Classifications

• • D—TEXTILES; PAPER
  • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
  • D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
  • D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
  • D06P5/13—Fugitive dyeing or stripping dyes
  • D06P5/137—Fugitive dyeing or stripping dyes with other compounds
• • D—TEXTILES; PAPER
  • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
  • D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
  • D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
  • D06P5/15—Locally discharging the dyes
  • D06P5/158—Locally discharging the dyes with other compounds

Definitions

• the present methods relate to modifying the color of sized fabrics using a perhydrolase enzyme system, thereby elimination the need for prior desizing.
• Amylases are used for desizing, cellulases are used for abrading and polishing, pectate lyases and pectinases are used for scouring, and catalases are used for bleach clean-up. More recently, enzymes such as perhydrolases and laccases have been used in textile processing to affect color modification.
• compositions and methods relating to color modification of sized fabrics are described.
• a method for modifying the color of a dyed, sized textile comprising, contacting the dyed, sized textile with a perhydrolase enzyme system to modify the color of the textile, wherein the contacting is performed without first desizing the textile.
• the contacting is performed in the absence of desizing the textile. In some embodiments, the contacting is performed prior to desizing the textile.
• the perhydrolase enzyme system comprises a perhydrolase enzyme and an ester substrate, wherein the perhydrolase enzyme catalyzes perhydrolysis of the ester substrate with a perhydrolysis :hydrolysis ratio equal to or greater than 1.
• the perhydrolase enzyme system comprises a Mycobacterium perhydrolase or a variant, thereof.
• the perhydrolase is a Mycobacterium smegmatis perhydrolase.
• the perhydrolase enzyme is a variant of Mycobacterium smegmatis perhydrolase comprising the amino acid substitution S54V.
• the ester substate is PGDA or triacetin.
• the size comprises starch, a starch-like material, or polyvinyl alcohol (PVA). In some embodiments, the size comprises starch, or a starch-like material. In some embodiments, the size comprises starch.
• the textile is denim. In some embodiments, the textile comprises cotton. In some embodiments, the dye is a sulphur dye.
• compositions and methods are particularly relevant to the processing of textile fabrics that are dyed prior to sizing, for example, denim fabrics.
• a "perhydrolase” is an enzyme capable of catalyzing a perhydrolysis reaction that results in the production of a sufficiently high amount of peracid for use in an oxidative dye decolorization method as described. Generally, the perhydrolase enzyme exhibits a high perhydrolysis to hydrolysis ratio.
• the perhydrolase comprises, consists of, or consists essentially of the Mycobacterium smegmatis perhydrolase amino acid sequence set forth in SEQ ID NO: 1, or a variant or homolog thereof.
• the perhydrolase enzyme comprises acyltransferase and/or arylesterase activity.
• perhydrolyzation refers to a reaction wherein a peracid is generated from ester and hydrogen peroxide substrate.
• the perhydrolyzation reaction is catalyzed with a perhydrolase, e.g., acyl transferase or aryl esterase, enzyme.
• -OR 2 is -OH.
• -OR 2 is replaced by -NH 2 .
• a peracid is produced by perhydrolysis of a carboxylic acid or amide substrate.
• an "effective amount of perhydrolase enzyme” refers to the quantity of perhydrolase enzyme necessary to produce the decolorization effects described herein. Such effective amounts are determined by the skilled artisan in view of the present description, and are based on several factors, such as the particular enzyme variant used, the pH used, the temperature used, and the like, as well as the results desired ⁇ e.g., level of whiteness).
• peracid products are able to transfer one of their oxygen atoms to another molecule, such as a dye. It is this ability to transfer oxygen atoms that enables a peracid, for example, peracetic acid, to function as a bleaching agent.
• the ester source is an acetate ester. In some embodiments, the ester source is selected from one or more of propylene glycol diacetate, ethylene glycol diacetate, triacetin, ethyl acetate and tributyrin.
• the ester source is selected from the esters of one or more of the following acids: formic acid, acetic acid, propionic acid, butyric acid, valeric acid, caproic acid, caprylic acid, nonanoic acid, decanoic acid, dodecanoic acid, myristic acid, palmitic acid, stearic acid, and oleic acid.
• hydrogen peroxide source refers to a molecule capable of generating hydrogen peroxide, e.g., in situ.
• Hydrogen peroxide sources include hydrogen peroxide, itself, as well as molecules that spontaneously or enzymatically produce hydrogen peroxide as a reaction product. Such molecules include, e.g., perborate and percarbonate.
• perhydrolysis to hydrolysis ratio refers to the ratio of enzymatically produced peracid to enzymatically produced acid (e.g., in moles) that is produced by a perhydrolase enzyme from an ester substrate under defined conditions and within a defined time.
• the assays provided in WO 05/056782 are used to determine the amounts of peracid and acid produced by the enzyme.
• acyl refers to an organic group with the general formula RCO-, derived from an organic acid by removal of the -OH group.
• acyl group names end with the suffix "-oyl,” e.g., methanoyl chloride, CH 3 CO-Cl, is the acyl chloride formed from methanoic acid, CH 3 CO-OH).
• acylation refers to a chemical transformation in which one of the substituents of a molecule is substituted by an acyl group, or the process of introduction of an acyl group into a molecule.
• transferase refers to an enzyme that catalyzes the transfer of a functional group from one substrate to another substrate.
• an acyl transferase may transfer an acyl group from an ester substrate to a hydrogen peroxide substrate to form a peracid.
• hydrogen peroxide generating oxidase refers to an enzyme that catalyzes an oxidation/reduction reaction involving molecular oxygen (0 2 ) as the electron acceptor. In such a reaction, oxygen is reduced to water (H 2 0) or hydrogen peroxide (H 2 0 2 ).
• An oxidase suitable for use herein is an oxidase that generates hydrogen peroxide (as opposed to water) on its substrate.
• An example of a hydrogen peroxide generating oxidase and its substrate suitable for use herein is glucose oxidase and glucose.
• oxidase enzymes that may be used for generation of hydrogen peroxide include alcohol oxidase, ethylene glycol oxidase, glycerol oxidase, amino acid oxidase, etc.
• the hydrogen peroxide generating oxidase is a carbohydrate oxidase.
• the term "textile” refers to fibers, yarns, fabrics, garments, and non- wovens.
• the term encompasses textiles made from natural, synthetic (e.g., manufactured), and various natural and synthetic blends. Textiles may be unprocessed or processed fibers, yarns, woven or knit fabrics, non-wovens, and garments and may be made using a variety of materials, some of which are mentioned, herein.
• a "cellulosic" fiber, yarn or fabric is made at least in part from cellulose. Examples include cotton and non-cotton cellulosic fibers, yarns or fabrics. Cellulosic fibers may optionally include non-cellulosic fibers.
• a "non-cotton cellulosic" fiber, yarn or fabric is comprised primarily of a cellulose based composition other than cotton. Examples include linen, ramie, jute, flax, rayon, lyocell, cellulose acetate, bamboo and other similar compositions, which are derived from non- cotton cellulosics.
• non-cellulosic fiber, yarn or fabric is comprised primarily of a material other than cellulose. Examples include polyester, nylon, rayon, acetate, lyocell, and the like.
• the term "fabric” refers to a manufactured assembly of fibers and/or yarns that has substantial surface area in relation to its thickness and sufficient cohesion to give the assembly useful mechanical strength.
• coloring refers to applying a color, especially by soaking in a coloring solution, to, for example, textiles.
• dye refers to a colored substance (i.e. , chromophore) that has an affinity to a substrate to which it is applied. Numerous classes of dyes are described herein.
• color modification As used herein, the terms "color modification,” “color adjustment,” “modifying or adjusting the color,” or similar, are used to refer to any change to the color of a dyed textile resulting from the destruction, modification, or removal of a dye associated with the textile.
• the color modification is decolorization (see below). Examples of color modification include but are not limited to, bleaching, fading, imparting a grey cast, altering hue, saturation, or luminescence, and the like. The amount and type of color modification can be determined by comparing the color of a textile following enzymatic treatment with a
• perhydrolase enzyme i.e., residual color
• enzymatic treatment i.e. , original color
• decolorizing and “decolorization” refer to color elimination or reduction via the destruction, modification, or removal of dye, e.g. , from an aqueous medium.
• decolorizing or decolorization is defined as a percentage of color removal from aqueous medium.
• the amount of color removal can be determined by comparing the color of a textile following enzymatic treatment with a perhydrolase enzyme (i.e. , residual color) to the color of the textile prior to enzymatic treatment (i.e. , original color) using known spectrophotometric or visual inspection methods.
• Original color refers to the color of a dyed textile prior to enzymatic treatment. Original color may be measured using known spectrophotometric or 5 visual inspection methods.
• residual color refers to the color of a dyed textile prior to enzymatic treatment. Residual color may be measured using known spectrophotometric or visual inspection methods.
• size refers to compositions used in the o textile industry to improve weaving performance by increasing the abrasion resistance and/or strength of threads or yarns. Size is usually made of, for example, starch or starch-like material (i.e. , chemically-modified starch), polyvinyl alcohol (PVA), carboxymethyl cellulose (CMC), acrylates, and the like.
• starch or starch-like material i.e. , chemically-modified starch
• PVA polyvinyl alcohol
• CMC carboxymethyl cellulose
• acrylates and the like.
• desize or “desizing” refer to the process of removing or5 eliminating size from textiles, usually prior to applying special finishes, dyes or bleach.
• Desizing can be performed enzymatic ally, e.g. , using enzymes such as amylases and/or mannanases, or using caustic conditions.
• a "desizing enzyme” is an enzyme used to remove size.
• exemplary enzymes are amylases and mannanases.
• the expression “dyed prior to sizing,” refers to a fabric that has been dyed, completely or in part, or includes a component, such as a fiber or yarn, that has been dyed completely or in part, before the application of a sizing material to the fabric.
• a "cellulase” is an enzyme capable of hydrolyzing cellulose.
• the term "abrading” refers generally to contacting a textile comprising 5 cellulose fibers with one or more cellulases to produce an effect. Such effects include but are not limited to softening, smoothing, defuzzing, depilling, biopolishing, and/or intentionally distressing the textile, locally or in its entirety. In some cases, more than one abrading step may be desirable.
• an "aqueous medium” is a solution and/or suspension primarily
• the aqueous medium typically includes at least one dye to be decolorized, as well as any number of dissolved or suspended components, including but not limited to surfactants, salts, buffers, stabilizers, complexing agents, chelating agents, builders, metal ions, additional enzymes and substrates, and the like.
• exemplary aqueous media are textile dying solutions. Materials such as textile articles, textile fibers, and other solid materials may also be present in or in contact with the aqueous medium.
• contacting means bringing into physical contact, such as by incubating a subject item (e.g. , a textile) in the presence of an aqueous solution containing a reaction component (e.g. , an enzyme).
• a subject item e.g. , a textile
• a reaction component e.g. , an enzyme
• packaging refers to a container capable of providing a perhydrolase enzyme, substrate for the perhydrolase enzyme, and/or hydrogen peroxide source in an easy to handle and transport form.
• Exemplary packaging includes boxes, tubs, cans, barrels, drums, bags, or even tanker trucks.
• the terms “purified” and “isolated” refer to the removal of contaminants from a sample and/or to a material (e.g. , a protein, nucleic acid, cell, etc.) that is removed from at least one component with which it is naturally associated.
• a material e.g. , a protein, nucleic acid, cell, etc.
• these terms may refer to a material which is substantially or essentially free from components which normally accompany it as found in its native state, such as, for example, an intact biological system
• polynucleotide refers to a polymeric form of nucleotides of any length and any three-dimensional structure and single- or multi- stranded (e.g. , single- stranded, double-stranded, triple-helical, etc.), which contain deoxyribonucleotides,
• ribonucleotides and/or analogs or modified forms of deoxyribonucleotides or ribonucleotides, including modified nucleotides or bases or their analogs.
• polypeptide refers to any composition comprising amino acids linked by peptide bonds and recognized as a protein by those of skill in the art.
• the conventional one- letter or three-letter code for amino acid residues is used herein.
• polypeptide and protein are used interchangeably herein to refer to polymers of amino acids of any length.
• the polymer may be linear or branched, it may comprise modified amino acids, and it may be interrupted by non-amino acids.
• the terms also encompass an amino acid polymer that has been modified naturally or by intervention; for example, disulfide bond formation, glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation or modification, such as conjugation with a labeling component.
• polypeptides containing one or more analogs of an amino acid including, for example, unnatural amino acids, etc.
• proteins are considered to be "related proteins.”
• these proteins are derived from a different genus and/or species, including differences between classes of organisms (e.g. , a bacterial protein and a fungal protein).
• related proteins are provided from the same species. Indeed, it is not intended that the processes, methods and/or compositions described herein be limited to related proteins from any particular source(s).
• the term "related proteins” encompasses tertiary structural homologs and primary sequence homologs. In further embodiments, the term encompasses proteins that are immunologically cross-reactive.
• the term "derivative" refers to a protein which is derived from a protein by addition of one or more amino acids to either or both the C- and N-terminal end(s), substitution of one or more amino acids at one or a number of different sites in the amino acid sequence, and/or deletion of one or more amino acids at either or both ends of the protein or at one or more sites in the amino acid sequence, and/or insertion of one or more amino acids at one or more sites in the amino acid sequence.
• the preparation of a protein derivative is preferably achieved by modifying a DNA sequence which encodes for the native protein, transformation of that DNA sequence into a suitable host, and expression of the modified DNA sequence to form the derivative protein.
• variant proteins differ from a parent protein, e.g. , a wild-type protein, and one another by a small number of amino acid residues.
• the number of differing amino acid residues may be one or more, for example, 1, 2, 3, 4, 5, 10, 15, 20, 30, 40, 50, or more amino acid residues.
• related proteins and particularly variant proteins comprise at least 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or even 99% or more amino acid sequence identity.
• a related protein or a variant protein refers to a protein that differs from another related protein or a parent protein in the number of prominent regions.
• variant proteins have 1, 2, 3, 4, 5, or 10 corresponding prominent regions that differ from the parent protein.
• Prominent regions include structural features, conserved regions, epitopes, domains, motifs, and the like.
• analogous sequence refers to a sequence within a protein that provides similar function, tertiary structure, and/or conserved residues as the protein of interest (i.e., typically the original protein of interest). For example, in epitope regions that contain an alpha-helix or a beta-sheet structure, the replacement amino acids in the analogous sequence preferably maintain the same specific structure.
• the term also refers to nucleotide sequences, as well as amino acid sequences. In some embodiments, analogous sequences are developed such that the replacement amino acids result in a variant enzyme showing a similar or improved function.
• the tertiary structure and/or conserved residues of the amino 5 acids in the protein of interest are located at or near the segment or fragment of interest.
• the replacement amino acids preferably maintain that specific structure.
• homologous protein refers to a protein that has similar activity and/or structure to a reference protein. It is not intended that homologs necessarily be o evolutionarily related. Thus, it is intended that the term encompass the same, similar, or
• homologous proteins induce similar immunological response(s) as a reference protein.
• homologous proteins are engineered to produce enzymes with desired
• the degree of homology between sequences may be determined using any suitable method known in the art (see, e.g., Smith and Waterman (1981) Adv. Appl. Math. 2:482;
• PILEUP is a useful program to determine sequence homology levels. PILEUP creates a multiple sequence alignment from a group of related sequences using
• PILEUP uses a simplification of the progressive alignment method of Feng and Doolittle, (Feng and Doolittle (1987) J. Mol. Evol. 35:351-360). The method is similar to that described by Higgins and Sharp (Higgins and Sharp (1989) CABIOS 5: 151-153).
• Useful PILEUP parameters including a default gap weight of 3.00, a default gap length weight 0 of 0.10, and weighted end gaps.
• Another example of a useful algorithm is the BLAST
• BLAST program is the WU-BLAST-2 program (See, Altschul et al. (1996) Meth. Enzymol. 266:460- 480). Parameters "W,” "T,” and "X” determine the sensitivity and speed of the alignment.
• the BLAST program uses as defaults a word- length (W) of 11, the BLOSUM62 scoring matrix (See, Henikoff and Henikoff (1989) Proc. Natl. Acad. Sci. USA 89: 10915) alignments (B) of 50, expectation (E) of 10, M'5, N'-4, and a comparison of both strands.
• sequence identity 99% sequence identity, compared to the reference (i.e., wild-type) sequence. Sequence identity may be determined using known programs such as BLAST, ALIGN, and CLUSTAL using standard parameters. (See e.g., Altschul, et al. (1990) J. Mol. Biol. 215:403-410; Henikoff et al. (1989) Proc. Natl. Acad. Sci. USA 89: 10915; Karin et al. (1993) Proc. Natl. Acad. Sci USA
• polypeptides that differ by conservative amino acid substitutions are immunologically cross- reactive.
• a polypeptide is substantially identical to a second polypeptide, for example, where the two peptides differ only by a conservative substitution.
• Another indication that two nucleic acid sequences are substantially identical is that the two molecules hybridize to each other under stringent conditions (e.g., within a range of medium to high stringency).
• wild-type and “native” proteins are those found in nature.
• wild-type sequence and “wild-type gene” are used interchangeably herein, to refer to a sequence that is native or naturally occurring in a host cell.
• the wild-type sequence refers to a sequence of interest that is the starting point of a protein engineering project.
• the genes encoding the naturally-occurring protein may be obtained in accord with the 0 general methods known to those skilled in the art. The methods generally comprise synthesizing labeled probes having putative sequences encoding regions of the protein of interest, preparing genomic libraries from organisms expressing the protein, and screening the libraries for the gene of interest by hybridization to the probes. Positively hybridizing clones are then mapped and sequenced. [62] As used herein, the singular articles “a,” “an,” and “the” encompass the plural referents unless the context clearly dictates otherwise. All references sited herein are hereby incorporated by reference in their entirety.
• the present methods relate to the enzymatic color-modification of textile materials using an enzymatic perhydrolase system, wherein the textile is sized prior to color-modification. Such methods eliminate the need to desize the textile prior to color modification.
• the textile is color-modified in the absence of desizing, either before or after color-modification.
• the textile is color-modified prior to desizing.
• the process of color- modification using the perhydrolase system may remove at least a portion of the size. The ability to color modify a sized textile saves a step in processing, and/or provides textile
• the present methods can be applied to a fabric sized with any sizing material that can be removed using a conventional oxidative desizing step, e.g., using a desizing agent such as potassium persulfate, sodium persulfate, sodium bromite, permanganate, and the like.
• a desizing agent such as potassium persulfate, sodium persulfate, sodium bromite, permanganate, and the like.
• the present methods eliminate the o need to desize the textile by contacting it with an oxidizing agent prior to color modification.
• the textile is color-modified without contacting it with an oxidizing agent, either before or after color-modification.
• the textile is color-modified prior to contacting it with an oxidizing agent.
• the process of color-modification using the perhydrolase system may remove at least a portion of the sizing material.
• the present methods eliminate the need to desize the textile by contacting it with an amylase enzyme prior to color modification.
• the textile is color-modified without contacting it with an amylase enzyme, either before or after color-modification.
• the textile is color-modified prior to contacting it with an amylase enzyme.
• the process of o color-modification using the perhydrolase system may remove at least a portion of the starch, or starch-like sizing material.
• the present methods are particularly useful when applied to fabrics that are sized following dyeing, or include at least some fibers or yarns that are dyed prior to sizing.
• An exemplary fabric is denim, which is formed by weaving dyed weft fibers with non-dyed warp 5 fibers. These fibers are sized prior to weaving, and the resulting denim fabric is conventionally desized prior to enzymatic or chemical color modification.
• the present compositions and methods allow the direct color-modification of denim, in the absence of, or prior to, desizing.
• the methods are useful for color modifying fabrics dyed with a number of different dyes, including but not limited to sulphur-based dyes (such as sulphur black) and indigo dyes.
• the extent of color modification resulting from the present methods may be similar to that achieved using a conventional color-modification process, in which the fabric is desized prior to color modification. In other cases, the extent of color modification resulting from the present methods may be less than that achieved using a conventional color-modification process, but may nonetheless be sufficient to produce a desired effect, while offering the advantage of not having to desize the fabric prior to treatment. For example, the extent of color modification resulting from the present methods may be about 95%, about 90%, about 85%, about 80%, about 75%, or even about 70% or less of the amount of color modification achieved using a
• a feature of the present methods is the use of a perhydolase enzyme system, comprising a perhydrolase enzyme capable of generating peracids in the present of a suitable ester substrate o and hydrogen peroxide source.
• the perhydrolase enzyme is naturally-occurring enzyme.
• the perhydrolase enzyme comprises, consists of, or consists essentially of an amino acid sequence that is at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5% identical to the amino acid sequence of a naturally-5 occurring perhydrolase enzyme.
• the perhydrolase enzyme is from a
• microbial source such as a bacterium or fungus.
• the perhydrolase enzyme is a naturally occurring Mycobacterium smegmatis perhydrolase enzyme or a variant thereof. This enzyme, its enzymatic properties, its structure, and numerous variants and homologs, thereof, are described in detail in International o Patent Application Publications WO 05/056782A and WO 08/063400 A, and U.S . Patent
• the perhydrolase enzyme has a perhydrolysis:hydrolysis ratio of at least 1. In some embodiments, the perhydrolase enzyme has a perhydrolysis:hydrolysis ratio greater than 1. In some embodiments, the perhydrolysis:hydrolysis ratio is greater than 1.5, 5 greater than 2.0, greater than 2.5, or even greater than 3.0. These high perhydrolysis:hydrolysis ratios are features unique to of M. smegmatis perhydrolase and variants, thereof.
• a perhydrolase enzyme comprises, consists of, or consists essentially of the amino acid sequence set forth in SEQ ID NO: 1 or a variant or homologue thereof.
• the perhydrolase enzyme comprises, consists of, or consists essentially of an amino acid sequence that is at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5% identical to the amino acid sequence set forth in SEQ ID NO: 1.
• the perhydrolase enzyme comprises one or more substitutions at one or more amino acid positions equivalent to position(s) in the M. smegmatis perhydrolase amino acid 5 sequence set forth in SEQ ID NO: 1.
• the perhydrolase enzyme comprises any one or any combination of substitutions of amino acids selected from Ml, K3, R4, 15, L6, C7, D10, Sl l, L12, T13, W14, W16, G15, V17, P18, V19, D21, G22, A23, P24, T25, E26, R27, F28, A29, P30, D31, V32, R33, W34, T35, G36, L38, Q40, Q41, D45, L42, G43, A44, F46, E47, V48, 149, E50, E51, G52, L53, S54, A55, R56, T57, T58, N59, 160, D61, D62, P63, T64,
• the perhydrolase enzyme comprises one or more of the following
• the perhydrolase enzyme comprises a combination of amino acid 2 o substitutions at amino acid positions equivalent to amino acid positions in the M. smegmatis perhydrolase amino acid sequence set forth in SEQ ID NO: 1: L12I S54V; L12M S54T; L12T S54V; L12Q T25S S54V; L53H S54V; S54P V125R; S54V V125G; S54V F196G; S54V K97R V125G; or A55G R67T K97R V125G.
• the perhydrolase enzyme is the S54V variant of the M.
• the perhydrolase enzyme includes the S54V substitution but is otherwise at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5% identical to the amino acid sequence set forth in SEQ ID NOs: 1 or 2.
• the perhydrolase enzyme is provided at a concentration of about 1 to about 100 ppm, or more.
• the perhydrolase enzyme is provided at a molar ratio with respect to the amount of dye on the textile. In some embodiments, the molar ratio is from about 1/10,000 to about 1/10, or even from about 1/5,000 to about 1/100.
• the concentration of perhydrolase enzyme is from about 10 "9 M to about 10 "5 M, from about 10 "8 M to about 10 "5 M, from about 10 "8 M to about 10 "6 M, about 5 x 10 "8 M to
• the amount of perhydrolase enzyme is below a predetermined amount to improve the efficiency of color modification.
• the perhydrolase enzyme system may include at least one ester molecule that serves as a substrate for the perhydrolase enzyme for production of a peracid in the presence of hydrogen peroxide.
• the ester substrate is an ester of an aliphatic and/or aromatic carboxylic acid or alcohol.
• the ester substrate may be a mono-, di-, or multivalent ester, or a mixture thereof.
• the ester substrate may be a carboxylic acid and a single alcohol (monovalent, e.g. , ethyl acetate, propyl acetate), two carboxylic acids and a diol [e.g.
• propylene glycol diacetate PGDA
• ethylene glycol diacetate EGDA
• a mixture for example, 2- acetyloxy 1 -propionate, where propylene glycol has an acetate ester on alcohol group 2 and a propyl ester on alcohol group 1]
• three carboxylic acids and a triol e.g. , glycerol triacetate or a mixture of acetate/propionate, etc., attached to glycerol or another multivalent alcohol.
• the ester substrate is an ester of a nitroalcohol (e.g. , 2-nitro- l- propanol).
• the ester substrate is a polymeric ester, for example, a partially acylated (acetylated, propionylated, etc.) poly carboxy alcohol, acetylated starch, etc.
• the ester substrate is an ester of one or more of the following: formic acid, acetic acid, propionic acid, butyric acid, valeric acid, caproic acid, caprylic acid, nonanoic acid, decanoic acid, dodecanoic acid, myristic acid, palmitic acid, stearic acid, and oleic acid.
• triacetin, tributyrin, and other esters serve as acyl donors for peracid formation.
• the ester substrate is propylene glycol diacetate, ethylene glycol diacetate, or ethyl acetate. In one embodiment, the ester substrate is propylene glycol diacetate.
• suitable substrates may be monovalent (i.e. , comprising a single carboxylic acid ester moiety) or plurivalent (i.e. , comprising more than one carboxylic acid ester moiety).
• the amount of substrate used for color modification may be adjusted depending on the number carboxylic acid ester moieties in the substrate molecule.
• the concentration of carboxylic acid ester moieties in the aqueous medium is about 20-500 mM, for example, about 40 mM to about 400 mM, about 40 mM to about 200 mM, or even about 60 mM to about 200 mM.
• Exemplary concentrations of carboxylic acid ester moieties include about 60 mM, about 80 mM, about 100 mM, about 120 mM, about 140 mM, about 160 mM, about 180 mM, and about 200 mM.
• ester substrate is divalent (as in the case of PGDA) it is provided in an amount of about 10-200 mM, for example, about 20 mM to about 200 mM, about 20 mM to about 100 mM, or even about 30 mM to about 100 mM.
• Exemplary amounts of ester substrate include about 30 mM, about 40 mM, about 50 mM, about 60 mM, about 70 mM, about 80 mM, about 90 mM, and about 100 mM.
• the skilled person can readily calculate the corresponding amounts of trivalent, or other plurivalent ester substrates based on the number of carboxylic acid esters moieties per molecule.
• the ester substrate is provided in a molar excess with respect to the molar amount of dye on the textile to be subjected to color modification.
• the carboxylic acid ester moieties of the ester substrate are provided at about 20 to about 20,000 times the molar amount of dye.
• Exemplary molar ratios of carboxylic acid ester moieties to dye molecules are from about 100/1 to about 10,000/1, from about 1,000/1 to about 10,000/1, or even 2,000/1 to about 6,000/1. In some cases, the molar ratio of ester substrate to dye molecules is at least 2,000/1, or at least 6,000/1.
• ester substrate is divalent (as in the case of PGDA) the ester substrate is provided at about 10 to about 10,000 times the molar amount of dye.
• Exemplary molar ratios of ester substrate to dye molecules are from about 50/1 to about 5,000/1, from about 500/1 to about 5,000/1, or even 1,000/1 to about 3,000/1. In some cases, the molar ratio of ester substrate to dye molecules is at least 1,000/1, or at least 3,000/1. As before, the skilled person can readily calculate the corresponding amounts of trivalent, or other plurivalent ester substrates based on the number of carboxylic acid esters moieties per molecule.
• the ester substrate is provided at a concentration of about 100 ppm to about 100,000 ppm, ppm, or about 2500 to about 3500 ppm. In some embodiments, the ester substrate is provided in a molar excess with respect to the perhydrolase enzyme. In some embodiments, the molar ratio of carboxylic acid ester moieties to perhydrolase enzyme is at least about 2 x 10 5 /1, at least about 4 x 10 5 /1, at least about 1 x 10 6 /1, at least about 2 x 10 6 /1, at least about 4 x 10 6 /1, or even at least about 1 x 10 7 /1, or more.
• the ester substrate is provided in a molar excess of from about 4 x 10 5 /1, to about 4 x 10 6 /1, with respect to the perhydrolase enzyme.
• the ester substrate is divalent (as in the case of PGDA)
• the molar ratio of ester substrate to perhydrolase enzyme is at least about 1 x 10 5 /1, at least about 2 x 10 5 /1, at least about 5 x 10 5 /1, at least about 1 x 10 6 /1, at least about 2 x 10 6 /1, or even at least about 5 x 10 6 /1, or more.
• the ester substrate is provided in a molar excess of from about 2 x 10 5 /1 to about 2 x 10 6 /1, with respect to the perhydrolase enzyme.
• the skilled person can readily calculate the corresponding amounts of trivalent, or other plurivalent ester substrates based on the number of carboxylic acid esters moieties per molecule.
• the perhydrolase enzyme system further includes at least one hydrogen peroxide source.
• hydrogen peroxide can be provided directly (i.e., in batch), or generated continuously (i.e., in situ) by chemical, electro-chemical, and/or enzymatic means.
• the hydrogen peroxide source is hydrogen peroxide, itself.
• the hydrogen peroxide source is a compound that generates hydrogen peroxide upon addition to water.
• the compound may be a solid compound.
• Such compounds include adducts of hydrogen peroxide with various inorganic or organic compounds, of which the most widely employed is sodium carbonate per hydrate, also referred to as sodium
• the hydrogen peroxide source is an inorganic perhydrate salt.
• inorganic perhydrate salts are perborate, percarbonate, perphosphate, persulfate and persilicate salts.
• Inorganic perhydrate salts are normally alkali metal salts.
• Additional hydrogen peroxide sources include adducts of hydrogen peroxide with zeolites, or urea hydrogen peroxide.
• the hydrogen peroxide source may be in a crystalline form and/or substantially pure solid form without additional protection.
• preferred forms are granular compositions involving a coating, which provides better storage stability for the perhydrate salt in the granular product.
• Suitable coatings comprise inorganic salts such as alkali metal silicate, carbonate or borate salts or mixtures thereof, or organic materials such as waxes, oils, or fatty soaps.
• the hydrogen peroxide source is an enzymatic hydrogen peroxide generation system.
• the enzymatic hydrogen peroxide generation system comprises an oxidase and its substrate.
• Suitable oxidase enzymes include, but are not limited to: glucose oxidase, sorbitol oxidase, hexose oxidase, choline oxidase, alcohol oxidase, glycerol oxidase, cholesterol oxidase, pyranose oxidase, carboxyalcohol oxidase, L-amino acid oxidase, glycine oxidase, pyruvate oxidase, glutamate oxidase, sarcosine oxidase, lysine oxidase, lactate oxidase, vanillyl oxidase, glycolate oxidase, galactose oxidase
• H 2 0 2 + ester substrate alcohol + peracid It is not intended that the generation of H 2 0 2 be limited to any specific enzyme, as any enzyme that generates H 2 0 2 with a suitable substrate may be used.
• any enzyme that generates H 2 0 2 with a suitable substrate may be used.
• lactate oxidases from Lactobacillus species known to create H 2 0 2 from lactic acid and oxygen may be used.
• acid e.g., gluconic acid in the above example
• Such a reduction in pH is also brought about directly by the production of peracid.
• enzymes e.g., alcohol oxidase, ethylene glycol oxidase, glycerol oxidase, amino acid oxidase, etc.
• ester substrates in combination with a perhydrolase enzyme to generate peracids.
• hydrogen peroxide is generated electrochemically, it may be produced, for example, using a fuel cell supplied with oxygen and hydrogen gas.
• hydrogen peroxide is provided at a concentration of about 100 ppm to about 10,000 ppm, about 1,000 ppm to about 3,000 ppm, or about 1,500 to about 2,500 ppm. In some embodiments, hydrogen peroxide is provided at about 10 to about 1,000 times the molar amount of dye.
• hydrogen peroxide is provided in an amount of about 10-200 mM, for example, about 20 mM to about 200 mM, about 20 mM to about 100 mM, or even about 30 mM to about 100 mM.
• Exemplary amounts of hydrogen peroxide include about 30 mM, about 40 mM, about 50 mM, about 60 mM, about 70 mM, about 80 mM, about 90 mM, and about 100 mM.
• hydrogen peroxide is provided in a molar excess with respect to the molar amount of dye to be subjected to color modification. In some embodiments, the hydrogen peroxide is provided at about 10 to about 10,000 times the molar amount of dye. Exemplary molar ratios of hydrogen peroxide to dye molecules are from about 500/1 to about 5,000/1, or even 1,000/1 to about 3,000/1. In some cases, the molar ratio of hydrogen peroxide to dye molecules is at least 1,000/1, or at least 3,000/1.
• the hydrogen peroxide is provided in a molar excess with respect to the perhydrolase enzyme.
• the molar ratio of hydrogen peroxide to 5 perhydrolase enzyme is at least about 1 x 10 5 /1, at least about 2 x 10 5 /1, at least about 5 x 10 5 /1, at least about 1 x 10 6 /1, at least about 2 x 10 6 /1, or even at least about 5 x 10 6 / 1 , or more.
• the hydrogen peroxide is provided in a molar excess of about 2 x 10 5 /1 to 2 x 10 6 /1, with respect to the perhydrolase enzyme.
• catalase it may in some circumstances be desirable to add catalase to the textile bath to destroy o residual hydrogen peroxide. In such cases, catalase can be added directly to the bath, without prior rinsing of the textiles.
• a method for modifying the color of a dyed, sized textile comprising, contacting the dyed, sized textile with a perhydrolase enzyme system to modify the color of the textile, wherein the contacting is performed without first desizing the textile.
• the method of the preceding paragraph is performed in the absence of desizing the textile.
• the method of paragraph 1 is performed prior to desizing the o textile.
• the perhydrolase enzyme system used to perform the method of any of the preceding paragraphs comprises a perhydrolase enzyme and an ester substrate, wherein the perhydrolase enzyme catalyzes perhydrolysis of the ester substrate with a perhydrolysis:hydrolysis ratio equal to or greater than 1.
• perhydrolase enzyme system comprises a Mycobacterium perhydrolase or a variant, thereof, for example, a Mycobacterium smegmatis perhydrolase.
• the perhydrolase enzyme is a variant of Mycobacterium smegmatis perhydrolase comprising the 0 amino acid substitution S54V.
• the ester substrate is PGDA or triacetin.
• the size comprises starch, a starch-like material, or PVA.
• the textile is denim.
• the textile comprises cotton.
• the dye is a sulphur dye.
• Example 1 Color adjustment of sulphur-dyed, sized denim, using a perhydrolase system with a PGDA substrate

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• Enzymes And Modification Thereof (AREA)
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• Chemical Or Physical Treatment Of Fibers (AREA)

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• 2012
  • 2012-03-14 AR ARP120100834A patent/AR085810A1/es unknown
  • 2012-03-14 EP EP12711727.3A patent/EP2686477A1/de not_active Withdrawn
  • 2012-03-14 WO PCT/US2012/029009 patent/WO2012125685A1/en active Application Filing
  • 2012-03-14 CN CN2012800137709A patent/CN103476985A/zh active Pending
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