US20120088291A1 - Enzymatic Textile Colour Modification - Google Patents

Enzymatic Textile Colour Modification Download PDF

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Publication number
US20120088291A1
US20120088291A1 US13/321,840 US201013321840A US2012088291A1 US 20120088291 A1 US20120088291 A1 US 20120088291A1 US 201013321840 A US201013321840 A US 201013321840A US 2012088291 A1 US2012088291 A1 US 2012088291A1
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Prior art keywords
perhydrolase
enzymatic
textile
hydrogen peroxide
treatment composition
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US13/321,840
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English (en)
Inventor
Lode Vermeersch
Erwin Redling
Wayne Ashton
Christopher C. Barnett
Andreas Jacobus Johanna Krouwer
Piera Pericu
Rafael F. Sala
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Huntsman International LLC
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Huntsman International LLC
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Priority to US13/321,840 priority Critical patent/US20120088291A1/en
Assigned to HUNTSMAN INTERNATIONAL LLC reassignment HUNTSMAN INTERNATIONAL LLC ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: ASHTON, WAYNE, REDLING, ERWIN, VERMEERSCH, LODE, KROUWER, ANDREAS JACOBUS JOHANNA, PERICU, PIERA, BARNETT, CHRISTOPHER C., SALA, RAFAEL F.
Publication of US20120088291A1 publication Critical patent/US20120088291A1/en
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    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/39—Organic or inorganic per-compounds
    • C11D3/3947—Liquid compositions
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D11/00—Special methods for preparing compositions containing mixtures of detergents
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2093—Esters; Carbonates
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38654—Preparations containing enzymes, e.g. protease or amylase containing oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/39—Organic or inorganic per-compounds
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
    • D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
    • 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
    • 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 invention relates to methods for the enzymatic colour modification of dyed cellulosic textile fibre material, in particular denim dyed with indigo or sulphide dyes.
  • Some textile materials are washed after dyeing with the objective of adjusting the colour tone or shade on the dyed textile, also known as washdown effect.
  • blue jeans made from indigo-dyed denim can be washed in the presence of pumice stones and enzymatic desizing agents, followed by an on tone-washdown process to obtain a desired worn appearance.
  • Washdown with hydrogen peroxide is an alternative solution.
  • the adjusting effect obtainable with hydrogen peroxide is rather limited.
  • the required high pH is ecologically undesirable.
  • the present invention accordingly relates to a method for adjusting the colour tone of dyed cellulosic textile fibre material comprising contacting said textile material with an enzymatic textile treatment composition comprising
  • a perhydrolase enzyme (i) a perhydrolase enzyme, (ii) an ester substrate for said perhydrolase enzyme, and (iii) a hydrogen peroxide source.
  • the enzymatic treatment step of the present invention will employ, unless otherwise indicated, conventional techniques of molecular biology (including recombinant techniques), microbiology, cell biology, and biochemistry, which are within the skill of the art. Such techniques are explained fully in the literature, for example, Molecular Cloning: A Laboratory Manual, 2 nd ed., (Sambrook et al., 1989); Oligonucleotide Synthesis (M. J. Gait, ed., 1984); Current Protocols in Molecular Biology (F. M. Ausubel et al, eds., 1994); PCR: The Polymerase Chain Reaction (Mullis et al., eds., 1994); and Gene Transfer and Expression: A Laboratory Manual (Kriegler, 1990).
  • nucleic acids are written left to right in 5′ to 3′ orientation; amino acid sequences are written left to right in amino to carboxy orientation, respectively.
  • adjusting means the process of treating a textile material for a sufficient length of time and under appropriate pH and temperature conditions to produce a lighter colour in said textile material by removal, modification or masking of color-causing compounds in the textile material.
  • adjusting refers to the treatment of a textile material to effect a brightening of the textile material.
  • cellulosic textile fibre material comprises natural cellulosic fibres such as cotton, linen and hemp, semi-synthetic cellulosic fibres such as viscose and lyocell as well as blends of cellulosic fibres and synthetic fibres such as elastane.
  • the method according to the invention is particularly suitable for the treatment of denim dyed with vat dyes, reactive dyes, direct dyes and sulphur dyes, most preferably for indigo-dyed denim.
  • Suitable substrates that can be treated with the method according to the invention are yarns, wovens, knits and garments.
  • the method according to the invention provides textile material distinguishing by soft handle and very good crease recovery properties.
  • a “perhydrolase” refers to an enzyme that is capable of catalyzing a perhydrolysis reaction that results in the production of a sufficiently high amount of peracid suitable for use in an enzymatic textile adjusting composition according to the method described herein.
  • a perhydrolase enzyme used in the methods described herein 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 acyl transferase activity and catalyzes an aqueous acyl transfer reaction.
  • a “peracid” is an organic acid of the formula RC( ⁇ O)OOH, wherein R is an aliphatic, aromatic or araliphatic radical.
  • esters substrate in reference to an enzymatic textile adjusting composition according to the invention described herein refers to a perhydrolase substrate that contains an ester linkage.
  • Esters comprising aliphatic and/or aromatic carboxylic acids and alcohols may be utilized as substrates with perhydrolase enzymes.
  • 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.
  • 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, glycerol triacetate, ethyl acetate, and glycerol tributyrate.
  • perhydrolyzation or “perhydrolyze” or “perhydrolysis” as used herein refer to a reaction wherein a peracid is generated from an ester substrate and a hydrogen peroxide source.
  • the perhydrolyzation reaction is catalyzed with a perhydrolase, e.g., acyl transferase or aryl esterase, enzyme.
  • a peracid is produced by perhydrolysis of an ester substrate of the formula RC( ⁇ O)OR*, where R and R* are the same or different organic moieties, in the presence of hydrogen peroxide (H 2 O 2 ).
  • —OR* is —OH.
  • —OR* is replaced by —NH 2 .
  • a peracid is produced by perhydrolysis of a carboxylic acid or amide substrate.
  • peracid refers to a molecule derived from a carboxylic acid ester which has been reacted with hydrogen peroxide to form a highly reactive product that is able to transfer one of its oxygen atoms. It is this ability to transfer oxygen atoms that enables a peracid, for example, peracetic acid, to function as a brightening agent.
  • perhydrolysis to hydrolysis ratio refers to the ratio of the amount of enzymatically produced peracid to the amount of enzymatically produced acid 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.
  • an effective amount of perhydrolase enzyme refers to the quantity of perhydrolase enzyme necessary to achieve the enzymatic activity required in the processes or methods described herein. Such effective amounts are readily ascertained by one of ordinary skill in the art and are based on many 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 brightening).
  • 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.
  • 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., ethanoyl chloride, CH 3 CO—Cl, is the acyl chloride formed from ethanoic 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.
  • oxidizing chemical refers to a chemical that has the capability of brightening a textile.
  • the oxidizing chemical is present at an amount, pH and temperature suitable for brightening.
  • the term includes, but is not limited to hydrogen peroxide and peracids.
  • 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. Because the genetic code is degenerate, more than one codon may be used to encode a particular amino acid, and the polynucleotides applied applied within the context of the present invention encode a particular amino acid sequence.
  • any type of modified nucleotide or nucleotide analog may be used, so long as the polynucleotide retains the desired functionality under conditions of use, including modifications that increase nuclease resistance (e.g., deoxy, 2′-O-Me, phosphorothioates, etc.).
  • Labels may also be incorporated for purposes of detection or capture, for example, radioactive or nonradioactive labels or anchors, e.g., biotin.
  • polynucleotide also includes peptide nucleic acids (PNA). Polynucleotides may be naturally occurring or non-naturally occurring.
  • Polynucleotide and “nucleic acid” and “oligonucleotide” are used herein interchangeably.
  • Polynucleotides of the invention may contain RNA, DNA, or both, and/or modified forms and/or analogs thereof.
  • a sequence of nucleotides may be interrupted by non-nucleotide components.
  • One or more phosphodiester linkages may be replaced by alternative linking groups.
  • linking groups include, but are not limited to, embodiments wherein phosphate is replaced by P(O)S (“thioate”), P(S)S (“dithioate”), (O)NR 2 (“amidate”), P(O)R, P(O)OR′, CO or CH 2 (“formacetal”), in which each R or R′ is independently H or substituted or unsubstituted alkyl (C 1 -C 20 ) optionally containing an ether (—O—) linkage, aryl, alkenyl, cycloalkyl, cycloalkenyl or araldyl. Not all linkages in a polynucleotide need be identical.
  • Polynucleotides may be linear or circular or comprise a combination of linear and circular portions. Suitable polynucleotides are described in WO 2005/056782.
  • polypeptide refers to any composition comprised of amino acids 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.
  • homologous proteins are familiar to those skilled in the art and are described in more detail in WO 2005/056782 on pages 12, 13 and 50 to 52, which are herein incorporated by reference.
  • homologous proteins are engineered to produce enzymes with desired activity(ies).
  • the degree of homology between sequences may be determined using any suitable method known in the art.
  • PILEUP is a useful program to determine sequence homology levels. PILEUP creates a multiple sequence alignment from a group of related sequences using progressive, pairwise alignments. It can also plot a tree showing the clustering relationships used to create the alignment.
  • Another example of a useful algorithm is the BLAST algorithm. Useful methods and programs are referred to in WO 2005/056782 on pages 59 and 60, which are herein incorporated by reference.
  • “Surfactant” refers to a substance that reduces surface tension of a liquid.
  • Emmulsifier refers to a substance that promotes the suspension of one liquid in another.
  • “Sequestering agent” refers to a substance capable of reacting with metallic ions by forming a water-soluble complex in which the metal is held in a non-ionizable form.
  • Catalase refers to an enzyme (i.e., a polypeptide having catalytic activity) that catalyzes the decomposition of hydrogen peroxide to water and oxygen.
  • Batch process or “batchwise process” or “discontinuous process” or “exhaust process” refers to processing of textiles as lots or batches in which the whole of each batch is subjected to a process or one stage of a process at a time.
  • Liquor ratio refers to the ratio of the weight of liquor (liquid) employed in a textile treatment process to the weight of the textile treated.
  • the enzymatic textile adjusting methods described herein are particularly carried out as a discontinuous process but can also be carried out as a semi-continuous process like pad-batch or pad-roll.
  • the enzymatic colour tone adjusting composition used in accordance with the enzymatic textile adjusting method of the present invention contain a perhydrolase enzyme, an ester substrate for the perhydrolase enzyme suitable for production of a peracid upon catalytic reaction of the perhydrolase enzyme on the substrate in the presence of a hydrogen peroxide source and/or hydrogen peroxide.
  • the enzymatic colour tone adjusting composition may, optionally, further contain a surfactant and/or an emulsifier, a peroxide stabilizer, a fluorescence whitening agent, an enzymatic desizing agent, a biopolishing agent, a combination product, a sequestering agent or a buffer which maintains a pH of about 6 to about 8 during a textile colour tone adjusting process.
  • One or more perhydrolase enzymes may be used in the compositions according to the methods for enzymatic textile colour tone adjusting as described herein.
  • the perhydrolase enzyme is naturally-occurring (i.e., a perhydrolase enzyme encoded by a genome of a cell).
  • the perhydrolase enzyme comprises, consists of, or consists essentially of an amino acid sequence that is at least about 80%, 85%, 90%, 95%, 97%, 98%, 99%, or 99.5% identical to the amino acid sequence of a naturally-occurring perhydrolase enzyme.
  • the perhydrolase enzyme is a naturally-occurring M. smegmatis perhydrolase enzyme.
  • the 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 80%, 85%, 90%, 95%, 97%, 98%, 99%, or 99.5% identical to the amino acid sequence set forth in SEQ ID NO:1.
  • M. smegmatis perhydrolase The amino acid sequence of M. smegmatis perhydrolase is shown below:
  • 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 sequence set forth in SEQ ID NO:1.
  • the perhydrolase enzyme comprises any one or any combination of substitutions of amino acids selected from M1, K3, R4, I5, L6, C7, D10, S11, L12, T13, W14, W16, G15, V17, P18, V19, O21, G22, A23, P24, I25, E26, R27, F28, A29, P30, D31, V32, R33, W34, T35, G36, L38, Q40, Q41, D45, L42, G43, A44, F46, E47, V48, I49, E50, E51, G52, L53, S54, A55, R56, T57, T58, N59, I60, D61, D62, P63, T64, D65, P66
  • the perhydrolase enzyme comprises one or more of the following substitutions at one or more amino acid positions equivalent to position(s) in the M. smegmatis perhydrolase amino acid sequence set forth in SEQ ID NO:1: L12C, Q, or G; 125S, G, or P; L53H, Q, G, or S; S54V, L A, P, T, or R; A55G or T; R67T, Q, N, G, E, L, or F; K97R; V125S, G, R, A, or P; F154Y; F196G.
  • the perhydrolase enzyme is the S54V variant of SEQ ID NO:1.
  • the perhydrolase enzyme comprises a combination of amino acid 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; S54V; L12Q T25S S54V; L53H S54V; S54P V125R; S54V V125G; S54V F196G; S54V K97R V125G; or A55G R67T K97R V125G.
  • the perhydrolase enzyme comprises a perhydrolysis to hydrolysis ratio of at least 1. In some embodiments, the perhydrolase enzyme comprises a perhydrolysis to hydrolysis ratio greater than 1.
  • the perhydrolase enzyme is provided in the enzymatic textile colour tone adjusting composition used according to the textile colour tone adjusting method of the present invention at a concentration of about 0.5 to about 2.5 ppm, about 1.5 to about 2.0 ppm, for example, about 1.7 ppm, based on the total weight of the aqueous composition (bath) applied for treatment of the textile material.
  • the enzymatic colour tone adjusting compositions used in accordance with the method described herein include an ester which 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.
  • 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.
  • glycerol triacetate, glycerol tributyrate, and other esters serve as acyl donors for peracid formation.
  • the ester substrate is selected from propylene glycol diacetate, ethylene glycol diacetate, glycerol triacetate, ethyl acetate, and glycerol tributyrate.
  • the ester substrate is propylene glycol diacetate, ethylene glycol diacetate, or ethyl acetate.
  • the ester substrate is propylene glycol diacetate.
  • the ester substrate for example, propylene glycol diacetate
  • the ester substrate is provided at a concentration of about 2000 to about 4000 ppm, about 2500 to about 3500 ppm, about 2800 ppm to about 3200 ppm, or about 3000 ppm, based on the total weight of the aqueous composition (bath) applied for treatment of the textile material.
  • the enzymatic colour tone adjusting compositions used in accordance with the method described herein include a hydrogen peroxide source.
  • Hydrogen peroxide can be either added directly in batch, or generated continuously “in situ” by chemical, electro-chemical, and/or enzymatic means.
  • the hydrogen peroxide source is hydrogen peroxide.
  • the hydrogen peroxide source is a solid compound that generates hydrogen peroxide spontaneously upon addition to water.
  • Such compounds include adducts of hydrogen peroxide with various inorganic or organic compounds, of which the most widely employed is sodium carbonate perhydrate, also referred to as sodium percarbonate.
  • Inorganic perhydrate salts are one embodiment of hydrogen peroxide source.
  • Examples of inorganic perhydrate salts include perborate, percarbonate, perphosphate, persulfate and persilicate salts.
  • the inorganic perhydrate salts are normally the alkali metal salts.
  • hydrogen peroxide adducts useful in the compositions used in accordance with the method described herein include adducts of hydrogen peroxide with zeolites, or urea hydrogen peroxide.
  • the hydrogen peroxide source compounds may be included as the crystalline and/or substantially pure solid without additional protection.
  • the preferred executions of such granular compositions utilize a coated form of the material 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, uri
  • any enzyme that generates H 2 O 2 with a suitable substrate may be used in the present invention.
  • lactate oxidases from Lactobacillus species which are known to create H 2 O 2 from lactic acid and oxygen may be used.
  • acid e.g., gluconic acid in the above example
  • One advantage of the enzymatic generation of acid is that this reduces the pH of a basic solution to the pH range in which a peracid is most effective in colour tone adjusting (i.e., at or below the pKa).
  • enzymes e.g., alcohol oxidase, ethylene glycol oxidase, glycerol oxidase, amino acid oxidase, etc.
  • ester substrates in combination with the perhydrolase enzymes of the present invention to generate peracids.
  • the hydrogen peroxide generating oxidase is a carbohydrate oxidase.
  • Hydrogen peroxide may also be generated electrochemically, for example using a fuel cell fed oxygen and hydrogen gas.
  • the hydrogen peroxide source is hydrogen peroxide provided at a concentration of about 1000 to about 3200 ppm, about 1500 to about 2800 ppm, about 2000 ppm to about 2200 ppm, or about 2100 ppm, based on the total weight of the aqueous composition (bath) applied for treatment of the textile material.
  • the enzymatic textile colour tone adjusting compositions used in accordance with the present method may contain one or more, i.e., at least one surfactant and/or at least one emulsifier.
  • Surfactants suitable for use in practicing the present invention include, without limitation, nonionic (see, e.g., U.S. Pat. No. 4,565,647, which is herein incorporated by reference); anionic; cationic; and zwitterionic surfactants (see, e.g., U.S. Pat. No. 3,929,678 which is herein incorporated by reference).
  • Anionic surfactants include, without limitation, linear alkylbenzenesulfonate, ⁇ -olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid, and soap.
  • Non-ionic surfactants include, without limitation, fatty alcohol ethoxylate, isotridecanol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, and N-acyl N-alkyl derivatives of glucosamine (“glucamides”).
  • the surfactant and/or emulsifier comprises a non-ionic surfactant.
  • the non-ionic surfactant is a fatty alcohol ethoxylate.
  • the non-ionic surfactant is isotridecanol ethoxylate.
  • the non-ionic surfactant is a fatty alcohol ethoxylate and isotridecanol ethoxylate.
  • the composition used in accordance with the present method comprises a surfactant and an emulsifier.
  • a surfactant may be present at a concentration of about 300 ppm to about 4800 ppm, about 600 ppm to about 3600 ppm, or about 300 ppm to about 1200 ppm, based on the total weight of the aqueous composition (bath) applied for treatment of the textile material.
  • the enzymatic colour tone adjusting composition contains isotridecanol ethoxylate at a concentration of about 300 ppm to about 3600 ppm, about 600 ppm to about 3000 ppm, or about 900 ppm to about 2400 ppm, based on the total weight of the aqueous composition (bath) applied for treatment of the textile material.
  • the enzymatic colour tone adjusting compositions used in accordance with the method described herein may contain a peroxide stabilizer.
  • peroxide stabilizers include, but are not limited to, sodium silicate, sodium carbonate, acrylic polymers, magnesium salts, and phosphonic acid.
  • the peroxide stabilizer is phosphonic acid.
  • a peroxide stabilizer may be present in the enzymatic textile colour tone adjusting composition at a concentration of about 60 ppm to about 600 ppm, about 60 ppm to about 1200 ppm, or about 120 ppm to about 960 ppm based on the total weight of the aqueous composition (bath) applied for treatment of the textile material.
  • At least one surfactant and/or emulsifier, at least one peroxide stabilizer and at least one sequestering agent are applied as a combination product containing each of at least one surfactant and/or emulsifier, at least one peroxide stabilizer and at least one sequestering agent.
  • the said combination product is designated bleaching processor and is commercially available, for example, CLARITE® LTC, CLARITE® WIN or CLARITE® ONE (products of Huntsman).
  • a surfactant may be present at a concentration of about 5% to about 40%, about 20% to about 30%, or about 5% to about 10%, based on the total weight of the bleaching processor.
  • a peroxide stabilizer may be present in the combination product at a concentration of about 1% to about 5%, about 1% to about 10%, or about 2% to about 8%, based on the total weight of the bleaching processor.
  • a sequestering agent may be present in the bleaching processor at a concentration of about 1% to about 15%, about 5% to about 10%, or about 3% to about 10%, based on the total weight of the bleaching processor.
  • the bleaching processor contains isotridecanol ethoxylate at a concentration of about 5% to about 30%, about 10% to about 25%, or about 15% to about 20%, based on the total weight of the bleaching processor.
  • the bleaching processor is suitably provided as an aqueous composition comprising the above indicated components.
  • the enzymatic colour tone adjusting composition may contain a buffer that is capable of maintaining the pH of the composition at a pH of about 6 to about 8.
  • the buffer may be, for example, a phosphate buffer, pH 7, or a sodium carbonate or potassium carbonate, pH 7.
  • the method of the invention utilizes a liquor ratio of about 2:1 to about 50:1, about 5:1 to about 20:1, for example, about 20:1 or 10:1.
  • Textiles are contacted with the enzymatic colour tone adjusting composition at a temperature of about 55° C. to about 75° C., about 60° C. to about 70° C., for a processing time of about 20 to about 60 minutes at a pH of about 6 to about 8.
  • the treatment temperature is about 65° C. and the processing time is about 50 minutes.
  • the temperature of the enzymatic colour tone adjusting composition is raised by about 2° C. per minute from a starting temperature of about 20° C. to about 50° C., for example, about 20° C. to about 40° C., until the processing temperature for colour tone adjusting is reached.
  • One or more rinsing steps are performed after treatment of the textile material with the enzymatic colour tone adjusting composition, to remove the colour tone adjusting composition.
  • the textile is rinsed with an aqueous composition (water or a composition containing water).
  • the rinsing temperature is about 40° C. to about 60° C., for example, about 50° C.
  • the aqueous rinsing composition contains a catalase enzyme to catalyze the decomposition of hydrogen peroxide to water and oxygen.
  • the textile is rinsed twice with a catalase containing aqueous composition for about 10 minutes for each rinse.
  • residual hydrogen peroxide is removed by rinsing twice with an aqueous composition containing catalase at about 50° C.
  • polyester substrates suitable for use in the present invention may be used, for example, pectinases, cutinases or lipases. These enzymes, their application as well as assays to determine enzyme activity are described and referred to in more detail in WO 2007/136469 on pages 21 and 22, which are herein incorporated by reference.
  • amylases deizing agents
  • cellulases biopolishing agents
  • a comparison between the method of the present invention and conventional oxidation bleach with hydrogen peroxide is performed according to the procedures given below by treating the fabric in exhaust using a Mathis AG Labomat.
  • Indigo dyed denim swatches (length: 11 cm, width: 9.5 cm), washed at 65° C./5 min and cold in overflow/5 min, are treated in a bath containing the combination product, the buffer, propylene glycol diacetate, hydrogen peroxide and the perhydrolase enzyme in the amounts given in Table 1 using a liquor ratio of 10:1.
  • the temperature is raised from ambient temperature to a target temperature of 65° C. at a rate of 2° C. per minute.
  • the bath is then held at 65° C. for 5 0 minutes and after cooling and draining the swatches are rinsed twice for 10 minutes each at 50° C. and then dried at 70° C.
  • 0.5 g/l of a 25% solution of Catalase T100 (available from Genencor) is included in each rinse.
  • Indigo dyed denim swatches (length: 11 cm, width: 9.5 cm), desized at 10:1 liquor ratio, 60° C./10 min, with 0.5 g/l CLARITE® WIN, 0.5 g/l Albfluid C and 1.5 g/l ULTRAVON® RW (non-ionic surfactant, commercial product supplied by Huntsman) are treated in the same bath with 1.5 g/l of INVAZYME® LTE (perhydrolase enzyme) at 10:1 liquor ratio, 60° C./10 min. Following desizing, the denim is stonewashed in a rotary washing machine with 1 kg of pumice stones (60° C./40 min).
  • Perhydrolase (PrimaGreen® EcoWhite 1 (321 U/g), available from Genencor Division, Danisco US, Inc.), is used in this experiment. H 2 O 2 analysis grade (30 wt %) and propylene glycol diacetate >99.7% (PDGA) were purchased from Sigma Aldrich.
  • Denim, 12 legs (ACG denim style 80270) weighing approximately 3 kg, is desized in a Unimac UF 50 washing machine under the following conditions:
  • the denim is stonewashed in a Unimac UF 50 rotary washing machine according to the following program:
  • the denim is dried in a household dryer and then used to make swatches (7 ⁇ 7 cm).
  • the denim swatches are evaluated after perhydrolase treatment with a Minolta Chromameter CR 310 in the CIE Lab color space with a D 65 light source. Measurements are done before and after perhydrolase treatment and the results from five swatches are averaged.
  • the denim swatches are evaluated after perhydrolase treatment with a Minolta Chromameter CR 310 in the CIE Lab color space with a D 65 light source. Measurements are done before and after perhydrolase treatment and the results from five swatches are averaged.
  • Denim, 12 legs (ACG denim style 80270) weighing approximately 3 kg, is desized and stonewashed as described in Example 5. After stonewashing, the experiments are performed in a Launder-O-meter (Rapid Laboratory Dyeing Machine type H12) according to the following process.
  • the denim swatches are evaluated after perhydrolase treatment with a Minolta Chromameter CR 310 in the CIE Lab color space with a D 65 light source. Measurements are done before and after perhydrolase treatment and the results from five swatches are averaged.
  • Denim, 12 legs (ACG denim style 80270) weighing approximately 3 kg, is desized and stonewashed as described in Example 5. After stonewashing, the experiments are performed in a Launder-O-meter (Rapid Laboratory Dyeing Machine type H12) according to the following process.
  • the denim swatches are evaluated after perhydrolase treatment with a Minolta Chromameter CR 310 in the CIE Lab color space with a D 65 light source. Measurements are done before and after perhydrolase treatment and the results from five swatches are averaged.
  • Denim, 12 legs (ACG denim style 80270) weighing approximately 3 kg, is desized in a Unimac UF 50 washing machine under the following conditions:
  • the denim is stonewashed in a Unimac UF 50 rotary washing machine according to the following procedure:
  • Denim, 12 legs (ACG denim style 80270) weighing approximately 3 kg, is desized in a Unimac UF 50 washing machine under the following conditions:
  • the denim is stonewashed in a Unimac UF 50 rotary washing machine according to the following procedure:
  • laccase treatment is performed in a Unimac UF 50 washing machine according to the following process:
  • the denim is dried in a household dryer
  • Brightening of denim legs is evaluated after laccase treatment and after perhydrolase treatment with a Minolta Chromameter CR 310 in the CIE Lab color space with a D 65 light source. For each denim leg, 8 measurements are taken and the results of the 12 legs (96 measurements) are averaged.
  • Perhydrolase S54V variant of M smegmatis , containing 1.5 mg/g active protein
  • Hydrogen peroxide analytical grade; 30% w/w
  • propylene glycol diacetate >99.7%
  • Standard dyed fabrics are obtained from the Center for Test Materials, Vlaardingen, The Netherlands.
  • the fabrics are dyed with one of the dyes (or combinations of dyes) listed in Table 15, which are identified by their Color Index (CI) number according to the Society of Dyers and Colourists (UK) and by the American Association of Textile Chemists and Colorists (USA).
  • CI Color Index
  • each swatches of dyed fabric (see Table 9) of approximately 12.5 cm ⁇ 12.5 cm are treated in a Launder-O-Meter (Rapid Laboratory Dyeing Machine type H12) according to the following procedure:
  • Incubation is carried out for 30 minutes. Following incubation, the swatches are rinsed by overflow, spin dried in an AEG IPX4 centrifuge, and dried in a Novotronic T 494 C household type dryer.
  • TCD Total color difference

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US8883485B2 (en) 2009-03-03 2014-11-11 Danisco Us Inc. Oxidative decolorization of dyes with enzymatically generated peracid method, composition and kit of parts
CN107524018A (zh) * 2017-06-14 2017-12-29 浙江银河印染有限公司 一种棉坯布活性染料染色后用阳离子染料修色的方法
US10011931B2 (en) 2014-10-06 2018-07-03 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing dyed and welded substrates
US10982381B2 (en) 2014-10-06 2021-04-20 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing welded substrates
US11085133B2 (en) 2016-05-03 2021-08-10 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing dyed and welded substrates
WO2022180341A1 (fr) * 2021-02-26 2022-09-01 Induo Procede de fabrication de textile teint fonctionnalise, utilisation d´une solution de blanchiment pour accroitre la tenue d´une fonctionnalisation chimique sur un textile teint, et textile teint
FR3120238A1 (fr) * 2021-02-26 2022-09-02 Induo Textile en coton hydrophobe et procede de fabrication de textile teint fonctionnalise
FR3120240A1 (fr) * 2021-02-26 2022-09-02 Induo Procede de fabrication de textile teint fonctionnalise
US11766835B2 (en) 2016-03-25 2023-09-26 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing welded substrates

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AR085810A1 (es) * 2011-03-17 2013-10-30 Danisco Us Inc Modificacion del color en telas que tienen apresto
CN102561008B (zh) * 2012-01-10 2014-01-29 江门市宝发纺织服饰制造有限公司 一种水洗牛仔替代浮石的环保生物粗花酶制剂及其应用
CN102899880A (zh) * 2012-11-08 2013-01-30 天津工业大学 一种利用多酶耦合作用提高棉及混纺织物漂白效果的方法
CN104131476A (zh) * 2014-07-11 2014-11-05 芜湖富春染织有限公司 一种筒子纱白色染色用料配方
WO2022271121A1 (en) * 2021-06-25 2022-12-29 Realkom Tekstil Urunleri Sanayi Pazarlama Ve Dis Ticaret Anonim Sirketi A new enzyme mixture and a denim washing method using thereof

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US20070167344A1 (en) * 2003-12-03 2007-07-19 Amin Neelam S Enzyme for the production of long chain peracid
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US8883485B2 (en) 2009-03-03 2014-11-11 Danisco Us Inc. Oxidative decolorization of dyes with enzymatically generated peracid method, composition and kit of parts
US20120149269A1 (en) * 2009-08-27 2012-06-14 Danisco Us Inc. Combined Textile Abrading And Color Modification
US11555263B2 (en) 2014-10-06 2023-01-17 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing dyed and welded substrates
US10011931B2 (en) 2014-10-06 2018-07-03 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing dyed and welded substrates
US10982381B2 (en) 2014-10-06 2021-04-20 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing welded substrates
US12091815B2 (en) 2014-10-06 2024-09-17 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing welded substrates
US11766835B2 (en) 2016-03-25 2023-09-26 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing welded substrates
US11085133B2 (en) 2016-05-03 2021-08-10 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing dyed and welded substrates
US11920263B2 (en) 2016-05-03 2024-03-05 Natural Fiber Welding, Inc. Methods, processes, and apparatuses for producing dyed and welded substrates
CN107524018A (zh) * 2017-06-14 2017-12-29 浙江银河印染有限公司 一种棉坯布活性染料染色后用阳离子染料修色的方法
WO2022180341A1 (fr) * 2021-02-26 2022-09-01 Induo Procede de fabrication de textile teint fonctionnalise, utilisation d´une solution de blanchiment pour accroitre la tenue d´une fonctionnalisation chimique sur un textile teint, et textile teint
FR3120238A1 (fr) * 2021-02-26 2022-09-02 Induo Textile en coton hydrophobe et procede de fabrication de textile teint fonctionnalise
FR3120240A1 (fr) * 2021-02-26 2022-09-02 Induo Procede de fabrication de textile teint fonctionnalise

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