LOCAL COLOR MODIFICATION OF DYED FABRICS USING A LACCASE SYSTEM

Abstract

The present systems, compositions, and methods relate to local color modification of dyed fabrics using a laccase enzyme system.

Description

PRIORITY

[0001] The present application claims priority to U.S. Provisional Patent Application Ser. No. 61/394,312, filed on Oct. 18, 2010, which is hereby incorporated by reference in its entirety.

TECHNICAL FIELD

[0002] The present systems, compositions, and methods relate to local color modification of dyed fabrics using a laccase enzyme system.

BACKGROUND

[0003] Laccases are copper-containing phenol oxidizing enzymes that are known to be good oxidizing agents in the presence of oxygen. Laccases are found in microbes, fungi, and higher organisms. Laccase enzymes are used for many applications, including pulp and paper bleaching, treatment of pulp waste water, de-inking, industrial color removal, bleaching in laundry detergents, oral care teeth whiteners, as catalysts or facilitators for polymerization and oxidation reactions, in the textiles industry, and in the food industry.

[0004] Laccases are known to be produced by a wide variety of fungi, including species of the genii Aspergillus, Neurospora, Podospora, Botrytis, Pleurotus, Fornes, Phlebia, Trametes, Polyporus, Stachybotrys, Rhizoctonia, Bipolaris, Curvularia, Amerosporium, Lentinus, Myceliophtora, Coprinus, Thielavia, Cerrena, Streptomyces, and Melanocarpus. For many applications, the oxidizing efficiency of a laccase can be improved through the use of a mediator, also known as an enhancing agent.

SUMMARY

[0005] Described are systems, compositions, and methods relating to local color modification of dyed fabrics using a laccase enzyme system. In one aspect, a textile processing method is provided, comprising contacting a portion of dyed textile with a laccase enzyme system for a length of time and under conditions sufficient to cause a localized color modification to the portion of the textile.

[0006] In some embodiments, the method is performed by wetting but not submerging the portion of the dyed textile with a composition comprising the laccase enzyme system. In some embodiments, the method is performed by applying a composition comprising the laccase enzyme system to the portion of the dyed textile, and then wetting but not submerging the portion of the dyed textile.

[0007] In some embodiments, the laccase enzyme system is provided in a single composition. In some embodiments, the laccase enzyme system is provided as an aqueous, gel, semi-solid, or solid formulation.

[0008] In some embodiments, the color modification is selected from lightening of color, change of color, change in color cast, and bleaching.

[0009] In some embodiments, the textile is indigo-dyed denim In some embodiments, the textile is indigo and sulfur-dyed denim.

[0010] In some embodiments, the textile is a pair of jeans. In some embodiments, the portion of the textile is a pant leg, sleeve, cuff, collar, pocket, or belt loop. In some embodiments, the portion of the textile is in the form of a predetermined shape. In some embodiments, the portion of the textile is in the form of a letter, word, logo, or trademark.

[0011] In some embodiments, the laccase enzyme system comprises a laccase enzyme and a mediator. In some embodiments, the laccase is a microbial laccase. In some embodiments, the laccase is from a Cerrena species. In some embodiments, the laccase is from Cerrena unicolor. In some embodiments, the laccase is laccase D from C. unicolor. In some embodiments, the mediator is syringonitrile.

[0012] In some embodiments, the method is performed at a temperature of from about 20° C. to about 40° C. In some embodiments, the method is performed at a temperature of from about 20° C. to about 30° C. In some embodiments, the method is performed at the ambient temperature of tap water. In some embodiments, the method is performed at ambient air temperature.

[0013] In another aspect, a locally color-modified dyed textile produced by any of these methods is provided.

[0014] These and other aspects and embodiments of the present system, compositions, and methods will be apparent from the description and accompanying figures.

BRIEF DESCRIPTION OF THE FIGURES

[0015] FIG. 1 is an image of indigo-dyed jeans that were subjected to localized color modification in the shape of a heart.

DETAILED DESCRIPTION

[0016] Described are systems, compositions, and methods relating to local color modification of dyed fabrics using laccase enzymes and associated reagents. The systems, compositions, and methods are useful, for example, for processing textiles to affect local color modification on fabrics and garments, including complete, consumer-ready garments. Various aspects and embodiments of the systems, compositions, and methods are to be described.

Definitions

[0017] Unless defined otherwise herein, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art. Singleton et al., DICTIONARY OF MICROBIOLOGY AND MOLECULAR BIOLOGY, 2D ED., John Wiley and Sons, New York (1994), and Hale and Marham, THE HARPER COLLINS DICTIONARY OF BIOLOGY, Harper Perennial, N.Y. (1991) provide a general dictionary of many of the terms used herein. The following terms are defined for additional clarity.

[0018] As used herein, the term "enzyme" refers to a protein that catalyzes a chemical reaction. The catalytic function of an enzyme constitutes its "enzymatic activity" or "activity." An enzyme is typically classified according to the type of reaction it catalyzes, e.g., oxidation of phenols, hydrolysis of peptide bonds, incorporation of nucleotides, etc.

[0019] As used herein, the term "substrate" refers to a substance (e.g., a chemical compound) on which an enzyme performs its catalytic activity to generate a product.

[0020] As used herein, a "laccase" is a multi-copper containing oxidase (EC 1.10.3.2) that catalyzes the oxidation of phenols, polyphenols, and anilines by single-electron abstraction, with the concomitant reduction of oxygen to water in a four-electron transfer process.

[0021] As used herein, "laccase activity" is measured in units/gram (U/g), wherein one unit is defined as the amount of laccase activity required to oxidize 1 nmol of 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate; ABTS) substrate per second under conditions of an assay based on the ability of laccase enzyme to oxidize ABTS into its corresponding stable cation radical, i.e., ABTS⁺. Unlike the initial form of ABST, the radical form is dark green in color with increased absorbance at 420 nm. The amount of green color formation is proportional to the amount of laccase activity, and can be compared to a laccase standard curve to determine the absolute amount of laccase activity.

[0022] As used herein, "variant" proteins encompass related and derivative proteins that differ from a parent/reference protein by a small number of amino acid substitutions, insertions, and/or deletions. In some embodiments, the number of different amino acid residues is any of about 1, 2, 3, 4, 5, 10, 20, 25, 30, 35, 40, 45, or 50. In some embodiments, variants differ by about 1 to about 10 amino acids residues. In some embodiments, variant proteins have at least about 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5% amino acid sequence identity to a parent/reference protein.

[0023] As used herein, the term "analogous sequence" refers to a polypeptide sequence within a protein that provides a similar function, tertiary structure, and/or conserved residues with respect to a sequence within a parent/reference protein. For example, in structural regions that contain an alpha helix or a beta sheet structure, replacement amino acid residues in an analogous sequence maintain the same structural feature. In some embodiments, analogous sequences result in a variant protein that exhibits a similar or improved function with respect to the parent protein from which the variant is derived.

[0024] As used herein, a "homologous protein" or "homolog" refers to a protein (e.g., a laccase enzyme) that has a similar function (e.g., enzymatic activity) and/or structure as a reference protein (e.g., a laccase enzyme from a different source). Homologs may be from evolutionarily related or unrelated species. In some embodiments, a homolog has a quaternary, tertiary and/or primary structure similar to that of a reference protein, thereby potentially allowing for replacement of a segment or fragment in the reference protein with an analogous segment or fragment from the homolog, with reduced disruptiveness of structure and/or function of the reference protein in comparison with replacement of the segment or fragment with a sequence from a non-homologous protein.

[0025] As used herein, "wild-type," "native," and "naturally-occurring" proteins are those found in nature. The terms "wild-type sequence" refers to an amino acid or nucleic acid sequence that is found in nature or naturally occurring. In some embodiments, a wild-type sequence is the starting point of a protein engineering project, for example, production of variant proteins.

[0026] As used herein, a "signal sequence" refers to a sequence of amino acids bound to the N-terminal portion of a protein, and which facilitates the secretion of the mature form of the protein from the cell. The mature form of the extracellular protein lacks the signal sequence which is cleaved off during the secretion process.

[0027] As used herein, the term "derivative" refers to a protein that is derived from a parent/reference protein by addition of one or more amino acids to either or both the N- and C-terminal end(s), substitution of one or more amino acid residues at one or a number of different sites in the amino acid sequence, deletion of one or more amino acid residues 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 often 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.

[0028] As used herein, the terms "polypeptide, "protein," and "peptide," refer to a composition comprised of amino acids (i.e., amino acid residues). The conventional one-letter or three-letter codes for amino acid residues are used. A polypeptide may be linear or branched, may comprise modified amino acids, and 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. Also included within the definition are, for example, polypeptides containing one or more analogs of an amino acid (including, for example, unnatural amino acids, etc.), as well as other modifications known in the art.

[0029] As used herein, the term "textile" refers to fibers, yams, fabrics, garments, and non-woven materials. The term encompasses textiles made from natural and synthetic (e.g., manufactured) materials, as well as natural and synthetic blends. The term "textile" refers to both unprocessed and processed fibers, yarns, woven or knit fabrics, non-wovens, and garments. In some embodiments, a textile contains cellulose.

[0030] As used herein, 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.

[0031] As used herein, the term "garment" refers to a clothing item made from one or more fabrics. Garments typically include fabrics that are already cut to size and sewn or stitched together. Garments may or may not include buttons, eyelets, straps, zippers, hook-and-loop closures, and the like, which can be attached before or after localized color modification.

[0032] As used herein, the term "color modification" refers to a change in the chroma, saturation, intensity, luminance, and/or tint of a color associated with a fiber, yarn, fabric, garment, or non-woven material, collectively referred to as textile materials. Color modification encompasses chemical modification to a chromophore as well as chemical modification to the material to which a chromophore is attached. Examples of color modification include fading, bleaching, and altering tint. A particular color modification to indigo-dyed denim is fading to a "vintage look," which has a less intense blue/violet tint and more subdued grey appearance than the freshly-dyed denim.

[0033] As used herein, the term "local color modification" refers to color modification, as defined, above, that is performed on only a portion of a fabric or garment. Unlike generalized textile color modification, which is typically performed in a bath, i.e., in a submerged environment, local color modification is performed using a wetted but not submerged fabric or garment, typically on a table, work bench, or other hard surface, on a hanging or otherwise suspended fabric or garment, or using rollers or other processing equipment that do not subject the fabric or garment to a submerged environment, such that only a portion of the garment can be subjected to color modification without affecting the remainder of the fabric or garment.

[0034] As used herein, "a portion of a fabric or garment" refers to anything less than the whole fabric or garment. Where specified, a portion of a fabric or garment may refer to an indicated structural or decorative feature a fabric or garment, such as a pant leg, a sleeve, a pocket, a belt loop, a cuff, a hem, and the like.

[0035] As used herein, the term "bleaching" refers to the process of treating a textile material such as a fiber, yarn, fabric, garment or non-woven material to produce a lighter color. This term includes the production of a brighter and/or whiter textile, e.g., in the context of a textile processing application, as well as lightening of the color of a stain, e.g., in the context of a cleaning application.

[0036] As used herein, the terms "size" and "sizing" refer to compounds used in the textile industry to improve weaving performance by increasing the abrasion resistance and strength of a yarn. Size is usually made of starch or starch-like compounds.

[0037] As used herein, the terms "desize" and "desizing" refer to the process of eliminating/removing size (generally starch) from a textile, usually prior to applying special finishes, dyes or bleaches.

[0038] As used herein, the term "desizing enzyme" refers to an enzyme used to remove size. Exemplary enzymes are amylases, cellulases, and mannanases.

[0039] l As used herein, the term "% identity" refers to the level of nucleic acid sequence identity between a nucleic acid sequence that encodes a laccase as described herein and another nucleic acid sequence, or the level of amino acid sequence identity between a laccase enzyme as described herein and another amino aid sequence. Alignments may be performed using a conventional sequence alignment program. Exemplary levels of nucleic acid and amino acid sequence identity include, but are not limited to, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or even at least 99%, or more, sequence identity to a given sequence, e.g., the coding sequence for a laccase or the amino acid sequence of a laccase, as described herein.

[0040] Exemplary computer programs that can be used to determine identity between two sequences include, but are not limited to, the suite of BLAST programs, e.g., BLASTN, BLASTX, and TBLASTX, BLASTP and TBLASTN, publicly available on the Internet at www.ncbi.nlm.nih.gov/BLAST. See also, Altschul, et al., 1990 and Altschul, et al., 1997.

[0041] Sequence searches are typically carried out using the BLASTN program when evaluating a given nucleic acid sequence relative to nucleic acid sequences in the GenBank DNA Sequences and other public databases. The BLASTX program is preferred for searching nucleic acid sequences that have been translated in all reading frames against amino acid sequences in the GenBank Protein Sequences and other public databases. Both BLASTN and BLASTX are run using default parameters of an open gap penalty of 11.0, and an extended gap penalty of 1.0, and utilize the BLOSUM-62 matrix. (See, e.g., Altschul, et al., 1997.)

[0042] An alignment of selected sequences in order to determine "% identity" between two or more sequences, may be performed using, for example, the CLUSTAL-W program in Mac Vector version 6.5, operated with default parameters, including an open gap penalty of 10.0, an extended gap penalty of 0.1, and a BLOSUM 30 similarity matrix.

[0043] As used herein, the terms "chemical mediator" and "mediator" are used interchangeably to refer to a chemical compound that functions as a redox mediator to shuttle electrons between an enzyme exhibiting oxidase activity (e.g., a laccase) and a secondary substrate or electron donor. Such chemical mediators are also known in the art as "enhancers" and "accelerators."

[0044] As used herein, the terms "secondary substrate" and "electron donor" are used interchangeably to refer to a dye, pigment (e.g., indigo), chromophore (e.g., polyphenolic, anthocyanin, or carotenoid), or other secondary substrate to and from which electrons can be shuttled by an enzyme exhibiting oxidase activity.

[0045] The following abbreviations/acronyms have the following meanings unless otherwise specified:

[0046] EC enzyme commission

[0047] EDTA ethylenediaminetetraacetic acid

[0048] kDa kiloDalton

[0049] MW molecular weight

[0050] w/v weight/volume

[0051] w/w weight/weight

[0052] v/v volume/volume

[0053] wt % weight percent

[0054] ° C. degrees Centigrade

[0055] H₂O water

[0056] dH₂O or DI deionized water

[0057] dIH₂O deionized water, Milli-Q filtration

[0058] g gram

[0059] μg microgram

[0060] mg milligram

[0061] kg kilogram

[0062] μL and μl microliter

[0063] mL and ml milliliter

[0064] mm millimeter

[0065] μm micrometer

[0066] M molar

[0067] mM millimolar

[0068] μM micromolar

[0069] U unit

[0070] sec and '' second

[0071] min and ' minute

[0072] hr hour

[0073] eq. equivalent

[0074] N normal

[0075] RTU ready-to-use

[0076] U Unit

[0077] owg on weight of goods

[0078] CIE International Commission on Illumination

[0079] Numeric ranges are inclusive of the numbers defining the range. The singular articles "a," "an," "the," and the like, include the plural referents unless otherwise clear from context. Unless otherwise specified, polypeptides are written in the standard N-terminal to C-terminal direction and polynucleotides are written in the standard 5' to 3' direction. It is to be understood that the particular methodologies, protocols, and reagents described, are not intended to be limiting, as equivalent methods and materials can be used in the practice or testing of the present compositions and methods. Although the description is divided into sections to assist the reader, section heading should not be construed as limiting and the description in one section may apply to another. All publications cited herein are expressly incorporated by reference.

Laccase and Laccase Related Enzymes

[0080] The present laccase enzyme systems, compositions, and methods include one or more laccases or laccase-related enzymes, herein collectively referred to as "laccases" or "laccase enzymes." Such laccases include any laccase enzyme encompassed by EC 1.10.3.2, according to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB). Laccase enzymes from microbial and plant origin are known in the art. A microbial laccase enzyme may be derived from bacteria or fungi (including filamentous fungi and yeasts). Suitable examples include a laccase derived or derivable from a strain of Aspergillus, Neurospora (e.g., N. crassa), Podospora, Botrytis, Collybia, Cerrena (e.g., C. unicolor), Stachybotrys, Panus (e.g., P. rudis), Thielavia, Fomes, Lentinus, Pleurotus, Trametes (e.g., T. villosa, and T. versicolor), Rhizoctonia (e.g., R. solani), Coprinus (e.g., C. plicatilis and C. cinereus), Psatyrella, Myceliophthora (e.g., M. thermonhila), Schytalidium, Phlebia (e.g., P. radita (WO 92/01046)), or Coriolus (e.g., C. hirsutus (JP 2238885)), Spongipellis, Polyporus, Ceriporiopsis subvermispora, Ganoderma tsunodae, and Trichoderma.

[0081] A laccase may be produced by culturing a host cell transformed with a recombinant DNA vector that includes nucleotide sequences encoding the laccase. The DNA vector may further include nucleotide sequences permitting the expression of the laccase in a culture medium, and optionally allowing the recovery of the laccase from the culture.

[0082] An expression vector containing a polynucleotide sequence encoding a laccase enzyme may be transformed into a suitable host cell. The host cell may be a fungal cell, such as a filamentous fungal cell, examples of which include but are not limited to species of Trichoderma [e.g., T. reesei (previously classified as T. longibrachiatum and currently also known as Hypocrea jecorina], T. viride, T. koningii, and T. harzianum), Aspergillus (e.g., A. niger, A. nidulans, A. oryzae, and A. awamori), Penicillium, Humicola (e.g., H. insolens and H. grisea), Fusarium (e.g., F. graminum and F. venenatum), Neurospora, Hypocrea, and Mucor. A host cell for expression of a laccase enzyme may also be from a species of Cerrena (e.g., C. unicolor). Fungal cells may be transformed by a process involving protoplast formation and transformation of the protoplasts followed by regeneration of the cell wall using techniques known in the art.

[0083] Alternatively, the host organism may from a species of bacterium, such as Bacillus [e.g., B. subtilis, B. licheniformis, B. lentus, B. (now Geobacillus) stearothermophilus, and B. brevis], Pseudomonas, Streptomyces (e.g., S. coelicolor, S. lividans), or E. coli. The transformation of bacterial cells may be performed according to conventional methods, e.g., as described in Maniatis, T. et al., "Molecular Cloning: A Laboratory Manual," Cold Spring Harbor, 1982. The screening of appropriate DNA sequences and construction of vectors may also be carried out by standard procedures (cf. supra).

[0084] The medium used to culture the transformed host cells may be any conventional medium suitable for growing the host cells. In some embodiments, the expressed enzyme is secreted into the culture medium and may be recovered therefrom by well-known procedures. For example, laccases may be recovered from a culture medium as described in U.S. Patent Publication No. 2008/0196173. In some embodiments, the enzyme is expressed intracellularly and is recovered following disruption of the cell membrane.

[0085] In particular embodiments, the expression host may be Trichoderma reesei with the laccase coding region under the control of a CBH1 promoter and terminator (see, e.g., U.S. Pat. No. 5,861,271). The expression vector may be, e.g., pTrex3g, as disclosed in U.S. Pat. No. 7,413,887. In some embodiments, laccases are expressed as described in U.S. Patent Publication Nos. 2008/0196173 or 2009/0221030.

[0086] The following laccase genes and laccases are described in U.S. Publication No. 2008/0196173, and may be used as described:

TABLE-US-00001 A. Cerrena laccase A1 from CBS115.075 strain (SEQ ID NO: 1): MSSKLLALIT VALVLPLGTD AGIGPVTDLR ITNQDIAPDG FTRPAVLAGG 50 TFPGALITGQ KGDSFQINVI DELTDASMLT QTSIHWHGFF QKGSAWADGP 100 AFVTQCPIVT GNSFLYDFDV PDQPGTFWYH SHLSTQYCDG LRGPFVVYDP 150 KDPNKRLYDI DNDHTVITLA DWYHVLARTV VGVATPDATL INGLGRSPDG 200 PADAELAVIN VKRGKRYRFR LVSISCDPNY IFSIDNHSMT VIEVDGVNTQ 250 SLTVDSIQIF AGQRYSFVLH ANRPENNYWI RAKPNIGTDT TTDSGMNSAI 300 LRYNGAPVAE PQTVQSPSLT PLLEQNLRPL VYTPVPGNPT PGGADIVHTL 350 DLSFDAGRFS INGASFLDPT VPVLLQILSG TQNAQDLLPP GSVIPLELGK 400 VVELVIPAGV VGGPHPFHLH GHNFWVVRSA GTDQYNFNDA ILRDVVSIGG 450 TGDQVTIRFV TDNPGPWFLH CHIDWHLEAG LAIVFAEGIE NTAASNLTPQ 500 AWDELCPKYN ALSAQKKLNP STT 523 B. Cerrena laccase A2 from CBS154.29 strain (SEQ ID NO: 2): MSSKLLALIT VALVLPLGTD AGIGPVTDLR ITNQDIAPDG FTRPAVLAGG 50 TFPGALITGQ KGDSFQINVI DELTDASMLT QTSIHWHGFF QKGSAWADGP 100 AFVTQCPIVT GNSFLYDFDV PDQPGTFWYH SHLSTQYCDG LRGPFVVYDP 150 KDPNKRLYDI DNDHTVITLA DWYHVLARTV VGVATPDATL INGLGRSPDG 200 PADAELAVIN VKRGKRYRFR LVSISCDPNY IFSIDNHSMT VIEVDGVNTQ 250 SLTVDSIQIF AGQRYSFVLH ANRPENNYWI RAKPNIGTDT TTDNGMNSAI 300 LRYNGAPVAE PQTVQSPSLT PLLEQNLRPL VYTPVPGNPT PGGADIVHTL 350 DLSFDAGRFS INGASFLDPT VPVLLQILSG TQNAQDLLPP GSVIPLELGK 400 VVELVIPAGV VGGPHPFHLH GHNFWVVRSA GTDQYNFNDA ILRDVVSIGG 450 TEDQVTIRFV TDNPGPWFLH CHIDWHLEAG LAIVFAEGIE NTAASNPTPQ 500 AWDELCPKYN ALNAQKKLNP STT 523 C. Cerrena laccase B1 from CBS115.075 strain (SEQ ID NO: 3): MSLLRSLTSL IVLVIGAFAA IGPVTDLHIV NQNLDPDGFN RPTVLAGGTF 50 PGPLIRGNKG DNFKINVIDD LTEHSMLKAT SIHWHGFFQK GTNWADGPAF 100 VTQCPITSGN AFLYDFNVPD QAGTFWYHSH LSTQYCDGLR GAFVVYDPND 150 PNKQLYDVDN GNTVITLADW YHALAQTVTG VAVSDATLIN GLGRSATGPA 200 NAPLAVISVE RNKRYRFRLV SISCDPNFIF SIDHHPMTVI EMDGVNTQSM 250 TVDSIQIFAG QRYSFVMQAN QPVGNYWIRA KPNVGNTTFL GGLNSAILRY 300 VGAPDQEPTT DQTPNSTPLV EANLRPLVYT PVPGQPFPGG ADIVKNLALG 350 FNAGRFTING ASLTPPTVPV LLQILSGTHN AQDLLPAGSV IELEQNKVVE 400 IVLPAAGAVG GPHPFHLHGH NFWVVRSAGQ TTYNFNDAPI RDVVSIGGAN 450 DQVTIRFVTD NPGPWFLHCH IDWHLEAGFA VVFAEGINGT AAANPVPAAW 500 NQLCPLYDAL SPGDT 515 D. Cerrena laccase B2 from CBS154.29 strain (SEQ ID NO: 4): MSLLRSLTSL IVLATGAFAA IGPVTDLHIV NQNLAPDGLN RPTVLAGGTF 50 PGPLIRGNKG DNFKINVIDD LTEHSMLKAT SIHWHGFFQK GTNWADGPAF 100 VTQCPITSGN AFLYDFNVPD QAGTFWYHSH LSTQYCDGLR GAFVVYDPND 150 PNKQLYDVDN GNTVITLADW YHALAQTVTG VAVSDATLIN GLGRSATGPA 200 NAPLAVISVE RNKRYRFRLV SISCDPNFIF SIDHHPMTVI EMDGVNTQSM 250 TVDSIQIFAG QRYSFVMQAN QPVGNYWIRA KPNVGNTTFL GGLNSAILRY 300 VGAPDQEPTT DQTPNSTPLV EANLRPLVYT PVPGQPFPGG ADIVKNLALG 350 FNAGRFTING TSFTPPTVPV LLQILSGTHN AQDLLPAGSV IELEQNKVVE 400 IVLPAAGAVG GPHPFHLHGH NFWVVRSAGQ TTYNFNDAPI RDVVSIGGAN 450 DQVTIRFVTD NPGPWFLHCH IDWHLEAGFA VVFAEGINGT AAANPVPAAW 500 NQLCPLYDAL SPGDT 515 E. Cerrena laccase B3 (partial) from ATCC20013 strain (SEQ ID NO: 5): MSLLRSLTSL IVLATGAFAA IGPVTDLHIV NQNLAPDGFN RPTVLAGGTF 50 PGPLIRGNKG DNFKINVIDD LTEHSMLKAT SIHWHGFFQK GTNWADGPAF 100 VTQCPITSGN SFLYDFNVPD QAGTFWYHSH LSTQYCDGLR GAFVVYDPND 150 PNKQLYDVDN GKTVITLADW YHALAQTVTG VAVSDATLIN GLGRSATGPA 200 NAPLAVISVE RNKRYRFRLV SISCDPNFIF SIDHHPMTVI EMDGVNTQSM 250 TVDSIQIFAG QRYSFVMQAN QPVGNYWI 278 F. Cerrena laccase C (partial) from CBS154.29 strain (SEQ ID NO: 6): AIGPVADLHI TDDTIAPDGF SRPAVLAGGG FPGPLITGNK GDAFKLNVID 50 ELTDASMLKX TSIHWHGFFQ KGTNWADGPA FVNQCPITTG NSFLYDFQVP 100 DQAGTYWYHS HLSTQYCDGL RGAFVVYDPS DPHKDLYDVD DESTVITLAD 150 WYHTLARQIV GVAISDTTLI NGLGRNTNGP ADAALAVINV DAGKRYRFRL 200 VSISCDPNWV FSIDNHDFTV IEVDGVNSQP LNVDSVQIFA GQRYSF 246 G. Cerrena laccase D1 from CBS154.29 strain (SEQ ID NO: 7): MGLNSAITSL AILALSVGSY AAIGPVADIH IVNKDLAPDG VQRPTVLAGG 50 TFPGTLITGQ KGDNFQLNVI DDLTDDRMLT PTSIHWHGFF QKGTAWADGP 100 AFVTQCPIIA DNSFLYDFDV PDQAGTFWYH SHLSTQYCDG LRGAFVVYDP 150 NDPHKDLYDV DDGGTVITLA DWYHVLAQTV VGAATPDSTL INGLGRSQTG 200 PADAELAVIS VEHNKRYRFR LVSISCDPNF TFSVDGHNMT VIEVDGVNTR 250 PLTVDSIQIF AGQRYSFVLN ANQPEDNYWI RAMPNIGRNT TTLDGKNAAI 300 LRYKNASVEE PKTVGGPAQS PLNEADLRPL VPAPVPGNAV PGGADINHRL 350 NLTFSNGLFS INNASFTNPS VPALLQILSG AQNAQDLLPT GSYIGLELGK 400 VVELVIPPLA VGGPHPFHLH GHNFWVVRSA GSDEYNFDDA ILRDVVSIGA 450 GTDEVTIRFV TDNPGPWFLH CHIDWHLEAG LAIVFAEGIN QTAAANPTPQ 500 AWDELCPKYN GLSASQKVKP KKGTAI 526 H. Cerrena laccase D2 from CBS115.075 strain (SEQ ID NO: 8): MGLNSAITSL AILALSVGSY AAIGPVADIH IVNKDLAPDG VQRPTVLAGG 50 TFPGTLITGQ KGDNFQLNVI DDLTDDRMLT PTSIHWHGFF QKGTAWADGP 100 AFVTQCPIIA DNSFLYDFDV PDQAGTFWYH SHLSTQYCDG LRGAFVVYDP 150 NDPHKDLYDV DDGGTVITLA DWYHVLAQTV VGAATPDSTL INGLGRSQTG 200 PADAELAVIS VEHNKRYRFR LVSISCDPNF TFSVDGHNMT VIEVDGVNTR 250 PLTVDSIQIF AGQRYSFVLN ANQPDDNYWI RAMPNIGRNT TTLDGKNAAI 300 LRYKNASVEE PKTVGGPAQS PLNEADLRPL VPAPVPGNAV PGGADINHRL 350 NLTFSNGLFS INNASFTNPS VPALLQILSG AQNAQDLLPT GSYIGLELGK 400 VVELVIPPLA VGGPHPFHLH GHNFWVVRSA GSDEYNFDDA ILRDVVSIGA 450 GTDEVTIRFV TDNPGPWFLH CHIDWHLEAG LAIVFAEGIN QTAAANPTPQ 500 AWDELCPKYN GLSASQKVKP KKGTAI 526 I. Cerrena laccase E (partial) from CBS154.29 strain (SEQ ID NO: 9): AIGPVADLKI VNRDIAPDGF IRPAVLAGGS FPGPLITGQK GNEFKINVVN 50 QLTDGSMLKS TSIHWHGFFQ KGTNWADGPA FVNQCPIATN NSFLYQFTSQ 100 EQPGTFWYHS HLSTQYCDGL RGPLVVYDPQ DPHAVLYDVD DESTIITLAD 150 WYHTLARQVK GPAVPGTTLI NGLGRHNNGP LDAELAVISV QAGKRQVQFT 200 LFTLYRFRLI SISCDPNYVF SIDGHDMTVI EVDSVNSQPL KVDSIQIFAG 250 QRYSFVLNAN QP 262 In some embodiments, a laccase D enzyme having the following amino acid sequence (SEQ ID NO: 10; signal sequence in italics) may be used: MGLNSAITSL AILALSVGSY AAIGPVADLH IVNKDLAPDG VQRPTVLAGG 50 TFPGTLITGQ KGDNFQLNVI DDLTDDRMLT PTSIHWHGFF QKGTAWADGP 100 AFVTQCPIIA DNSFLYDFDV PDQAGTFWYH SHLSTQYCDG LRGAFVVYDP 150 NDPHKDLYDV DDGGTVITLA DWYHVLAQTV VGAATPDSTL INGLGRSQTG 200 PADAELAVIS VEHNKRYRFR LVSISCDPNF TFSVDGHNMT VIEVDGVNTR 250 PLTVDSIQIF AGQRYSFVLN ANQPEDNYWI RAMPNIGRNT TTLDGKNAAI 300 LRYKNASVEE PKTVGGPAQS PLNEADLRPL VPAPVPGNAV PGGADINHRL 350 NLTFSNGLFS INNASFTNPS VPALLQILSG AQNAQDLLPT GSYIGLELGK 400 VVELVIPPLA VGGPHPFHLH GHNFWVVRSA GSDEYNFDDA ILRDVVSIGA 450 GTDEVTIRFV TDNPGPWFLH CHIDWHLEAG LAIVFAEGIN QTAAANPTPQ 500 AWDELCPKYN GLSASQKVKP KKGTAI 526 The mature processed form of this polypeptide is as follows (SEQ ID NO: 11): AIGPVADLHIVNKDLAPDGVQRPTVLAGGTFPGILITGQKGDNFQLNVIDDLTDDRMLTPTS IHWHGFFQKGTAWADGPAFVTQCPIIADNSFLYDFDVPDQAGTFWYHSHLSTQYCDGLRGAF VVYDPNDPHKDLYDVDDGGTVITLADWYHVLAQTVVGAATPDSTLINGLGRSQTGPADAELA VISVEHNKRYRFRLVSISCDPNFTFSVDGHNMTVIEVDGVNTRPLTVDSIQIFAGQRYSFVL NANQPEDNYWIRAMPNIGRNTTTLDGKNAAILRYKNASVEEPKTVGGPAQSPLNEADLRPLV PAPVPGNAVPGGADINHRLNLIFSNGLFSINNASFTNPSVPALLQILSGAQNAQDLLPTGSY IGLELGKVVELVIPPLAVGGPHPFHLHGHNFWVVRSAGSDEYNFDDAILRDVVSIGAGTDEV TIRFVTDNPGPWFLHCHIDWHLEAGLAIVFAEGINQTAAANPTPQAWDELCPKYNGLSASQK VKPKKGTAI

[0087] In some embodiments, laccase enzymes suitable for use in the present compositions and methods are mature polypeptides that lack a signal sequence that may be used to direct secretion of a full-length polypeptide from a cell. A suitable mature polypeptide may have at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or even at least 99%, or more, amino acid sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11. Preferably, such polypeptides have enzymatic laccase activity, as determined using the assays and procedures described, herein.

[0088] In some embodiments, laccase enzymes suitable for use in the present compositions and methods are truncated with respect to a full-length or mature parent/reference sequence. Such truncated polypeptides may be generated by the proteolytic degradation of a full-length or mature polypeptide sequence or by engineering a polynucleotide to encode a truncated polypeptide. Exemplary polypeptides are truncated at the amino and/or carboxyl-terminus with respect to an amino acid sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11. The truncation may be of a small number, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid residues, or of entire structural or functional domains. A suitable truncated polypeptide may have at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or even at least 99%, or more, amino acid sequence identity to the corresponding portion of one or more of the above-references amino acid sequences. Preferably, such polypeptides have enzymatic laccase activity, as determined using the assays and procedures described, herein.

Mediators

[0089] In some embodiments, the present laccase enzyme systems, compositions, and methods, further include one or more chemical mediator agents that enhance the activity of the laccase enzyme. A mediator (also called an enhancer or accelerator) is a chemical that acts as a redox mediator to effectively shuttle electrons between the enzyme exhibiting oxidase activity and a dye, pigment (e.g., indigo), chromophore (e.g., polyphenolic, anthocyanin, or carotenoid, for example, in a colored stain), or other secondary substrate or electron donor.

[0090] In some embodiments the chemical mediator is a phenolic compound, for example, methyl syringate, or a related compound, as described in, e.g., PCT Application Nos. WO 95/01426 and WO 96/12845. The mediator may also be an N-hydroxy compound, an N-oxime compound, or an N-oxide compound, for example, N-hydroxybenzotriazole, violuric acid, or N-hydroxyacetanilide. The mediator may also be a phenoxazine/phenothiazine compound, for example, phenothiazine-10-propionate. The mediator may further be 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). Other chemical mediators are well known in the art, for example, the compounds disclosed in PCT Application No. WO 95/01426, which are known to enhance the activity of a laccase. The mediator may also be acetosyringone, methyl syringate, ethyl syringate, propyl syringate, butyl syringate, hexyl syringate, or octyl syringate.

[0091] In some embodiments, the mediator is 4-cyano-2,6-dimethoxyphenol, 4-carboxamido-2,6-dimethoxyphenol or an N-substituted derivative thereof such as, for example, 4-(N-methyl carboxamido)-2,6-dimethoxyphenol, 4-[N-(2-hydroxyethyl) carboxamido]-2,6-dimethoxyphenol, or 4-(NN-dimethyl carboxamido)-2,6-dimethoxyphenol.

[0092] In some embodiments, the mediator is described by the following formula:

##STR00001##

in which A is a group such as -R, -D, --CH═CH-D, --CH═CH--CH═CH-D, --CH═N-D, --N═N-D, or N═CH-D, D is selected from the group consisting of --CO-E, --SO₂-E, --CN, -NXY, and --N⁺XYZ, E is --H, --OH, -R, --OR, or --NXY, and X,Y, and Z are independently selected from --H, --OH, --OR, and -R; where R is a C₁-C₁6 alkyl, preferably a C₁-C₈ alkyl, which alkyl may be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C are independently selected from C_m H₂m+1; 1≦m≦5.

[0093] In some embodiments, A in the above mentioned formula is --CN or --CO-E, wherein E may be --H, --OH, -R, --OR, or --NXY, where X and Y are independently selected from --H, --OH, --OR, and -R, where R is a C₁-C₁6 alkyl, preferably a C₁-C₈ alkyl, which alkyl may be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C are independently selected from C_m H₂m+1; 1≦m≦5. In some embodiments, the mediator is 4-hydroxy-3,5-dimethoxybenzonitrile (also referred to as "syringonitrile" or "SN").

[0094] Note that in the above mentioned formula, A may be placed meta to the hydroxy group, instead of being placed in the para position as shown.

[0095] For applications such as textile processing, the mediator may be present in a concentration of about 0.005 to about 1,000 mole per g denim, about 0.05 to about 500 mole per g denim, about 0.1 to about 100μ mole per g denim, about 1 to about 50μ mole per g denim, or about 2 to about 20μ mole per g denim.

[0096] The mediators may be prepared by methods known to the skilled artisan, such as those disclosed in PCT Application Nos. WO 97/11217 and WO 96/12845 and U.S. Pat. No. 5,752,980. Other suitable mediators are described in, e.g., U.S. Patent Publication No. 2008/0189871.

Methods of Use

[0097] Generally, the methods involve locally contacting a textile or garment with a laccase enzyme system for a length of time, and under conditions, sufficient to produce at least one measurable or visual local effect to the fabric or textile. Exemplary effects are, e.g., a change in color, a change in color cast, lightening, bleaching, and fading. The present laccase enzyme systems, compositions, and methods can be use in applications where localized color modification of dyed fabrics is desirable. Examples of localized color modification include color modification the fronts or backs of jeans, to sleeves, to collars, to cuffs, to belt loops, and the like.

[0098] The method may be performed by wetting (but not submerging) a portion of the dyed textile with a composition comprising the laccase enzyme system, or performed by applying a composition comprising the laccase enzyme system to a portion of the dyed textile, and then wetting (but not submerging) the portion of the dyed textile. An important feature of the method is that less than the entire fabric or garment is contacted with the laccase enzyme system, and that color modification occurs on less than the entire fabric or garment.

[0099] The laccase enzyme system may be provided in a single composition, which may be aqueous, gel, semi-solid, or solid in form. Alternatively, the laccase enzyme system may be provided in a plurality of compositions, which may be aqueous, gel, semi-solid, or solid, or a combination, thereof. Where the laccase system, or components, thereof, are provided in liquid form, they can be applied to fabrics or garments by pouring, dripping, brushing, blotting, spraying, dipping, and the like. Where the laccase system, or components, thereof, are provided in gel, paste, or other semi-solid form, they can be applied using a stick applicator, by dispensing from a tube or syringe, drawn with a crayon, or the like. Where the laccase system, or components, thereof, are provided in dry or solid form, they can be applied by shaking from a container, as a talc, or the like.

[0100] In many embodiments, the fabric or garment may be wetted before and/or after application of the laccase; however, the fabric or garment is generally not submerged in an aqueous medium (i.e., in a "bath"), since this procedure would allow the color modification to become generalized. Thus, particular embodiments of the methods are expressly not performed under submerged conditions.

[0101] In some embodiments, the localized color modification may be in the form of a predetermined pattern or shape, as exemplified by the heart shape illustrated in FIG. 1. In further embodiments, the pattern or shape may in the form of letters (including numbers and symbols), words, logos, trademarks (including tradedress), or the like. In some embodiments, the pattern or shape may be designed to mimic the appearance of conventional textile processing methods, such as sandblasting.

[0102] In some embodiments, the predetermined pattern or shape is selected by the textile manufacturer. In other embodiments, the predetermined pattern or shape is selected by a retailer or consumer. In some cases, the term predetermined may apply to the overall aesthetic desired, rather than an exact pattern. For example, local color variant can be in the form of unique and artistic designs, even designs with a random element, which are still considered to be predetermined as used herein.

[0103] In some embodiments, different levels of local color modification are produced by applying different amounts of a laccase enzyme system, applying a laccase enzyme system for different amounts of time, or applying laccase enzyme systems that have been preincubated for different amounts of time to dyed fabric. In this manner, a dyed fabric can be modified to have more than one color modification, e.g., a "light-colored portion" and a "lighter colored portion." The ability to produce different levels of color modification greatly increases the complexity of patterns and shapes that can be produced.

[0104] Textiles that can be subjected to color modification as described include cellulosic and non-cellulosis textiles, for example, cotton, linen, flax, hemp, jute wool, silk, nylon, polyester, acrylic, and blends, thereof.

[0105] The textile may be dyed with any dye that may be decolorized using a laccase enzyme. Examples of dyes include, but are not limited to, azo, monoazo, disazo, nitro, xanthene, quinoline, anthroquinone, triarylmethane, paraazoanyline, azineoxazine, stilbene, aniline, and phthalocyanine dyes, or mixtures thereof. In some embodiments, the dye is an azo dye (e.g., Reactive Black 5 (2,7-naphthalenedisulfonic acid, 4-amino-5- hydroxy-3,6-bis((4-((2-(sulfooxy)ethyl)sulfonyl)phenyl)azo)-tetrasodium salt), Reactive Violet 5, methyl yellow, congo red). In some embodiments, the dye is an anthraquinone dye (e.g., remazol blue), indigo (indigo carmine), or a triarylmethane/paraazoanyline dye (e.g., crystal violet, malachite green). In various embodiments, the dye is a reactive, direct, disperse, or pigment dye. In some embodiments, the dye is comprised within an ink In some embodiments, the dye is indigo and/or a sulfur-based dye. In some embodiments, the textile is denim dyed with indigo and/or a sulfur-based dye. In a particular embodiment, the textile is dyed with indigo, and the laccase enzyme and mediator are used to oxidize the indigo to isatin.

[0106] The methods contemplate the use of one or more of the laccases, many of which are described herein. In some embodiments, the laccase is from a Cerrena species, such as C. unicolor. In some embodiments, the laccase comprises, consists of, or consists essentially of the amino acid sequence of any of the C. unicolor laccase enzymes described herein, or an amino acid sequence having any of at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5% identity to any of the C. unicolor laccase enzymes described herein, and having laccase enzymatic activity. In a particular embodiment, the laccases is C. unicolor laccase D, or a closely related laccase.

[0107] In some embodiments, such methods include localized incubation of a laccase enzyme with a dyed fabric at a low temperature, for example, about 50° C. or less, about 45° C. or less, or even about 40° C. or less. In some embodiments, the temperature is between about 10° C. and about 50° C. In some embodiments, the temperature is between about 15° C. and about 45° C. In some embodiments, the temperature is between about 20° C. and about 40° C. In some embodiments, the temperature is between about 25° to about 35° C. In some embodiments, the temperature is about 10° C., 15° C., 20° C., 25° C., 30° C., 35° C., 40° C., 45° C., or 50° C. In some embodiments, the temperature is ambient air temperature.

[0108] In some embodiments, one or more laccase enzymes are used at a concentration of about 0.005 to about 5,000 mg/liter, about 0.05 to about 500 mg/liter, about 0.1 to about 100 mg/liter, or about 0.5 to about 10 mg/liter. In some processing embodiments, a laccase is used at a concentration of about 0.005 to about 5,000 mg/kg of fabric (such as denim), e.g., about 0.05 to about 500 mg/kg of fabric, about 0.1 to about 100 mg/kg of fabric, or about 0.5 to about 10 mg/kg of fabric. In some embodiments, a laccase is used at a pH of about 5 to about 8, about 5 to about 7.5, about 5 to about 7, about 5.5 to about 6.5, about 5 to about 6, or about 6. Exemplary pH values are about 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, and 8.0.

[0109] The present localized color modification systems, compositions, and methods, can be utilized following various textile processing steps applied to whole garments or fabrics, for example, desizing, abrading (physical or enzymatic), scouring, dyeing, bleach clean-up, biopolishing, enzymatic or chemical color modification, and the like.

[0110] Abrading and/or biopolishing may be performed using a suitable cellulase, such as those derived from microorganisms which are known to be capable of producing cellulolytic enzymes, e.g., species of Humicola, Thermomyces, Bacillus, Trichoderma, Fusarium, Myceliophthora, Phanerochaete, Irpex, Scytalidium, Schizophyllum, Penicillium, Aspergillus or Geotricum. Known species capable for producing celluloytic enzymes include Humicola insolens, Fusarium oxysporum or Trichoderma reesei. Non-limiting examples of suitable cellulases are disclosed in U.S. Pat. No. 4,435,307; European patent application No. 0 495 257; PCT Patent Application No. WO 91/17244; and European Patent Application No. EP-A2-271 004, all of which are incorporated herein by reference.

[0111] In some embodiments, the present systems, compositions, and methods, are using before or after "stonewashing" using a cellulase, bleaching using an aryl esterase, and/or color modification to the entire textile or garment using a laccase, can be combined to provide a comprehensive enzymatic textile processing system. Such a system allows a textile processor to produce textiles with a wide variety of finishes without the need to use conventional textile processing chemical.

[0112] In some embodiments, the present systems, compositions, and methods, are using before or after "desizing," e.g., using an amylase, "scouring", e.g., using a pectate lyase, and/or bleach-clean-up," using catalase.

Compositions and Kits for Local Color Modification

[0113] The present systems and compositions can be provided in one of more aqueous, gel, semi-solid, or solid compositions comprising, consisting of, or consisting essentially of a laccase enzyme and, optionally, a mediator suitable for localized fabric application. In some embodiments, the present systems and compositions can be provided in the form of a single "just add water" or "ready to use" (RTU) composition. Such compositions may further contain one or more buffers, dispersants, surfactants, blockers, polymers, preservatives, and the like. An exemplary buffer is a monosodium phosphate/adipic acid system. In particular embodiments, the compositions are in granular form for ease of storage and transportation. Such compositions are diluted with water prior to use.

[0114] Once reconstituted for use from a convenient storage form, the laccase enzyme system may be allowed to preincubate for a period of time, e.g., 5 minutes to 2 hours, 10 minutes to 1 hour, 15 minutes to 45 minutes, 20 minutes to 30 minutes, and the like. Exemplary pre-incubation times are about 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90, 95, 100, 105, 110, 115, and 120 minutes.

[0115] The laccase compositions may then be applied to a fabric or garment by pouring, dripping, brushing, blotting, spraying, using a stick applicator, by dispensing from a tube or syringe, drawn with a crayon, shaking from a container, as a talc, or the like. Where the laccase enzyme system is in the form of a liquid, it is preferably applied by spraying (e.g., using an air brush or aerosol bottle), or using a free-hand brush, roller, or the like. A stencil may be used to help define the pattern or shape.

[0116] The present systems, compositions, and methods are further described in the following numbered paragraphs.

[0117] 1. A textile processing method is provided, comprising contacting a portion of dyed textile with a laccase enzyme system for a length of time and under conditions sufficient to cause a localized color modification to the portion of the textile.

[0118] 2. In some embodiments, the method of paragraph 1 is performed by wetting but not submerging the portion of the dyed textile with a composition comprising the laccase enzyme system.

[0119] 3. In some embodiments, the method of paragraph 1 is performed by applying a composition comprising the laccase enzyme system to the portion of the dyed textile, and then wetting but not submerging the portion of the dyed textile.

[0120] 4. In some embodiments of the method of any of the preceding paragraphs, the laccase enzyme system is provided in a single composition.

[0121] 5. In some embodiments of the method of any of the preceding paragraphs, the laccase enzyme system is provided as an aqueous, gel, semi-solid, or solid formulation.

[0122] 6. In some embodiments of the method of any of the preceding paragraphs, the color modification is selected from lightening of color, change of color, change in color cast, and bleaching.

[0123] 7. In some embodiments of the method of any of the preceding paragraphs, the textile is indigo-dyed denim.

[0124] 8. In some embodiments of the method of any of the preceding paragraphs, the textile is indigo and sulfur-dyed denim.

[0125] 9. In some embodiments of the method of any of the preceding paragraphs, the textile is a pair of jeans.

[0126] 10. In some embodiments of the method of any of the preceding paragraphs, the portion of the textile is a pant leg, sleeve, cuff, collar, pocket, or belt loop.

[0127] 11. In some embodiments of the method of any of the preceding paragraphs, the portion of the textile is in the form of a predetermined shape.

[0128] 12. In some embodiments of the method of any of the preceding paragraphs, the portion of the textile is in the form of a letter, word, logo, or trademark.

[0129] 13. In some embodiments of the method of any of the preceding paragraphs, the laccase enzyme system comprises a laccase enzyme and a mediator.

[0130] 14. In some embodiments of the method of paragraph 13, the laccase is a microbial laccase.

[0131] 15. In some embodiments of the method of paragraph 13, the laccase is from a Cerrena species.

[0132] 16. In some embodiments of the method of paragraph 13, the laccase is from Cerrena unicolor.

[0133] 17. In some embodiments of the method of paragraph 13, the laccase is laccase D from C. unicolor.

[0134] 18. In some embodiments of the method of any of paragraphs 13-17, the mediator is syringonitrile.

[0135] 19. In some embodiments of the method of any of the preceding paragraphs, the method is performed at a temperature of from about 20° C. to about 40° C.

[0136] 20. In some embodiments of the method of any of the preceding paragraphs, the method is performed at a temperature of from about 20° C. to about 30° C.

[0137] 21. In some embodiments of the method of any of the preceding paragraphs, the method is performed at the ambient temperature of tap water.

[0138] 22. In some embodiments of the method of any of the preceding paragraphs, the method is performed at ambient air temperature.

[0139] 23. Further provided is a locally color-modified dyed textile produced by the method of any of the preceding paragraphs.

[0140] The following examples are provided to illustrate the systems, compositions, and methods, and should in no way be construed as limiting. Other aspects and embodiments will be apparent to the skilled person in view of the description.

EXAMPLES

Example 1

Effect of Dose on Laccase-Mediated Color Modification of Stonewashed Denim

[0141] Various amounts of a laccase enzyme/mediator system (PRIMAGREEN® EcoFade LT 100; Danisco US Inc.) were applied locally to denim fabric and the resulting changes in color were measured. PRIMAGREEN® EcoFade LT 100 includes a Cerrena unicolor laccase D enzyme and 4-hydroxy-3,5-dimethoxybenzonitrile (syringonitrile) in a dry granular formulation, which can be prepared for use by addition of water (or other aqueous medium). The amount of laccase activity in the formulation is at least 38,000 U/g.

[0142] The amounts of laccase/mediator system tested were 1%, 3%, and 10% (w/v) in water, which were applied to denim after a pre-incubation at room temperature of 1 hour, and incubated on the denim for a period of 30 and 60 minutes at 40° C. The amount of color modification was determined using a chromameter. The results obtained at the 30 minute time point are shown in Table 1, wherein a higher L value indicates a higher bleaching level. The results obtained at the 60 minute time point were similar, suggesting that the process is essentially complete at 30 minutes. Increasing amounts of the laccase/mediator system produced increasing amounts of color modification, in this case a bleaching effect, demonstrating dose response.

TABLE-US-00002 TABLE 1 Local color modification obtained using various doses of the laccase/mediator system. Bleaching level CIE Description CIE L/a/b L value * Control (stonewashed denim 27.53/0.89/-12.97 27.53 1% PRIMAGREEN ® 27.94/0.66/-12.49 27.94 EcoFade LT100 3% PRIMAGREEN ® 29.81/-0.05/-11.80 29.81 EcoFade LT100 10% PRIMAGREEN ® 31.22/-0.43/-11.21 31.22 EcoFade LT100

Example 2

Effect of Pre-Incubation Time on Laccase-Mediated Color Modification of Stonewashed Denim

[0143] A 10% (w/v) solution of a laccase/mediator system (see Example 1) solution that was freshly made, and a 10% (w/v) solution that was pre-incubated for 45 minutes at room temperature, were separately applied to denim and incubated it for 25 minutes at 40° C. The fabric was then rinsed and dried. The amount of color modification was determined using a chromameter (Table 2). The color modification was more pronounced when the solution of the laccase/mediator system was pre-incubated prior to application to the fabric.

TABLE-US-00003 TABLE 2 Local color modification obtained using pre-incubated laccase/mediator. Bleaching level Description L a b values CIE L value Stonewashed denim 28.98/-0.01/-12.47 29.0 Direct application 30.03/-0.56/-11.59 30.0 45-minute pre-incubation 32.00/-1.38/-10.06 32.0

[0144] In a related experiment, a 10% (w/v) solution of laccase/mediator system was prepared in water and pre-incubated for 90 minutes at room temperature. The pre-incubated solution was then applied to the denim by spraying. The fabric was incubated at room temperature overnight, rinsed, and dried. The amount of color modification was determined using a chromameter. As summarized in Table 3, moderate local color modification effects were visible.

TABLE-US-00004 TABLE 3 Local color modification obtained using pre-incubated laccase/mediator. Description L a b values Denim 27.5/1.0/-13.3 Local effect 30.7/0.2/-12.4

[0145] In a related experiment, a 10% (w/v) solution of laccase/mediator system was prepared in water and pre-incubated for 90 minutes at 50° C. The pre-incubated solution was then applied to denim by spraying. The fabric was incubated for 1 hour at 40° C., rinsed, and dried. The amount of color modification was determined using a chromameter. As summarized in Table 4, clear local color modification effects were visible. An image of the treated garment, showing a region of local modification in the form of a heart shape, is shown in FIG. 1.

TABLE-US-00005 TABLE 4 Local color modification obtained using pre-incubated laccase/mediator. Description L a b values Denim 27.1/1.1/-12.8 Local effect 32.5/0.2/11.7

[0146] The aspects, embodiments, and examples described herein are for illustrative purposes only. Various modifications will be apparent to the skilled person, and are included within the spirit and purview of this application, and the scope of the appended claims. All publications and patent documents cited herein are hereby incorporated by reference in their entirety.

Sequence CWU 1

1

111523PRTCerrena unicolor 1Met Ser Ser Lys Leu Leu Ala Leu Ile Thr Val Ala Leu Val Leu Pro 1 5 10 15 Leu Gly Thr Asp Ala Gly Ile Gly Pro Val Thr Asp Leu Arg Ile Thr 20 25 30 Asn Gln Asp Ile Ala Pro Asp Gly Phe Thr Arg Pro Ala Val Leu Ala 35 40 45 Gly Gly Thr Phe Pro Gly Ala Leu Ile Thr Gly Gln Lys Gly Asp Ser 50 55 60 Phe Gln Ile Asn Val Ile Asp Glu Leu Thr Asp Ala Ser Met Leu Thr 65 70 75 80 Gln Thr Ser Ile His Trp His Gly Phe Phe Gln Lys Gly Ser Ala Trp 85 90 95 Ala Asp Gly Pro Ala Phe Val Thr Gln Cys Pro Ile Val Thr Gly Asn 100 105 110 Ser Phe Leu Tyr Asp Phe Asp Val Pro Asp Gln Pro Gly Thr Phe Trp 115 120 125 Tyr His Ser His Leu Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Pro 130 135 140 Phe Val Val Tyr Asp Pro Lys Asp Pro Asn Lys Arg Leu Tyr Asp Ile 145 150 155 160 Asp Asn Asp His Thr Val Ile Thr Leu Ala Asp Trp Tyr His Val Leu 165 170 175 Ala Arg Thr Val Val Gly Val Ala Thr Pro Asp Ala Thr Leu Ile Asn 180 185 190 Gly Leu Gly Arg Ser Pro Asp Gly Pro Ala Asp Ala Glu Leu Ala Val 195 200 205 Ile Asn Val Lys Arg Gly Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile 210 215 220 Ser Cys Asp Pro Asn Tyr Ile Phe Ser Ile Asp Asn His Ser Met Thr 225 230 235 240 Val Ile Glu Val Asp Gly Val Asn Thr Gln Ser Leu Thr Val Asp Ser 245 250 255 Ile Gln Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val Leu His Ala Asn 260 265 270 Arg Pro Glu Asn Asn Tyr Trp Ile Arg Ala Lys Pro Asn Ile Gly Thr 275 280 285 Asp Thr Thr Thr Asp Ser Gly Met Asn Ser Ala Ile Leu Arg Tyr Asn 290 295 300 Gly Ala Pro Val Ala Glu Pro Gln Thr Val Gln Ser Pro Ser Leu Thr 305 310 315 320 Pro Leu Leu Glu Gln Asn Leu Arg Pro Leu Val Tyr Thr Pro Val Pro 325 330 335 Gly Asn Pro Thr Pro Gly Gly Ala Asp Ile Val His Thr Leu Asp Leu 340 345 350 Ser Phe Asp Ala Gly Arg Phe Ser Ile Asn Gly Ala Ser Phe Leu Asp 355 360 365 Pro Thr Val Pro Val Leu Leu Gln Ile Leu Ser Gly Thr Gln Asn Ala 370 375 380 Gln Asp Leu Leu Pro Pro Gly Ser Val Ile Pro Leu Glu Leu Gly Lys 385 390 395 400 Val Val Glu Leu Val Ile Pro Ala Gly Val Val Gly Gly Pro His Pro 405 410 415 Phe His Leu His Gly His Asn Phe Trp Val Val Arg Ser Ala Gly Thr 420 425 430 Asp Gln Tyr Asn Phe Asn Asp Ala Ile Leu Arg Asp Val Val Ser Ile 435 440 445 Gly Gly Thr Gly Asp Gln Val Thr Ile Arg Phe Val Thr Asp Asn Pro 450 455 460 Gly Pro Trp Phe Leu His Cys His Ile Asp Trp His Leu Glu Ala Gly 465 470 475 480 Leu Ala Ile Val Phe Ala Glu Gly Ile Glu Asn Thr Ala Ala Ser Asn 485 490 495 Leu Thr Pro Gln Ala Trp Asp Glu Leu Cys Pro Lys Tyr Asn Ala Leu 500 505 510 Ser Ala Gln Lys Lys Leu Asn Pro Ser Thr Thr 515 520 2523PRTCerrena unicolor 2Met Ser Ser Lys Leu Leu Ala Leu Ile Thr Val Ala Leu Val Leu Pro 1 5 10 15 Leu Gly Thr Asp Ala Gly Ile Gly Pro Val Thr Asp Leu Arg Ile Thr 20 25 30 Asn Gln Asp Ile Ala Pro Asp Gly Phe Thr Arg Pro Ala Val Leu Ala 35 40 45 Gly Gly Thr Phe Pro Gly Ala Leu Ile Thr Gly Gln Lys Gly Asp Ser 50 55 60 Phe Gln Ile Asn Val Ile Asp Glu Leu Thr Asp Ala Ser Met Leu Thr 65 70 75 80 Gln Thr Ser Ile His Trp His Gly Phe Phe Gln Lys Gly Ser Ala Trp 85 90 95 Ala Asp Gly Pro Ala Phe Val Thr Gln Cys Pro Ile Val Thr Gly Asn 100 105 110 Ser Phe Leu Tyr Asp Phe Asp Val Pro Asp Gln Pro Gly Thr Phe Trp 115 120 125 Tyr His Ser His Leu Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Pro 130 135 140 Phe Val Val Tyr Asp Pro Lys Asp Pro Asn Lys Arg Leu Tyr Asp Ile 145 150 155 160 Asp Asn Asp His Thr Val Ile Thr Leu Ala Asp Trp Tyr His Val Leu 165 170 175 Ala Arg Thr Val Val Gly Val Ala Thr Pro Asp Ala Thr Leu Ile Asn 180 185 190 Gly Leu Gly Arg Ser Pro Asp Gly Pro Ala Asp Ala Glu Leu Ala Val 195 200 205 Ile Asn Val Lys Arg Gly Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile 210 215 220 Ser Cys Asp Pro Asn Tyr Ile Phe Ser Ile Asp Asn His Ser Met Thr 225 230 235 240 Val Ile Glu Val Asp Gly Val Asn Thr Gln Ser Leu Thr Val Asp Ser 245 250 255 Ile Gln Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val Leu His Ala Asn 260 265 270 Arg Pro Glu Asn Asn Tyr Trp Ile Arg Ala Lys Pro Asn Ile Gly Thr 275 280 285 Asp Thr Thr Thr Asp Asn Gly Met Asn Ser Ala Ile Leu Arg Tyr Asn 290 295 300 Gly Ala Pro Val Ala Glu Pro Gln Thr Val Gln Ser Pro Ser Leu Thr 305 310 315 320 Pro Leu Leu Glu Gln Asn Leu Arg Pro Leu Val Tyr Thr Pro Val Pro 325 330 335 Gly Asn Pro Thr Pro Gly Gly Ala Asp Ile Val His Thr Leu Asp Leu 340 345 350 Ser Phe Asp Ala Gly Arg Phe Ser Ile Asn Gly Ala Ser Phe Leu Asp 355 360 365 Pro Thr Val Pro Val Leu Leu Gln Ile Leu Ser Gly Thr Gln Asn Ala 370 375 380 Gln Asp Leu Leu Pro Pro Gly Ser Val Ile Pro Leu Glu Leu Gly Lys 385 390 395 400 Val Val Glu Leu Val Ile Pro Ala Gly Val Val Gly Gly Pro His Pro 405 410 415 Phe His Leu His Gly His Asn Phe Trp Val Val Arg Ser Ala Gly Thr 420 425 430 Asp Gln Tyr Asn Phe Asn Asp Ala Ile Leu Arg Asp Val Val Ser Ile 435 440 445 Gly Gly Thr Glu Asp Gln Val Thr Ile Arg Phe Val Thr Asp Asn Pro 450 455 460 Gly Pro Trp Phe Leu His Cys His Ile Asp Trp His Leu Glu Ala Gly 465 470 475 480 Leu Ala Ile Val Phe Ala Glu Gly Ile Glu Asn Thr Ala Ala Ser Asn 485 490 495 Pro Thr Pro Gln Ala Trp Asp Glu Leu Cys Pro Lys Tyr Asn Ala Leu 500 505 510 Asn Ala Gln Lys Lys Leu Asn Pro Ser Thr Thr 515 520 3515PRTCerrena unicolor 3Met Ser Leu Leu Arg Ser Leu Thr Ser Leu Ile Val Leu Val Ile Gly 1 5 10 15 Ala Phe Ala Ala Ile Gly Pro Val Thr Asp Leu His Ile Val Asn Gln 20 25 30 Asn Leu Asp Pro Asp Gly Phe Asn Arg Pro Thr Val Leu Ala Gly Gly 35 40 45 Thr Phe Pro Gly Pro Leu Ile Arg Gly Asn Lys Gly Asp Asn Phe Lys 50 55 60 Ile Asn Val Ile Asp Asp Leu Thr Glu His Ser Met Leu Lys Ala Thr 65 70 75 80 Ser Ile His Trp His Gly Phe Phe Gln Lys Gly Thr Asn Trp Ala Asp 85 90 95 Gly Pro Ala Phe Val Thr Gln Cys Pro Ile Thr Ser Gly Asn Ala Phe 100 105 110 Leu Tyr Asp Phe Asn Val Pro Asp Gln Ala Gly Thr Phe Trp Tyr His 115 120 125 Ser His Leu Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Ala Phe Val 130 135 140 Val Tyr Asp Pro Asn Asp Pro Asn Lys Gln Leu Tyr Asp Val Asp Asn 145 150 155 160 Gly Asn Thr Val Ile Thr Leu Ala Asp Trp Tyr His Ala Leu Ala Gln 165 170 175 Thr Val Thr Gly Val Ala Val Ser Asp Ala Thr Leu Ile Asn Gly Leu 180 185 190 Gly Arg Ser Ala Thr Gly Pro Ala Asn Ala Pro Leu Ala Val Ile Ser 195 200 205 Val Glu Arg Asn Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile Ser Cys 210 215 220 Asp Pro Asn Phe Ile Phe Ser Ile Asp His His Pro Met Thr Val Ile 225 230 235 240 Glu Met Asp Gly Val Asn Thr Gln Ser Met Thr Val Asp Ser Ile Gln 245 250 255 Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val Met Gln Ala Asn Gln Pro 260 265 270 Val Gly Asn Tyr Trp Ile Arg Ala Lys Pro Asn Val Gly Asn Thr Thr 275 280 285 Phe Leu Gly Gly Leu Asn Ser Ala Ile Leu Arg Tyr Val Gly Ala Pro 290 295 300 Asp Gln Glu Pro Thr Thr Asp Gln Thr Pro Asn Ser Thr Pro Leu Val 305 310 315 320 Glu Ala Asn Leu Arg Pro Leu Val Tyr Thr Pro Val Pro Gly Gln Pro 325 330 335 Phe Pro Gly Gly Ala Asp Ile Val Lys Asn Leu Ala Leu Gly Phe Asn 340 345 350 Ala Gly Arg Phe Thr Ile Asn Gly Ala Ser Leu Thr Pro Pro Thr Val 355 360 365 Pro Val Leu Leu Gln Ile Leu Ser Gly Thr His Asn Ala Gln Asp Leu 370 375 380 Leu Pro Ala Gly Ser Val Ile Glu Leu Glu Gln Asn Lys Val Val Glu 385 390 395 400 Ile Val Leu Pro Ala Ala Gly Ala Val Gly Gly Pro His Pro Phe His 405 410 415 Leu His Gly His Asn Phe Trp Val Val Arg Ser Ala Gly Gln Thr Thr 420 425 430 Tyr Asn Phe Asn Asp Ala Pro Ile Arg Asp Val Val Ser Ile Gly Gly 435 440 445 Ala Asn Asp Gln Val Thr Ile Arg Phe Val Thr Asp Asn Pro Gly Pro 450 455 460 Trp Phe Leu His Cys His Ile Asp Trp His Leu Glu Ala Gly Phe Ala 465 470 475 480 Val Val Phe Ala Glu Gly Ile Asn Gly Thr Ala Ala Ala Asn Pro Val 485 490 495 Pro Ala Ala Trp Asn Gln Leu Cys Pro Leu Tyr Asp Ala Leu Ser Pro 500 505 510 Gly Asp Thr 515 4515PRTCerrena unicolor 4Met Ser Leu Leu Arg Ser Leu Thr Ser Leu Ile Val Leu Ala Thr Gly 1 5 10 15 Ala Phe Ala Ala Ile Gly Pro Val Thr Asp Leu His Ile Val Asn Gln 20 25 30 Asn Leu Ala Pro Asp Gly Leu Asn Arg Pro Thr Val Leu Ala Gly Gly 35 40 45 Thr Phe Pro Gly Pro Leu Ile Arg Gly Asn Lys Gly Asp Asn Phe Lys 50 55 60 Ile Asn Val Ile Asp Asp Leu Thr Glu His Ser Met Leu Lys Ala Thr 65 70 75 80 Ser Ile His Trp His Gly Phe Phe Gln Lys Gly Thr Asn Trp Ala Asp 85 90 95 Gly Pro Ala Phe Val Thr Gln Cys Pro Ile Thr Ser Gly Asn Ala Phe 100 105 110 Leu Tyr Asp Phe Asn Val Pro Asp Gln Ala Gly Thr Phe Trp Tyr His 115 120 125 Ser His Leu Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Ala Phe Val 130 135 140 Val Tyr Asp Pro Asn Asp Pro Asn Lys Gln Leu Tyr Asp Val Asp Asn 145 150 155 160 Gly Asn Thr Val Ile Thr Leu Ala Asp Trp Tyr His Ala Leu Ala Gln 165 170 175 Thr Val Thr Gly Val Ala Val Ser Asp Ala Thr Leu Ile Asn Gly Leu 180 185 190 Gly Arg Ser Ala Thr Gly Pro Ala Asn Ala Pro Leu Ala Val Ile Ser 195 200 205 Val Glu Arg Asn Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile Ser Cys 210 215 220 Asp Pro Asn Phe Ile Phe Ser Ile Asp His His Pro Met Thr Val Ile 225 230 235 240 Glu Met Asp Gly Val Asn Thr Gln Ser Met Thr Val Asp Ser Ile Gln 245 250 255 Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val Met Gln Ala Asn Gln Pro 260 265 270 Val Gly Asn Tyr Trp Ile Arg Ala Lys Pro Asn Val Gly Asn Thr Thr 275 280 285 Phe Leu Gly Gly Leu Asn Ser Ala Ile Leu Arg Tyr Val Gly Ala Pro 290 295 300 Asp Gln Glu Pro Thr Thr Asp Gln Thr Pro Asn Ser Thr Pro Leu Val 305 310 315 320 Glu Ala Asn Leu Arg Pro Leu Val Tyr Thr Pro Val Pro Gly Gln Pro 325 330 335 Phe Pro Gly Gly Ala Asp Ile Val Lys Asn Leu Ala Leu Gly Phe Asn 340 345 350 Ala Gly Arg Phe Thr Ile Asn Gly Thr Ser Phe Thr Pro Pro Thr Val 355 360 365 Pro Val Leu Leu Gln Ile Leu Ser Gly Thr His Asn Ala Gln Asp Leu 370 375 380 Leu Pro Ala Gly Ser Val Ile Glu Leu Glu Gln Asn Lys Val Val Glu 385 390 395 400 Ile Val Leu Pro Ala Ala Gly Ala Val Gly Gly Pro His Pro Phe His 405 410 415 Leu His Gly His Asn Phe Trp Val Val Arg Ser Ala Gly Gln Thr Thr 420 425 430 Tyr Asn Phe Asn Asp Ala Pro Ile Arg Asp Val Val Ser Ile Gly Gly 435 440 445 Ala Asn Asp Gln Val Thr Ile Arg Phe Val Thr Asp Asn Pro Gly Pro 450 455 460 Trp Phe Leu His Cys His Ile Asp Trp His Leu Glu Ala Gly Phe Ala 465 470 475 480 Val Val Phe Ala Glu Gly Ile Asn Gly Thr Ala Ala Ala Asn Pro Val 485 490 495 Pro Ala Ala Trp Asn Gln Leu Cys Pro Leu Tyr Asp Ala Leu Ser Pro 500 505 510 Gly Asp Thr 515 5278PRTCerrena unicolor 5Met Ser Leu Leu Arg Ser Leu Thr Ser Leu Ile Val Leu Ala Thr Gly 1 5 10 15 Ala Phe Ala Ala Ile Gly Pro Val Thr Asp Leu His Ile Val Asn Gln 20 25 30 Asn Leu Ala Pro Asp Gly Phe Asn Arg Pro Thr Val Leu Ala Gly Gly 35 40 45 Thr Phe Pro Gly Pro Leu Ile Arg Gly Asn Lys Gly Asp Asn Phe Lys 50 55 60 Ile Asn Val Ile Asp Asp Leu Thr Glu His Ser Met Leu Lys Ala Thr 65 70 75 80 Ser Ile His Trp His Gly Phe Phe Gln Lys Gly Thr Asn Trp Ala Asp 85 90 95 Gly Pro Ala Phe Val Thr Gln Cys Pro Ile Thr Ser Gly Asn Ser Phe 100 105 110 Leu Tyr Asp Phe Asn Val Pro Asp Gln Ala Gly Thr Phe Trp Tyr His 115 120 125 Ser His Leu Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Ala Phe Val 130 135 140 Val Tyr Asp Pro Asn Asp Pro Asn Lys Gln Leu Tyr Asp Val Asp Asn 145 150 155 160 Gly Lys Thr Val Ile Thr Leu Ala Asp Trp Tyr His Ala Leu Ala Gln 165 170 175 Thr Val Thr Gly Val Ala Val Ser Asp Ala Thr Leu Ile Asn Gly Leu 180 185 190 Gly Arg Ser Ala Thr Gly Pro Ala Asn Ala Pro Leu Ala Val Ile Ser 195 200 205 Val Glu Arg Asn Lys Arg Tyr Arg Phe Arg Leu Val Ser

Ile Ser Cys 210 215 220 Asp Pro Asn Phe Ile Phe Ser Ile Asp His His Pro Met Thr Val Ile 225 230 235 240 Glu Met Asp Gly Val Asn Thr Gln Ser Met Thr Val Asp Ser Ile Gln 245 250 255 Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val Met Gln Ala Asn Gln Pro 260 265 270 Val Gly Asn Tyr Trp Ile 275 6246PRTCerrena unicolormisc_feature(60)..(60)Xaa can be any naturally occurring amino acid 6Ala Ile Gly Pro Val Ala Asp Leu His Ile Thr Asp Asp Thr Ile Ala 1 5 10 15 Pro Asp Gly Phe Ser Arg Pro Ala Val Leu Ala Gly Gly Gly Phe Pro 20 25 30 Gly Pro Leu Ile Thr Gly Asn Lys Gly Asp Ala Phe Lys Leu Asn Val 35 40 45 Ile Asp Glu Leu Thr Asp Ala Ser Met Leu Lys Xaa Thr Ser Ile His 50 55 60 Trp His Gly Phe Phe Gln Lys Gly Thr Asn Trp Ala Asp Gly Pro Ala 65 70 75 80 Phe Val Asn Gln Cys Pro Ile Thr Thr Gly Asn Ser Phe Leu Tyr Asp 85 90 95 Phe Gln Val Pro Asp Gln Ala Gly Thr Tyr Trp Tyr His Ser His Leu 100 105 110 Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Ala Phe Val Val Tyr Asp 115 120 125 Pro Ser Asp Pro His Lys Asp Leu Tyr Asp Val Asp Asp Glu Ser Thr 130 135 140 Val Ile Thr Leu Ala Asp Trp Tyr His Thr Leu Ala Arg Gln Ile Val 145 150 155 160 Gly Val Ala Ile Ser Asp Thr Thr Leu Ile Asn Gly Leu Gly Arg Asn 165 170 175 Thr Asn Gly Pro Ala Asp Ala Ala Leu Ala Val Ile Asn Val Asp Ala 180 185 190 Gly Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile Ser Cys Asp Pro Asn 195 200 205 Trp Val Phe Ser Ile Asp Asn His Asp Phe Thr Val Ile Glu Val Asp 210 215 220 Gly Val Asn Ser Gln Pro Leu Asn Val Asp Ser Val Gln Ile Phe Ala 225 230 235 240 Gly Gln Arg Tyr Ser Phe 245 7526PRTCerrena unicolor 7Met Gly Leu Asn Ser Ala Ile Thr Ser Leu Ala Ile Leu Ala Leu Ser 1 5 10 15 Val Gly Ser Tyr Ala Ala Ile Gly Pro Val Ala Asp Ile His Ile Val 20 25 30 Asn Lys Asp Leu Ala Pro Asp Gly Val Gln Arg Pro Thr Val Leu Ala 35 40 45 Gly Gly Thr Phe Pro Gly Thr Leu Ile Thr Gly Gln Lys Gly Asp Asn 50 55 60 Phe Gln Leu Asn Val Ile Asp Asp Leu Thr Asp Asp Arg Met Leu Thr 65 70 75 80 Pro Thr Ser Ile His Trp His Gly Phe Phe Gln Lys Gly Thr Ala Trp 85 90 95 Ala Asp Gly Pro Ala Phe Val Thr Gln Cys Pro Ile Ile Ala Asp Asn 100 105 110 Ser Phe Leu Tyr Asp Phe Asp Val Pro Asp Gln Ala Gly Thr Phe Trp 115 120 125 Tyr His Ser His Leu Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Ala 130 135 140 Phe Val Val Tyr Asp Pro Asn Asp Pro His Lys Asp Leu Tyr Asp Val 145 150 155 160 Asp Asp Gly Gly Thr Val Ile Thr Leu Ala Asp Trp Tyr His Val Leu 165 170 175 Ala Gln Thr Val Val Gly Ala Ala Thr Pro Asp Ser Thr Leu Ile Asn 180 185 190 Gly Leu Gly Arg Ser Gln Thr Gly Pro Ala Asp Ala Glu Leu Ala Val 195 200 205 Ile Ser Val Glu His Asn Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile 210 215 220 Ser Cys Asp Pro Asn Phe Thr Phe Ser Val Asp Gly His Asn Met Thr 225 230 235 240 Val Ile Glu Val Asp Gly Val Asn Thr Arg Pro Leu Thr Val Asp Ser 245 250 255 Ile Gln Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val Leu Asn Ala Asn 260 265 270 Gln Pro Glu Asp Asn Tyr Trp Ile Arg Ala Met Pro Asn Ile Gly Arg 275 280 285 Asn Thr Thr Thr Leu Asp Gly Lys Asn Ala Ala Ile Leu Arg Tyr Lys 290 295 300 Asn Ala Ser Val Glu Glu Pro Lys Thr Val Gly Gly Pro Ala Gln Ser 305 310 315 320 Pro Leu Asn Glu Ala Asp Leu Arg Pro Leu Val Pro Ala Pro Val Pro 325 330 335 Gly Asn Ala Val Pro Gly Gly Ala Asp Ile Asn His Arg Leu Asn Leu 340 345 350 Thr Phe Ser Asn Gly Leu Phe Ser Ile Asn Asn Ala Ser Phe Thr Asn 355 360 365 Pro Ser Val Pro Ala Leu Leu Gln Ile Leu Ser Gly Ala Gln Asn Ala 370 375 380 Gln Asp Leu Leu Pro Thr Gly Ser Tyr Ile Gly Leu Glu Leu Gly Lys 385 390 395 400 Val Val Glu Leu Val Ile Pro Pro Leu Ala Val Gly Gly Pro His Pro 405 410 415 Phe His Leu His Gly His Asn Phe Trp Val Val Arg Ser Ala Gly Ser 420 425 430 Asp Glu Tyr Asn Phe Asp Asp Ala Ile Leu Arg Asp Val Val Ser Ile 435 440 445 Gly Ala Gly Thr Asp Glu Val Thr Ile Arg Phe Val Thr Asp Asn Pro 450 455 460 Gly Pro Trp Phe Leu His Cys His Ile Asp Trp His Leu Glu Ala Gly 465 470 475 480 Leu Ala Ile Val Phe Ala Glu Gly Ile Asn Gln Thr Ala Ala Ala Asn 485 490 495 Pro Thr Pro Gln Ala Trp Asp Glu Leu Cys Pro Lys Tyr Asn Gly Leu 500 505 510 Ser Ala Ser Gln Lys Val Lys Pro Lys Lys Gly Thr Ala Ile 515 520 525 8526PRTCerrena unicolor 8Met Gly Leu Asn Ser Ala Ile Thr Ser Leu Ala Ile Leu Ala Leu Ser 1 5 10 15 Val Gly Ser Tyr Ala Ala Ile Gly Pro Val Ala Asp Ile His Ile Val 20 25 30 Asn Lys Asp Leu Ala Pro Asp Gly Val Gln Arg Pro Thr Val Leu Ala 35 40 45 Gly Gly Thr Phe Pro Gly Thr Leu Ile Thr Gly Gln Lys Gly Asp Asn 50 55 60 Phe Gln Leu Asn Val Ile Asp Asp Leu Thr Asp Asp Arg Met Leu Thr 65 70 75 80 Pro Thr Ser Ile His Trp His Gly Phe Phe Gln Lys Gly Thr Ala Trp 85 90 95 Ala Asp Gly Pro Ala Phe Val Thr Gln Cys Pro Ile Ile Ala Asp Asn 100 105 110 Ser Phe Leu Tyr Asp Phe Asp Val Pro Asp Gln Ala Gly Thr Phe Trp 115 120 125 Tyr His Ser His Leu Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Ala 130 135 140 Phe Val Val Tyr Asp Pro Asn Asp Pro His Lys Asp Leu Tyr Asp Val 145 150 155 160 Asp Asp Gly Gly Thr Val Ile Thr Leu Ala Asp Trp Tyr His Val Leu 165 170 175 Ala Gln Thr Val Val Gly Ala Ala Thr Pro Asp Ser Thr Leu Ile Asn 180 185 190 Gly Leu Gly Arg Ser Gln Thr Gly Pro Ala Asp Ala Glu Leu Ala Val 195 200 205 Ile Ser Val Glu His Asn Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile 210 215 220 Ser Cys Asp Pro Asn Phe Thr Phe Ser Val Asp Gly His Asn Met Thr 225 230 235 240 Val Ile Glu Val Asp Gly Val Asn Thr Arg Pro Leu Thr Val Asp Ser 245 250 255 Ile Gln Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val Leu Asn Ala Asn 260 265 270 Gln Pro Asp Asp Asn Tyr Trp Ile Arg Ala Met Pro Asn Ile Gly Arg 275 280 285 Asn Thr Thr Thr Leu Asp Gly Lys Asn Ala Ala Ile Leu Arg Tyr Lys 290 295 300 Asn Ala Ser Val Glu Glu Pro Lys Thr Val Gly Gly Pro Ala Gln Ser 305 310 315 320 Pro Leu Asn Glu Ala Asp Leu Arg Pro Leu Val Pro Ala Pro Val Pro 325 330 335 Gly Asn Ala Val Pro Gly Gly Ala Asp Ile Asn His Arg Leu Asn Leu 340 345 350 Thr Phe Ser Asn Gly Leu Phe Ser Ile Asn Asn Ala Ser Phe Thr Asn 355 360 365 Pro Ser Val Pro Ala Leu Leu Gln Ile Leu Ser Gly Ala Gln Asn Ala 370 375 380 Gln Asp Leu Leu Pro Thr Gly Ser Tyr Ile Gly Leu Glu Leu Gly Lys 385 390 395 400 Val Val Glu Leu Val Ile Pro Pro Leu Ala Val Gly Gly Pro His Pro 405 410 415 Phe His Leu His Gly His Asn Phe Trp Val Val Arg Ser Ala Gly Ser 420 425 430 Asp Glu Tyr Asn Phe Asp Asp Ala Ile Leu Arg Asp Val Val Ser Ile 435 440 445 Gly Ala Gly Thr Asp Glu Val Thr Ile Arg Phe Val Thr Asp Asn Pro 450 455 460 Gly Pro Trp Phe Leu His Cys His Ile Asp Trp His Leu Glu Ala Gly 465 470 475 480 Leu Ala Ile Val Phe Ala Glu Gly Ile Asn Gln Thr Ala Ala Ala Asn 485 490 495 Pro Thr Pro Gln Ala Trp Asp Glu Leu Cys Pro Lys Tyr Asn Gly Leu 500 505 510 Ser Ala Ser Gln Lys Val Lys Pro Lys Lys Gly Thr Ala Ile 515 520 525 9262PRTCerrena unicolor 9Ala Ile Gly Pro Val Ala Asp Leu Lys Ile Val Asn Arg Asp Ile Ala 1 5 10 15 Pro Asp Gly Phe Ile Arg Pro Ala Val Leu Ala Gly Gly Ser Phe Pro 20 25 30 Gly Pro Leu Ile Thr Gly Gln Lys Gly Asn Glu Phe Lys Ile Asn Val 35 40 45 Val Asn Gln Leu Thr Asp Gly Ser Met Leu Lys Ser Thr Ser Ile His 50 55 60 Trp His Gly Phe Phe Gln Lys Gly Thr Asn Trp Ala Asp Gly Pro Ala 65 70 75 80 Phe Val Asn Gln Cys Pro Ile Ala Thr Asn Asn Ser Phe Leu Tyr Gln 85 90 95 Phe Thr Ser Gln Glu Gln Pro Gly Thr Phe Trp Tyr His Ser His Leu 100 105 110 Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Pro Leu Val Val Tyr Asp 115 120 125 Pro Gln Asp Pro His Ala Val Leu Tyr Asp Val Asp Asp Glu Ser Thr 130 135 140 Ile Ile Thr Leu Ala Asp Trp Tyr His Thr Leu Ala Arg Gln Val Lys 145 150 155 160 Gly Pro Ala Val Pro Gly Thr Thr Leu Ile Asn Gly Leu Gly Arg His 165 170 175 Asn Asn Gly Pro Leu Asp Ala Glu Leu Ala Val Ile Ser Val Gln Ala 180 185 190 Gly Lys Arg Gln Val Gln Phe Thr Leu Phe Thr Leu Tyr Arg Phe Arg 195 200 205 Leu Ile Ser Ile Ser Cys Asp Pro Asn Tyr Val Phe Ser Ile Asp Gly 210 215 220 His Asp Met Thr Val Ile Glu Val Asp Ser Val Asn Ser Gln Pro Leu 225 230 235 240 Lys Val Asp Ser Ile Gln Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val 245 250 255 Leu Asn Ala Asn Gln Pro 260 10526PRTArtificial SequenceSynthesized sequence 10Met Gly Leu Asn Ser Ala Ile Thr Ser Leu Ala Ile Leu Ala Leu Ser 1 5 10 15 Val Gly Ser Tyr Ala Ala Ile Gly Pro Val Ala Asp Leu His Ile Val 20 25 30 Asn Lys Asp Leu Ala Pro Asp Gly Val Gln Arg Pro Thr Val Leu Ala 35 40 45 Gly Gly Thr Phe Pro Gly Thr Leu Ile Thr Gly Gln Lys Gly Asp Asn 50 55 60 Phe Gln Leu Asn Val Ile Asp Asp Leu Thr Asp Asp Arg Met Leu Thr 65 70 75 80 Pro Thr Ser Ile His Trp His Gly Phe Phe Gln Lys Gly Thr Ala Trp 85 90 95 Ala Asp Gly Pro Ala Phe Val Thr Gln Cys Pro Ile Ile Ala Asp Asn 100 105 110 Ser Phe Leu Tyr Asp Phe Asp Val Pro Asp Gln Ala Gly Thr Phe Trp 115 120 125 Tyr His Ser His Leu Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Ala 130 135 140 Phe Val Val Tyr Asp Pro Asn Asp Pro His Lys Asp Leu Tyr Asp Val 145 150 155 160 Asp Asp Gly Gly Thr Val Ile Thr Leu Ala Asp Trp Tyr His Val Leu 165 170 175 Ala Gln Thr Val Val Gly Ala Ala Thr Pro Asp Ser Thr Leu Ile Asn 180 185 190 Gly Leu Gly Arg Ser Gln Thr Gly Pro Ala Asp Ala Glu Leu Ala Val 195 200 205 Ile Ser Val Glu His Asn Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile 210 215 220 Ser Cys Asp Pro Asn Phe Thr Phe Ser Val Asp Gly His Asn Met Thr 225 230 235 240 Val Ile Glu Val Asp Gly Val Asn Thr Arg Pro Leu Thr Val Asp Ser 245 250 255 Ile Gln Ile Phe Ala Gly Gln Arg Tyr Ser Phe Val Leu Asn Ala Asn 260 265 270 Gln Pro Glu Asp Asn Tyr Trp Ile Arg Ala Met Pro Asn Ile Gly Arg 275 280 285 Asn Thr Thr Thr Leu Asp Gly Lys Asn Ala Ala Ile Leu Arg Tyr Lys 290 295 300 Asn Ala Ser Val Glu Glu Pro Lys Thr Val Gly Gly Pro Ala Gln Ser 305 310 315 320 Pro Leu Asn Glu Ala Asp Leu Arg Pro Leu Val Pro Ala Pro Val Pro 325 330 335 Gly Asn Ala Val Pro Gly Gly Ala Asp Ile Asn His Arg Leu Asn Leu 340 345 350 Thr Phe Ser Asn Gly Leu Phe Ser Ile Asn Asn Ala Ser Phe Thr Asn 355 360 365 Pro Ser Val Pro Ala Leu Leu Gln Ile Leu Ser Gly Ala Gln Asn Ala 370 375 380 Gln Asp Leu Leu Pro Thr Gly Ser Tyr Ile Gly Leu Glu Leu Gly Lys 385 390 395 400 Val Val Glu Leu Val Ile Pro Pro Leu Ala Val Gly Gly Pro His Pro 405 410 415 Phe His Leu His Gly His Asn Phe Trp Val Val Arg Ser Ala Gly Ser 420 425 430 Asp Glu Tyr Asn Phe Asp Asp Ala Ile Leu Arg Asp Val Val Ser Ile 435 440 445 Gly Ala Gly Thr Asp Glu Val Thr Ile Arg Phe Val Thr Asp Asn Pro 450 455 460 Gly Pro Trp Phe Leu His Cys His Ile Asp Trp His Leu Glu Ala Gly 465 470 475 480 Leu Ala Ile Val Phe Ala Glu Gly Ile Asn Gln Thr Ala Ala Ala Asn 485 490 495 Pro Thr Pro Gln Ala Trp Asp Glu Leu Cys Pro Lys Tyr Asn Gly Leu 500 505 510 Ser Ala Ser Gln Lys Val Lys Pro Lys Lys Gly Thr Ala Ile 515 520 525 11505PRTArtificial SequenceSynthesized sequence 11Ala Ile Gly Pro Val Ala Asp Leu His Ile Val Asn Lys Asp Leu Ala 1 5 10 15 Pro Asp Gly Val Gln Arg Pro Thr Val Leu Ala Gly Gly Thr Phe Pro 20 25 30 Gly Thr Leu Ile Thr Gly Gln Lys Gly Asp Asn Phe Gln Leu Asn Val 35 40 45 Ile Asp Asp Leu Thr Asp Asp Arg Met Leu Thr Pro Thr Ser Ile His 50 55 60 Trp His Gly Phe Phe Gln Lys Gly Thr Ala Trp Ala Asp Gly Pro Ala 65 70 75 80 Phe Val Thr Gln Cys Pro Ile Ile Ala Asp Asn Ser Phe Leu Tyr Asp 85 90 95 Phe Asp Val Pro Asp Gln Ala Gly Thr Phe Trp Tyr His Ser His Leu 100 105 110 Ser Thr Gln Tyr Cys Asp Gly Leu Arg Gly Ala Phe Val Val Tyr Asp 115

120 125 Pro Asn Asp Pro His Lys Asp Leu Tyr Asp Val Asp Asp Gly Gly Thr 130 135 140 Val Ile Thr Leu Ala Asp Trp Tyr His Val Leu Ala Gln Thr Val Val 145 150 155 160 Gly Ala Ala Thr Pro Asp Ser Thr Leu Ile Asn Gly Leu Gly Arg Ser 165 170 175 Gln Thr Gly Pro Ala Asp Ala Glu Leu Ala Val Ile Ser Val Glu His 180 185 190 Asn Lys Arg Tyr Arg Phe Arg Leu Val Ser Ile Ser Cys Asp Pro Asn 195 200 205 Phe Thr Phe Ser Val Asp Gly His Asn Met Thr Val Ile Glu Val Asp 210 215 220 Gly Val Asn Thr Arg Pro Leu Thr Val Asp Ser Ile Gln Ile Phe Ala 225 230 235 240 Gly Gln Arg Tyr Ser Phe Val Leu Asn Ala Asn Gln Pro Glu Asp Asn 245 250 255 Tyr Trp Ile Arg Ala Met Pro Asn Ile Gly Arg Asn Thr Thr Thr Leu 260 265 270 Asp Gly Lys Asn Ala Ala Ile Leu Arg Tyr Lys Asn Ala Ser Val Glu 275 280 285 Glu Pro Lys Thr Val Gly Gly Pro Ala Gln Ser Pro Leu Asn Glu Ala 290 295 300 Asp Leu Arg Pro Leu Val Pro Ala Pro Val Pro Gly Asn Ala Val Pro 305 310 315 320 Gly Gly Ala Asp Ile Asn His Arg Leu Asn Leu Thr Phe Ser Asn Gly 325 330 335 Leu Phe Ser Ile Asn Asn Ala Ser Phe Thr Asn Pro Ser Val Pro Ala 340 345 350 Leu Leu Gln Ile Leu Ser Gly Ala Gln Asn Ala Gln Asp Leu Leu Pro 355 360 365 Thr Gly Ser Tyr Ile Gly Leu Glu Leu Gly Lys Val Val Glu Leu Val 370 375 380 Ile Pro Pro Leu Ala Val Gly Gly Pro His Pro Phe His Leu His Gly 385 390 395 400 His Asn Phe Trp Val Val Arg Ser Ala Gly Ser Asp Glu Tyr Asn Phe 405 410 415 Asp Asp Ala Ile Leu Arg Asp Val Val Ser Ile Gly Ala Gly Thr Asp 420 425 430 Glu Val Thr Ile Arg Phe Val Thr Asp Asn Pro Gly Pro Trp Phe Leu 435 440 445 His Cys His Ile Asp Trp His Leu Glu Ala Gly Leu Ala Ile Val Phe 450 455 460 Ala Glu Gly Ile Asn Gln Thr Ala Ala Ala Asn Pro Thr Pro Gln Ala 465 470 475 480 Trp Asp Glu Leu Cys Pro Lys Tyr Asn Gly Leu Ser Ala Ser Gln Lys 485 490 495 Val Lys Pro Lys Lys Gly Thr Ala Ile 500 505

Claims

1. A textile processing method, comprising contacting a portion of dyed textile with a laccase enzyme system for a length of time and under conditions sufficient to cause a localized color modification to the portion of the textile.

2. The method of claim 1, wherein the method is performed by wetting but not submerging the portion of the dyed textile with a composition comprising the laccase enzyme system.

3. The method of claim 1, wherein the method is performed by applying a composition comprising the laccase enzyme system to the portion of the dyed textile, and then wetting but not submerging the portion of the dyed textile.

4. The method of claim 1, wherein the laccase enzyme system is provided in a single composition.

5. The method of claim 1, wherein the laccase enzyme system is provided as an aqueous, gel, semi-solid, or solid formulation.

6. The method of claim 1, wherein the color modification is selected from lightening of color, change of color, change in color cast, and bleaching.

7. The method of claim 1, wherein the textile is indigo-dyed denim.

8. The method of claim 1, wherein the textile is indigo and sulfur-dyed denim.

9. The method of claim 1, wherein the textile is a pair of jeans.

10. The method of claim 1, wherein the portion of the textile is a pant leg, sleeve, cuff, collar, pocket, or belt loop.

11. The method of claim 1, wherein the portion of the textile is in the form of a predetermined shape.

12. The method of claim 1, wherein the portion of the textile is in the form of a letter, word, logo, or trademark.

13. The method of claim 1, wherein the laccase enzyme system comprises a laccase enzyme and a mediator.

14. The method of claim 13, wherein the laccase is a microbial laccase.

15. The method of claim 14, wherein the laccase is from a Cerrena species.

16. The method of claim 15, wherein the laccase is from Cerrena unicolor.

17. The method of claim 16, wherein the laccase is laccase D from C. unicolor.

18. The method of claim 13, wherein the mediator is syringonitrile.

19. The method of claim 1, wherein the method is performed at a temperature of from about 20.degree. C. to about 40.degree. C.

20. The method of claim 1, wherein the method is performed at a temperature of from about 20.degree. C. to about 30.degree. C.

21. The method of claim 1, wherein the method is performed at the ambient temperature of tap water.

22. The method of claim 1, wherein the method is performed at ambient air temperature.

23. A locally color-modified dyed textile produced by claim 1.

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