WO1997025468A1 - Tissu traite avec de la cellulase et de l'oxydoreductase - Google Patents

Tissu traite avec de la cellulase et de l'oxydoreductase Download PDF

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Publication number
WO1997025468A1
WO1997025468A1 PCT/DK1997/000002 DK9700002W WO9725468A1 WO 1997025468 A1 WO1997025468 A1 WO 1997025468A1 DK 9700002 W DK9700002 W DK 9700002W WO 9725468 A1 WO9725468 A1 WO 9725468A1
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Prior art keywords
fabric
alkyl
process according
cellulase
enzyme
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PCT/DK1997/000002
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English (en)
Inventor
Thomas Vollmond
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Novo Nordisk A/S
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Application filed by Novo Nordisk A/S filed Critical Novo Nordisk A/S
Priority to BR9706965A priority Critical patent/BR9706965A/pt
Priority to JP52476397A priority patent/JP3977429B2/ja
Priority to DE69717486T priority patent/DE69717486T2/de
Priority to EP97900194A priority patent/EP0935692B1/fr
Priority to AU13667/97A priority patent/AU1366797A/en
Priority to PL97327815A priority patent/PL186471B1/pl
Publication of WO1997025468A1 publication Critical patent/WO1997025468A1/fr
Priority to US09/079,027 priority patent/US5908472A/en

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    • 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
    • D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
    • D06P1/44—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders
    • D06P1/64—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders using compositions containing low-molecular-weight organic compounds without sulfate or sulfonate groups
    • D06P1/651—Compounds without nitrogen
    • D06P1/65106—Oxygen-containing compounds
    • 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
    • C11D3/26—Organic compounds containing nitrogen
    • C11D3/28—Heterocyclic compounds containing nitrogen in the ring
    • 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
    • C11D3/34—Organic compounds containing sulfur
    • C11D3/349—Organic compounds containing sulfur additionally containing nitrogen atoms, e.g. nitro, nitroso, amino, imino, nitrilo, nitrile groups containing compounds or their derivatives or thio urea
    • 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
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
    • 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
    • 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
    • D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
    • D06P1/44—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders
    • D06P1/64—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders using compositions containing low-molecular-weight organic compounds without sulfate or sulfonate groups
    • D06P1/642—Compounds containing nitrogen
    • D06P1/6426—Heterocyclic compounds
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
    • D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
    • D06P1/44—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders
    • D06P1/64—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders using compositions containing low-molecular-weight organic compounds without sulfate or sulfonate groups
    • D06P1/651—Compounds without nitrogen
    • D06P1/65106—Oxygen-containing compounds
    • D06P1/65118—Compounds containing hydroxyl groups
    • 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
    • D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
    • D06P1/44—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders
    • D06P1/64—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders using compositions containing low-molecular-weight organic compounds without sulfate or sulfonate groups
    • D06P1/651—Compounds without nitrogen
    • D06P1/65168—Sulfur-containing compounds
    • D06P1/65193—Compounds containing sulfite or sulfone groups
    • 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
    • D06P5/02—After-treatment
    • 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
    • D06P5/02—After-treatment
    • D06P5/04—After-treatment with organic compounds
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
    • D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
    • D06P5/02—After-treatment
    • D06P5/04—After-treatment with organic compounds
    • D06P5/06—After-treatment with organic compounds containing nitrogen
    • 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
    • C11D3/34—Organic compounds containing sulfur
    • C11D3/3418—Toluene -, xylene -, cumene -, benzene - or naphthalene sulfonates or sulfates
    • 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
    • C11D3/34—Organic compounds containing sulfur
    • C11D3/3472—Organic compounds containing sulfur additionally containing -COOH groups or derivatives thereof
    • 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 a process for providing a worn look in dyed fabric, especially cellulosic fabric such as denim.
  • the first step in the processing evolution was to sell jeans that had been laundered by the manufacturer. These "pre-washed” jeans had a slightly faded appearance and a softer hand that felt comfortable, as though they had been laundered several times. This trend became fashionable as well, and consumers were willing to pay the extra cost involved for this additional processing. Not long after the introduction of pre-washed jeans, the idea of using abrasive stones to accelerate the aging process was developed, and "stone washing" became the second step in the evolution. Volcanic stones were included in the wash, or tumbled with the damp garments to wear down the stiffest portions such as belt areas, cuffs, and pockets.
  • the fabric looses strength by using the stone- process described above, and the stone-free cellulase treatment does not alone give the desired worn look, so there is a need in industry for a more gentle process.
  • the present invention relates to a process for providing an abraded look with a reduced strength loss in dyed fabric comprising
  • formula X represents (-0-) or (-S-)
  • the substituent groups R 1 -R 9 which may be identical or different, independently represents any of the following radicals: hydrogen, halogen, hydroxy, formyl, carboxy, and esters and salts hereof, carbamoyl, sulfo, and esters and salts hereof, sulfamoyl, nitro, amino, phenyl, Ci-Cn-alkyl, Ci-Cs-alkoxy, carbonyl-Ci-Cs-alkyl, aryl-Ci-Cs-alkyl; which car ⁇ bamoyl, sulfamoyl, and amino groups may furthermore be un- substituted or substituted once or twice with a substituent group R 10 ; and which phenyl may furthermore be unsubstituted or substituted with one or more substituent groups R 10 ; and which C ⁇ -C ⁇ 4 -alkyl, d-C 5 -al
  • the former is a result of removal (bleaching) of dye from the dyed warp yarn. Since the bleaching takes place on the whole surface of every dyed yarn, the result is a general reduction in colour intensity. Thus, the bleached look of a pair of indigo-dyed jeans is characterised by a lighter blue shade than the corresponding reference.
  • the latter - the worn look - is a result of a treatment of denim with cellulase and/or pumice stone.
  • This process is characterised by an uneven removal of dye from the fabric, hence it results in a high level of contrast between dyed areas and areas from which dye has been removed.
  • the worn look is obtained by a process involving cellulase and/or pumice stone
  • the bleached look can be obtained by a process involving non-enzymatic bleaching agents such as hypochlorite or by a process involving oxidoreductase and an enhancing agent.
  • the present invention relates to a process of providing a worn but not bleached look, comprising a mild treatment with a cellulase and a subsequent mild treatment with an oxidoreductase and an enhancing agent.
  • the invention may be applied to any dyed fabric known in the art, in particular to synthetic fabrics such as polyester or to natural fabrics.
  • the invention is most beneficially applied to cel ⁇ lulose-containing fabrics, such as cotton, viscose, rayon, ramie, linen, Tencel, or mixtures thereof, or mixtures of any of these fibres, or mixtures of any of these fibres together with synthetic fibres.
  • the fabric is denim.
  • the fabric may be dyed with vat dyes such as indigo, or indigo-related dyes such as thioindigo.
  • the fabric may also be dyed with more than one dye, e.g., first with a sulphur dye and then with an indigo dye, or vice versa.
  • the fabric is an indigo-dyed denim with a sulphur-bottom, (i.e. the denim is first dyed with a sulphur dye and then with an indigo dye) ; including clothing items manufactured therefrom.
  • cellulase refers to an enzyme which catalyses the degradation of cellulose to glucose, cellobiose, triose and other cello-oligosaccharides .
  • the term “cellulase” is understood to include a mature protein or a precursor form thereof or a functional fragment thereof which essentially has the activity of the full-length enzyme.
  • the term “cellulase” is intended to include homologues or analogues of said enzyme. Such homologues comprise an amino acid sequence exhibiting a degree of identity of at least 60% with the amino acid sequence of the parent enzyme, i.e. the parent cellulase.
  • the degree of identity may be determined by conventional methods, see for instance, Altshul et al . , Bull. Math. Bio. __, 1986, pp. 603-616, and Henikoff and Henikoff, Proc. Natl. Acad. Sci. USA 8j9, 1992, pp. 10915-10919.
  • the cellulase to be used in the present invention is a monocomponent (recombinant) cellulase, i.e. a cellulase essentially free from other proteins or cellulase proteins.
  • a recombinant cellulase component may be cloned and expressed according to standard techniques conventional to the skilled person.
  • the cellulase to be used in the method is an endoglucanase (EC 3.2.1.4), preferably a monocomponent (recombinant) endogluc ⁇ anase.
  • the cellulase is a microbial cellulase, more preferably a bacterial or fungal cellulase.
  • bacterial cellulases are cellulases der ⁇ ived from or producible by bacteria from the group of genera consisting of Pseudomonas or Bacillus, in particular Bacillus lautus.
  • the cellulase or endoglucanase may be an acid, a neutral or an alkaline cellulase or endoglucanase, i.e. exhibiting maximum cellulolytic activity in the acid, neutral or alkaline range, respectively.
  • a useful cellulase is an acid cellulase, preferably a fungal acid cellulase, which is der- ived from or producible by fungi from the group of genera con ⁇ sisting of Trichoderma, Actinomyces, Myrothecium, Aspergillus, and Botrytis.
  • a preferred useful acid cellulase is derived from or producible by fungi from the group of species consisting of Trichoderma viride, Trichoderma reesei, Trichoderma longibra- chiatum, Myrothecium verrucaria, Aspergillus niger, Aspergil ⁇ lus oryzae, and Botrytis cinerea.
  • Another useful cellulase or endoglucanase is a neutral or alkaline cellulase, preferably a fungal neutral or alkaline cellulase, which is derived from or producible by fungi from the group of genera consisting of Aspergillus, Penicillium, Myceliophthora, Humicola, Irpex, Fusarium, Sta- chybotrys, Scopulariopsis, Chaetomium, Mycogone, Verticillium, Myrothecium, Pap ⁇ lospora, Gliocladium, Cephalosporiu and Acremonium.
  • a preferred alkaline cellulase is derived from or producible by fungi from the group of species consisting of Humicola insolens, Fusarium oxysporum, Myceliopthora ther- mophila, or Cephalosporium sp., preferably from the group of species consisting of Humicola insolens, DSM 1800, Fusarium oxysporum, DSM 2672, Myceliopthora thermophila, CBS 117.65, or Cephalosporium sp., RYM-202.
  • a preferred example of a native or parent cellulase is an alkaline endoglucanase which is immunologically reactive with an antibody raised against a highly purified ⁇ 43kD endo ⁇ glucanase derived from Humicola insolens, DSM 1800, or which is a derivative of the ⁇ 43kD endoglucanase exhibiting cellulase activity.
  • Other examples of useful cellulases are variants having, as a parent cellulase, a cellulase of fungal origin, e.g. a cellulase derivable from a strain of the fungal genus Humicola, Trichoderma or Fusarium.
  • the concentration of the cellulase enzyme in the aqueous medium may be 0.01-250 ⁇ g of enzyme protein per g of fabric, preferably 0.1-250 ⁇ g of enzyme protein per g of fabric, in particular 0.5-50 ⁇ g of enzyme protein per g of fabric.
  • cellulase activity can be expressed in ECU.
  • Cellulolytic enzymes hydrolyse CMC, thereby increasing the viscosity of the incubation mixture.
  • the resulting reduction in viscosity may be determined by a vibration viscosimeter (e.g. MIVI 3000 from Sofraser, France) .
  • Determination of the cellulolytic activity, measured in terms of ECU, may be determined according to the following analysis method (assay) :
  • the ECU assay quantifies the amount of catalytic activity present in the sample by measuring the ability of the sample to reduce the viscosity of a solution of carboxy-methylcellulose (CMC) .
  • the assay is carried out at 40°C; pH 7.5; 0. IM phosphate buffer; time 30 min; using a relative enzyme standard for reducing the viscosity of the CMC (carboxymethylcellulose Hercules 7 LFD) substrate; enzyme concentration approx. 0.15 ECU/ml .
  • the arch standard is defined to 8200 ECU/g.
  • a phenol oxidizing enzyme system is meant a system in which an enzyme, by using hydrogen peroxide or molecular oxygen, is capable of oxidizing organic compounds containing phenolic groups.
  • an enzyme by using hydrogen peroxide or molecular oxygen, is capable of oxidizing organic compounds containing phenolic groups. Examples of such enzymes are peroxidases and oxidases.
  • the source may be hydrogen peroxide or a hydrogen peroxide precursor for in situ produc ⁇ tion of hydrogen peroxide, e.g., percarbonate or perborate, or a hydrogen peroxide generating enzyme system, e.g., an oxidase and a substrate for the oxidase, or an amino acid oxidase and a suitable amino acid, or a peroxycarboxylic acid or a salt thereof.
  • Hydrogen peroxide may be added at the beginning of or during the process, e.g., in a concentration corresponding to 0.001-25 mM H 2 0 2 . If the phenol oxidizing enzyme system requires molecular oxygen, molecular oxygen from the atmosphere will usually be present in sufficient quantity.
  • the enzyme of the phenol oxidizing enzyme system may be an enzyme exhibiting peroxidase activity or a laccase or a laccase related enzyme as described below.
  • the concentration of the phenol oxidizing enzyme in the aqueous medium may be 0.01-250 ⁇ g of enzyme protein per g of fabric, preferably 0.1-250 ⁇ g of enzyme protein per g of fabric, in particular 0.5-50 ⁇ g of enzyme protein per g of fabric.
  • An enzyme exhibiting peroxidase activity may be any peroxidase enzyme comprised by the enzyme classification (EC 1.11.1.7), or any fragment derived therefrom, exhibiting peroxidase activity, or synthetic or semisynthetic derivatives thereof (e.g. porphyrin ring systems or microperoxidases, cf. e.g. US 4,077,768, EP 537 381, WO 91/05858 and WO 92/16634) .
  • Such enzymes are known from microbial, plant and animal origins.
  • the peroxidase employed in the method of the invention is producible by plants (e.g. horseradish or soybean peroxidase) or microorganisms such as fungi or bacteria.
  • Some preferred fungi include strains belonging to the subdivision Deuteromycotina, class Hyphomycetes, e.g., Fu ⁇ sarium, Humicola, Tricoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium or Dreschlera, in particular Fusarium oxysporum (DSM 2672) , Humicola insolens, Trichoderma resii, Myrothecium verrucana (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754) , Caldariomyces fumago, Ulocladium chartarum, Embellisia alii
  • fungi include strains belonging to the subdivision Basidiomycotina, class Basidiomycetes, e.g. Copr nus, Phanerochaete, Coriolus or Trametes, in particular Copnnus cinereus f. microsporus (IF0 8371) , Coprinus macror ⁇ hizus, Phanerochaete chrysosporium (e.g. NA-12) or Trametes (previously called Polyporus) , e.g. T. versicolor (e.g. PR4 28-A) .
  • fungi include strains belonging to the subdivision Zygomycotina, class Mycoraceae, e.g. Rh zopus or Mucor, in particular Mucor hiemalis.
  • Some preferred bacteria include strains of the order Actinomycetales, e.g., Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptovertic llum verticillium ssp. vertic llium.
  • Actinomycetales e.g., Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptovertic llum verticillium ssp. vertic llium.
  • Bacillus pumilus Bacillus pumilus
  • Further preferred bacteria include strains belonging to Myxococcus, e.g., M. virescens.
  • the peroxidase may furthermore be one which is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding said peroxidase as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the peroxidase, in a culture medLum under conditions permitting the expression of the peroxidase and recovering the peroxidase from the culture.
  • a recombinantly produced peroxidase is a peroxidase derived from a Coprinus sp., in particular C ⁇ macrorhizus or C. cinereus according to WO 92/16634, or a variant thereof, e.g., a variant as described in WO 94/12621.
  • peroxidase acting compounds comprise peroxidase active fragments derived from cytochromes, haemoglobin or peroxidase enzymes, and synthetic or semisynthetic derivatives thereof, e.g. iron porphins, iron porphyrins, and iron phthalocyanine and derivatives thereof.
  • 1 peroxidase unit is the amount of enzyme that catalyzes the conversion of 1 ⁇ mole hydrogen peroxide per minute at the following analytical conditions: 0.88 mM hydrogen peroxide, 1.67 mM 2, 2 ' -azinobis (3- ethylbenzothiazoline-6-sulfonate) , 0.1 M phosphate buffer, pH 7.0, incubated at 30°C, photometrically followed at 418 nm.
  • laccases and laccase related enzymes contemplate any laccase enzyme com ⁇ prised by the enzyme classification (EC 1.10.3.2), any cha- techol oxidase enzyme comprised by the enzyme classification (EC 1.10.3.1), any bilirubin oxidase enzyme comprised by the enzyme classification (EC 1.3.3.5) or any monophenol mono- oxygenase enzyme comprised by the enzyme classification (EC 1.14.99.1) .
  • the laccase enzymes are known from microbial and plant origin.
  • the microbial laccase enzyme may be derived from bacteria or fungi (including filamentous fungi and yeasts) and suitable examples include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N.
  • crassa Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, e.g., T. vil- losa and T. versicolor, Rhizoctonia, e.g., R. solani, Copri ⁇ nus, e.g. C. plicatilis and C. cinereus, Psatyrella, Myceliophthora, e.g. M. thermophila, Schytalidium, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radita (WO 92/01046), or Coriolus, e.g., C.
  • the laccase or the laccase related enzyme may furthermore be one which is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding said laccase as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the laccase, in a cul ⁇ ture medium under conditions permitting the expression of the laccase enzyme, and recovering the laccase from the culture.
  • LACU Laccase Activity
  • Laccase activity is determined from the oxidation of syringaldazin under aerobic conditions.
  • the violet colour produced is photometered at 530 nm.
  • the analytical conditions are 19 ⁇ M syringaldazin, 23.2 mM acetate buffer, pH 5.5, 30°C, 1 min. reaction time.
  • LACU laccase unit
  • an enhancing agent is any compound that enhances the bleaching process.
  • the enhancing agent will typically be an organic compound, e.g., an organic compound described by one of the following formulas:
  • the enhancing agent may be described by the following formula I :
  • a in the above mentioned formula is -CO-E, in which E may be -H, -OH, -R, or -OR; R being a C1-C16 alkyl, preferably a C ⁇ -C 8 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 may be the same or different and selected from C m H 2m+ ⁇ ; 1 ⁇ m ⁇ 5.
  • the enhancing agent is acetosyringone, methylsyringate, ethylsyringate, propyl- syringate, butylsyringate, hexylsyringate, or octylsyringate.
  • enhancing agents described above may be prepared using methods well known to those skilled in the art; some of the enhancing agents are also commercially available, e.g., acetosyringone. Methylsyringate, ethylsyringate, propyl- syringate, butylsyringate, hexylsyringate and octylsyringate may be produced as disclosed in Chem. Ber. 67, 1934, p. 67.
  • the enhancing agent used in the present invention may also be described by the following formula II:
  • formula X represents (-O-) or (-S-)
  • the substituent groups R 1 -R 9 which may be identical or different, independently represents any of the following radicals: hydrogen, halogen, hydroxy, formyl, carboxy, and esters and salts hereof, carbamoyl, sulfo, and esters and salts hereof, sulfamoyl, nitro, ammo, phenyl, Ci-Cs-alkoxy, carbonyl-Ci-Cs-alkyl, aryl-Ci-Cs-alkyl; which car- bamoyl, sulfamoyl, and ammo groups may furthermore be un ⁇ substituted or substituted once or twice with a substituent group R 10 ; and which phenyl may furthermore be unsubstituted or substituted with one or more substituent groups R 10 ; and which C ⁇ -C ⁇ 4 -alkyl, Ci-Cs-alkoxy, carbony
  • the enhancing agent is 10-methylphenoth ⁇ az ⁇ ne, phenoth ⁇ az ⁇ ne-10-prop ⁇ on ⁇ c acid, N-hydroxysuccmimide phenoth ⁇ az ⁇ ne-10-prop onate, 10-ethyl- phenoth ⁇ az ⁇ ne-4-carboxyl ⁇ c acid, 10-ethylphenoth ⁇ azme, 10- propylphenothiazine, 10- ⁇ sopropylphenoth ⁇ az ⁇ ne, methyl pheno- th ⁇ azme-10-prop ⁇ onate, 10-phenylphenoth ⁇ azme, 10-allylpheno- thiaz e, 10- (3- (4-methylp ⁇ peraz ⁇ n-l-yl)propyl)phenothiazine, 10- (2-pyrrol ⁇ dm-l-yl-ethyl) phenothiazine, 2-methoxy-10- methyl-phenothiazme, l-methoxy-10
  • N-methylated derivatives of phenothiazine and phenoxazme may be prepared by methylation with methyliodide as described by Cornel Bodea and loan Silberg in "Recent Advances in the Chemistry of Phenothiazines” (Advances in heterocyclic chemistry, 1968, Vol. 9, pp. 321-460); B. Cardillo & G. Casnati in Tetrahedron, 1967, Vol. 23, p. 3771. Phenothiazine and phenoxazine propionic acids may be prepared as described in J. Org. Chem.
  • Hydroxyethyl and hydroxypropyl derivatives of phenothiazine and phenoxazine may be prepared as described by G. Cauquil in Bulletin de la Society Chemique de France, 1960, p.1049.
  • the enhancing agent of the invention may be present in concentrations of from 0.05 to 500 ⁇ mole per g denim, preferably 0.05 to 100 ⁇ mole per g denim, in particular 0.05 to 20 ⁇ mole per g denim.
  • the present invention is typically used in industrial machines for cellulase treatment of fabric.
  • the fabric is normally added to the machine accord ⁇ ing to the machine capacity per the manufacturer's instruc- tions.
  • the fabric may be added to the machine prior to introducing water or the fabric may be added after water is introduced.
  • the cellulase treatment will be performed first, followed by the treatment with the phenol oxidizing enzyme system and the enhancing agent, but the two processes may be performed simultaneously, or vice versa.
  • the cellulase may be present in the water prior to adding the fabric or it may be added after the fabric has been wetted. Normally a buffer will be used in order to be close to the pH optimum of the enzyme in question. After the fabric has been contacted with the cellulase it should be agitated in the machine for a sufficient period of time to ensure that the fabric is fully wetted and to ensure the action of the enzyme. Typically a reaction time between 5 and 60 minutes and a reaction temperature between 20°C and 90°C, preferably between 30°C and 80°C, more preferably between 40°C and 70°C, will be suitable.
  • the phenol oxidizing enzyme system and the enhancing agent of the invention may be present in the water prior to adding the fabric or they may be added after the fabric has been wetted.
  • the phenol oxidizing enzyme system may be added simultaneously with the enhancing agent or they may be added separately.
  • a buffer will be used in order to be close to the pH optimum of the enzyme in question.
  • a reaction time between 5 and 60 minutes and a reaction temperature between 20°C and 90°C, preferably between 30°C and 80°C, more preferably between 40°C and 70°C, will be suitable.
  • denim all manufactured by Levi Strauss & Co
  • the 5 types of denim were all of the "sul ⁇ phur-bottom” type but the ratio between indigo and sulphur dye varied, as did the fabric construction.
  • Step 1 Abrasion with cellulase/pumice stone.
  • the denim was split into 2 different abrasion processes: 1) a standard abrasion process involving neutral ceLlulase + pumice stone or 2) an abrasion process with no addition of pumice stone.
  • MTF12EB neutral cellulase, available from T.S. Chemicals, UK 50 minutes, pH 6.5, 60°C
  • Step 2 Treatment with laccase and enhancing agent
  • the jeans from step 1 (except one of each type, which were kept as reference) were then treated with a laccase and an enhancing agent using following dosages and conditions:
  • the process consisting of a cellulase treatment step without pumice stone and a subsequent treatment with laccase and enhancing agent resulted in jeans with a highly worn look without having a bleached look.
  • This was evaluated as extremely interesting as the process provides a look that would otherwise require higher amounts of cellulase and addition of substantial amounts of pumice stone.
  • the process provided a highly worn look, without having the fabric damage that would be the result of a pumice stone or cellulase/pumice stone process for obtaining the same look.
  • a 12 kg Wascator FL 120 wash extractor was used for abrasion of the denim.
  • a Wascator FOM 71 wash extractor was used for abrasion enhancement of the denim.
  • L gives the change in black (-L*) /white (+L*)
  • a gives the change in green (-a*) /red (+a*)
  • b gives the change in blue (-b*) /yellow (+b*) .
  • a decrease in L* means an increase in blackness (decrease of white colour)
  • an increase in L* means an increase in whiteness (a decrease in black colour)
  • a decrease in a* means an increase in green colour (decrease in red colour)
  • an increase in a* means an increase in red colour (a decrease in green colour)
  • a decrease in b* means an increase in blue colour (a decrease in yellow colour)
  • an increase in b* means an increase in yellow colour (a decrease in blue colour) .
  • the Texflash 2000 was operated in the L*a*b* coordinate system.
  • the light source used was a CIE light standard C. Each measurement was an average of 10 measurements.
  • the instrument was calibrated using calibration plates (black and white) .
  • a 12 kg Wascator FL 120 wash extractor was used for abrasion of the denim. 3 different dosages of cellulase were used applied.
  • Enzyme DenimaxTM Ultra MG (a commercial mono-component cellulase product, available from Novo Nordisk A/S)
  • a Wascator FOM 71 wash extractor was used for abrasion enhancement of the denim.
  • the dosage of laccase and mediator was varied in 3 trials.
  • Enzyme Trametes villosa laccase (available from Novo).
  • abrasion enhancement is only obtained if the dosage of laccase and the dosage of enhancing agent is kept below a certain limit (otherwise the result will be a bleached appearance) . Also, it is seen that this limit depends on the dosage of cellulase in the abrasion step - the higher the cellulase dosage, the lower the limit is, i.e. following approximate rules:

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  • Engineering & Computer Science (AREA)
  • Chemical & Material Sciences (AREA)
  • Textile Engineering (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Biochemistry (AREA)
  • Microbiology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Or Physical Treatment Of Fibers (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Detergent Compositions (AREA)
  • Coloring (AREA)
  • Treatments For Attaching Organic Compounds To Fibrous Goods (AREA)

Abstract

Cette invention se rapporte à un procédé servant à produire un aspect râpé avec une perte de résistance réduite dans un tissu teint, ce procédé consistant: (a) à mettre en contact, dans un milieu aqueux, un tissu teint avec une cellulase selon une concentration correspondant à 0,01-250 νg de protéine d'enzyme par g de tissu; (b) et à traiter en même temps ou ultérieurement ce tissu avec un système d'enzymes oxydantes au phénol et un agent activateur.
PCT/DK1997/000002 1996-01-12 1997-01-08 Tissu traite avec de la cellulase et de l'oxydoreductase WO1997025468A1 (fr)

Priority Applications (7)

Application Number Priority Date Filing Date Title
BR9706965A BR9706965A (pt) 1996-01-12 1997-01-08 Processo para proporcionar um aspecto de usado com reduzida perda de resistência no tecido tingido e tecido
JP52476397A JP3977429B2 (ja) 1996-01-12 1997-01-08 セルラーゼ及びオキシドレダクターゼで処理した布帛
DE69717486T DE69717486T2 (de) 1996-01-12 1997-01-08 Gewebe behandelt mit cellulase und oxidoreductase
EP97900194A EP0935692B1 (fr) 1996-01-12 1997-01-08 Tissu traite avec de la cellulase et de l'oxydoreductase
AU13667/97A AU1366797A (en) 1996-01-12 1997-01-08 Fabric treated with cellulase and oxidoreductase
PL97327815A PL186471B1 (pl) 1996-01-12 1997-01-08 Zastosowanie celulazy w połączeniu z układem enzymatycznym utleniającym fenol i środkiem wzmacniającym
US09/079,027 US5908472A (en) 1996-01-12 1998-05-14 Fabric treated with cellulase and oxidoreductase

Applications Claiming Priority (2)

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DK0024/96 1996-01-12
DK2496 1996-01-12

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US09/079,027 Continuation US5908472A (en) 1996-01-12 1998-05-14 Fabric treated with cellulase and oxidoreductase

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BR (1) BR9706965A (fr)
DE (1) DE69717486T2 (fr)
ES (1) ES2187748T3 (fr)
MA (1) MA24059A1 (fr)
MX (1) MX9805592A (fr)
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PT (1) PT935692E (fr)
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Cited By (12)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1999013038A1 (fr) * 1997-09-08 1999-03-18 Unilever N.V. Procede servant a augmenter l'activite d'une enzyme
US5912405A (en) * 1994-09-27 1999-06-15 Novo Nordisk A/S Enhancers such as acetosyringone
WO1999032652A1 (fr) * 1997-12-19 1999-07-01 Novo Nordisk A/S Modification de polysaccharides a l'aide d'une enzyme oxydant le phenol
WO2006032723A1 (fr) * 2004-09-21 2006-03-30 Ab Enzymes Oy Nouvel enzyme laccase et son utilisation
WO2006032724A3 (fr) * 2004-09-21 2006-08-31 Ab Enzymes Oy Nouvelles enzymes laccase et leurs utilisations
US7319112B2 (en) 2000-07-14 2008-01-15 The Procter & Gamble Co. Non-halogenated antibacterial agents and processes for making same
US7927849B2 (en) 2004-09-21 2011-04-19 Ab Enzymes Oy Laccase enzyme and use thereof
CN102264892A (zh) * 2008-12-24 2011-11-30 丹尼斯科美国公司 漆酶及其在低温使用的方法
WO2013087027A1 (fr) 2011-12-16 2013-06-20 Novozymes, Inc. Polypeptides ayant une activité laccase et polynucléotides les codant
US8558058B2 (en) 2001-12-06 2013-10-15 Applied Biotechnology Institute Monocotyledonous seed expressing exo-1,4B-glucanase
WO2016090059A1 (fr) 2014-12-02 2016-06-09 Novozymes A/S Variants de laccase et polynucléotides codant pour ceux-ci
US10308948B2 (en) 2011-07-27 2019-06-04 Applied Biotechnology Institute, Inc. Method of increasing expression of nucleic acid molecules in plants using multiple transcription units

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2000050388A1 (fr) * 1999-02-24 2000-08-31 Sca Hygiene Products Zeist B.V. Procede de production d'ions nitrosonium

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1994012619A1 (fr) * 1992-12-01 1994-06-09 Novo Nordisk A/S Amelioration de reactions enzymatiques

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1994012619A1 (fr) * 1992-12-01 1994-06-09 Novo Nordisk A/S Amelioration de reactions enzymatiques

Cited By (18)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5912405A (en) * 1994-09-27 1999-06-15 Novo Nordisk A/S Enhancers such as acetosyringone
WO1999013038A1 (fr) * 1997-09-08 1999-03-18 Unilever N.V. Procede servant a augmenter l'activite d'une enzyme
US6169065B1 (en) 1997-09-08 2001-01-02 Lever Brothers Company Division Of Conopco Company Method for the activity of an enzyme
WO1999032652A1 (fr) * 1997-12-19 1999-07-01 Novo Nordisk A/S Modification de polysaccharides a l'aide d'une enzyme oxydant le phenol
US6087135A (en) * 1997-12-19 2000-07-11 Novo Nordisk A/S Modification of polysaccharides by means of a phenol oxidizing enzyme
US6346401B1 (en) 1997-12-19 2002-02-12 Novozymes A/S Modification of polysaccharides by means of a phenol oxidizing enzyme
US7319112B2 (en) 2000-07-14 2008-01-15 The Procter & Gamble Co. Non-halogenated antibacterial agents and processes for making same
US8558058B2 (en) 2001-12-06 2013-10-15 Applied Biotechnology Institute Monocotyledonous seed expressing exo-1,4B-glucanase
WO2006032724A3 (fr) * 2004-09-21 2006-08-31 Ab Enzymes Oy Nouvelles enzymes laccase et leurs utilisations
WO2006032723A1 (fr) * 2004-09-21 2006-03-30 Ab Enzymes Oy Nouvel enzyme laccase et son utilisation
US7732178B2 (en) 2004-09-21 2010-06-08 Ab Enzymes Oy Laccase enzymes and their uses
US7927849B2 (en) 2004-09-21 2011-04-19 Ab Enzymes Oy Laccase enzyme and use thereof
CN102264892A (zh) * 2008-12-24 2011-11-30 丹尼斯科美国公司 漆酶及其在低温使用的方法
US20110302722A1 (en) * 2008-12-24 2011-12-15 Danisco Us Inc. Laccases and methods of use thereof at low temperature
US10308948B2 (en) 2011-07-27 2019-06-04 Applied Biotechnology Institute, Inc. Method of increasing expression of nucleic acid molecules in plants using multiple transcription units
WO2013087027A1 (fr) 2011-12-16 2013-06-20 Novozymes, Inc. Polypeptides ayant une activité laccase et polynucléotides les codant
EP3272862A1 (fr) 2011-12-16 2018-01-24 Novozymes, Inc. Polypeptides ayant une activité laccase et polynecleotides les codant
WO2016090059A1 (fr) 2014-12-02 2016-06-09 Novozymes A/S Variants de laccase et polynucléotides codant pour ceux-ci

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Publication number Publication date
AU1366797A (en) 1997-08-01
DE69717486D1 (de) 2003-01-09
MA24059A1 (fr) 1997-10-01
JP2000503075A (ja) 2000-03-14
CN1130483C (zh) 2003-12-10
PT935692E (pt) 2003-04-30
EP0935692B1 (fr) 2002-11-27
TR199801300T2 (xx) 1998-10-21
DE69717486T2 (de) 2003-07-17
BR9706965A (pt) 1999-05-04
MX9805592A (es) 1998-10-31
PL186471B1 (pl) 2004-01-30
PL327815A1 (en) 1999-01-04
JP3977429B2 (ja) 2007-09-19
EP0935692A1 (fr) 1999-08-18
CN1218524A (zh) 1999-06-02
ES2187748T3 (es) 2003-06-16

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