9, wherein said biological kiering enzyme is selected from pectase, at, cellulase, hemicellulase, protease and lipase.

15. the described composition of claim 14, the combination that wherein said biological kiering enzyme is pectate lyase and/or pectate lyase and other enzyme, described other enzyme such as protease, at, lipase and cellulase.

16. the described composition of claim 9, wherein said destarch enzyme is selected from α-Dian Fenmei and beta amylase.

17. the described composition of claim 16, wherein said destarch enzyme is a α-Dian Fenmei.

18. the described composition of claim 10, wherein said surfactant are selected from nonionic, anionic, cationic, amphoteric ionic surfactant or their combination.

19. the described composition of claim 18, wherein said surfactant is a nonionic surface active agent.

20. the described composition of claim 12, wherein said chemical bleaching agent is selected from oxidative bleaches, sodium peroxide, clorox, calcium hypochlorite and DCCNa or their combination.

21. the method for bleaching of textiles comprises:

A. provide: i) ester source; Ii) acyltransferase; Iii) hydrogen peroxide source; Iv) need the textiles bleached;

B. being fit to allow described textiles can survey under the time span and condition of whiteness, described textiles is contacted with hydrogen peroxide source with described ester source, acyltransferase.

22. the described method of claim 21 further comprises one or more biological kiering enzymes.

23. the described method of claim 22, wherein said ester source is an acetic acid esters.

24. the described method of claim 23, wherein said ester source is selected from propylene-glycol diacetate, ethylene acetate, glycerol triacetate, ethyl acetate and glycerin tributyrate.

25. the described method of claim 21, wherein said acyltransferase show hydrolysis and hydrolysis ratio excessively greater than 1.

26. the described method of claim 21, wherein said hydrogen peroxide source comprise the substrate that hydrogen peroxide generates oxidizing ferment and is fit to.

27. the described method of claim 26, wherein said oxidizing ferment is a carbohydrate oxidase.

28. the described method of claim 21, wherein said suitable condition comprises the pH of about 5-11.

29. the described method of claim 28, wherein said pH is between about 6 to 10.

30. the described method of claim 28, wherein said pH is between about 6 to 8.

31. the described method of claim 21, wherein said suitable condition comprises the time span between about 2 minutes to 24 hours.

32. the described method of claim 31, wherein said time span is between about 15 minutes to 12 hours.

33. the described method of claim 31, wherein said time span is between about 30 minutes to 6 hours.

34. the described method of claim 21, wherein said suitable condition comprises the temperature between about 15 ℃ to 95 ℃.

35. the described method of claim 34, wherein said suitable condition comprises the temperature between about 24 ℃ to 60 ℃.

36. the described method of claim 34, wherein said suitable condition comprises the temperature between about 30 ℃ to 50 ℃.

37. the described method of claim 21, the concentration of wherein said hydrogen peroxide are between about 100ppm to 5000ppm.

38. the described method of claim 21, the concentration of wherein said hydrogen peroxide are between about 500ppm to 4000ppm.

39. the described method of claim 21, the concentration of wherein said hydrogen peroxide are between about 1000ppm to 3000ppm.

40. the described method of claim 21, the concentration of wherein said acyltransferase are between about 0.005ppm to 100ppm.

41. the described method of claim 21, the concentration of wherein said acyltransferase are between about 0.01ppm to 50ppm.

42. the described method of claim 21, the concentration of wherein said acyltransferase are between about 0.05ppm to 10ppm.

43. the described method of claim 21, the concentration in wherein said ester source is between about 100ppm to 10, between the 000ppm.

44. the described method of claim 21, the concentration in wherein said ester source is between about 1000ppm to 5000ppm.

45. the described method of claim 21, the concentration in wherein said ester source is between about 2000ppm to 4000ppm.

46. the processing method of textiles comprises:

A. provide: an i) step textile treatment composition; Ii) need the textiles handled;

B. allow under the time span and condition of described textiles destarch, kiering and bleaching being enough to, a described textiles and a described step textile treatment composition are contacted.

47. the described method of claim 46, a wherein said step textile treatment composition comprises: i) one or more biological kiering enzymes; Ii) one or more enzyme bleach systems.

48. the described method of claim 47 further comprises one or more destarch enzymes.

49. the described method of claim 47, wherein said enzyme bleach system comprises acyltransferase, ester source and hydrogen peroxide source.

50. the described method of claim 49, wherein said hydrogen peroxide source comprise the substrate that hydrogen peroxide generates oxidizing ferment and is fit to.

51. the described method of claim 50, wherein said oxidizing ferment is a carbohydrate oxidase.

52. the described method of claim 47, wherein said biological kiering enzyme is selected from pectase, at, protease, cellulase, hemicellulase and lipase.

53. the described method of claim 52, the composition that wherein said biological kiering enzyme is pectate lyase and/or pectate lyase and other enzyme, described other enzyme such as at, cellulase, protease, lipase and hemicellulase.

54. the described method of claim 48, wherein said destarch enzyme is selected from amylase, cellulase and mannase.

55. the described method of claim 54, wherein said destarch enzyme is a α-Dian Fenmei.

56. the described method of claim 47 further comprises the auxiliary element that is selected from surfactant, emulsifying agent, chelating agent, dispersant and/or stabilizing agent.

57. the described method of claim 56, wherein said surfactant is a nonionic surface active agent.

58. the described method of claim 47, wherein said enzyme bleach system generates bleaching agent, and further wherein said bleaching agent is under the existence and acyltransferase catalysis of hydrogen peroxide, the peracetic acid of the mistakes hydrolysis generation by acetate group.

59. the described method of claim 47, a wherein said step composition further comprises the chemical bleaching agent that is selected from oxidative bleaches, sodium peroxide, clorox, calcium hypochlorite and DCCNa or their combination.

60. the described method of claim 46, wherein said textiles is selected from the textiles of cellulose, cellulose and non-cellulose.

61. the described method of claim 60, the textiles of wherein said cellulose or cellulose comprises cotton.

62. the described method of claim 46, wherein said to be enough to allow the condition of described textiles kiering and bleaching be at temperature in the time between about 2 minutes to 24 hours, between about 15 ℃ to 95 ℃ and the pH between about 5 to 11.

63. the described method of claim 46, wherein said to be enough to allow the condition of described textiles destarch, kiering and bleaching be at temperature in the time between about 2 minutes to 24 hours, between about 15 ℃ to 95 ℃ and the pH between about 5 to 11.

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