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WO1997011217A1 - Blanchiment de taches - Google Patents

Blanchiment de taches Download PDF

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Publication number
WO1997011217A1
WO1997011217A1 PCT/DK1996/000390 DK9600390W WO9711217A1 WO 1997011217 A1 WO1997011217 A1 WO 1997011217A1 DK 9600390 W DK9600390 W DK 9600390W WO 9711217 A1 WO9711217 A1 WO 9711217A1
Authority
WO
WIPO (PCT)
Prior art keywords
alkyl
process according
esters
groups
peroxidase
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/DK1996/000390
Other languages
English (en)
Inventor
Ture Damhus
Palle Schneider
Lars Sparre Conrad
Søren EBDRUP
Nickie Inger Spile
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novo Nordisk AS
Original Assignee
Novo Nordisk AS
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Novo Nordisk AS filed Critical Novo Nordisk AS
Priority to AU68700/96A priority Critical patent/AU6870096A/en
Publication of WO1997011217A1 publication Critical patent/WO1997011217A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

Links

Classifications

    • 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
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
    • D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
    • D06L4/10—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen
    • D06L4/12—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen combined with specific additives

Definitions

  • the present invention relates to a process for removing coloured stains present on fabric at low washing temperatures .
  • coloured stains typically originate from red wine, fruit such as black currant, cherry, strawberry and tomato (in particular ketchup and spaghetti sauce) , vegetables such as carrots and beetroot, tea, coffee, spices such as curry and paprika, grass, or ball pens/ink.
  • bleaching agents to solve the above mentioned problem.
  • bleaching agents incorporated in detergent compositions are compounds which are precursors of hydrogen peroxide; hydrogen peroxide is then formed in the course of the washing procedure.
  • Perborates and percarbonates are the most important examples of such hydrogen peroxide precursors .
  • Perborate and percarbonate may also be combined with a peracid-forming bleach activator such as TAED (tetraacetylethylenediamine) or NOBS (nonanoyloxybenzenesulfonate) .
  • TAED tetraacetylethylenediamine
  • NOBS nonanoyloxybenzenesulfonate
  • E and F may be identical or different and selected from the group consisting of
  • B and C may be the same or different and selected from C m H 2m+ ⁇ ; 1 ⁇ m ⁇ 5; or
  • formula X represents (-0-) or (-S-)
  • the substituent groups R 1 -.. 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, C ⁇ -C ⁇ 4 -alkyl, C ⁇ -C 5 -alkoxy, carbonyl-C ⁇ -C 5 -alkyl, aryl-C ⁇ -C 5 -alkyl; which carbamoyl, sulfa ⁇ moyl, and amino groups may furthermore be unsubstituted 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 Ci-Cn-alkyl, C1
  • a bleaching process comprising contacting, in an aqueous medium, the fabric with a phenol oxidizing enzyme and a mediator for a sufficient period of time.
  • Stains which may be removed according to the present invention typically originate from for example spices such as curry and paprika or vegetables/fruits, e.g., carrots.
  • the bleaching time for removing the stain (s) may vary; the fabric may be soaked for one or two days or the bleaching may be performed within a shorter period, typically for a period of 1 to 90 minutes, preferably for a period of 1 to 30 minutes.
  • a phenol oxidizing enzyme an enzyme, which 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 production 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 .
  • the enzyme of the phenol oxidizing enzyme may be an enzyme possessing peroxidase activity or a laccase or a laccase related enzyme as described below.
  • the concentration of the phenol oxidizing enzyme in the aqueous medium where the stain bleaching of the fabric is taking place may be of from 0.001- 100 mg of enzyme protein per liter, in particular of from 0.01- 50 mg of enzyme protein per liter, even more preferably of from 0.1-10 mg of enzyme protein per liter.
  • 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) .
  • 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.
  • plants e.g. horseradish or soybean peroxidase
  • microorganisms such as fungi or bacteria.
  • Some preferred fungi include strains belonging to the sub ⁇ division Deuteromycotina, class Hyphomycetes, e.g.
  • Other preferred fungi include strains belonging to the subdivision Basidiomycotina, class Basidiomycetes, e.g. O 97/11217 PC17DK96/00390
  • Coprinus, Phanerochaete, Coriolus or Trametes in particular Coprinus cinereus f . microsporus (IFO 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. Rhizopus 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 Streptoverticill um verticillium ssp. verticillium .
  • Actinomycetales e.g. Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptoverticill um verticillium ssp. verticillium .
  • Bacill us pumil us ATCC 12905
  • Bacillus stearothermophil us Rhodobacter sphaeroides
  • Rhodomonas pal ustri Streptococcus lactis
  • Pseudomonas purrocinia ATCC 15958
  • Pseudomonas fl uorescens NRRL B-ll
  • 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 trans ⁇ formed 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 medium 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 93/24618 and WO 95/10602.
  • compounds possessing peroxidase activity comprise peroxidase enzymes and peroxidase active fragments derived from cytochromes, haemoglobin or peroxidase enzymes, and synthetic or semisynthetic derivatives thereof, e.g., iron porphyrins, and iron phthalocyanine and derivatives thereof.
  • PODU Peroxidase Activity
  • 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 comprise any laccase enzyme comprised by the enzyme classification (EC 1.10.3.2), any catechol 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 monooxygenase enzyme comprised by the enzyme classification (EC 1.14.18.1) .
  • the above mentioned enzymes may be derived from plants, 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. villosa and T. versicolor, Rhizoctonia , e.g., R . solani , Coprinus, e.g., C. plicatilis and C. cinereus, Psa tyrella , Myceliophthora , e.g., M. thermophila , Schytalidium, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P.
  • 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.
  • 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.
  • 1 laccase unit (LACU) is the amount of enzyme that catalyses the conversion of 1.0 ⁇ mole syringaldazin per minute at these conditions.
  • a mediator 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 mediator is acetosyringone, syringaldehyde, methylsyringate, syringic acid, ethylsyringate, propylsyringate, butylsyringate, hexylsyringate, octylsyringate or ethyl 3- (4-hydroxy-3, 5- dimethoxyphenyl) acrylate.
  • the mediator used in the present invention may also be described by the following formula:
  • formula X represents (-0-) or (-S-)
  • the substituent groups R ⁇ 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, C ⁇ -C ⁇ -alkyl, Ci-Cs-alkoxy, carbonyl-Ci-Cs-alkyl, aryl-C ⁇ -C 5 -alkyl; which carbamoyl, sulfamoyl, and amino groups may furthermore be unsubstituted 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, C1-C5- al
  • the mediator is 10-methyl- phenothiazine, 10-phenothiazine-propionic acid, N-hydroxy ⁇ succinimide-10-phenothiazine-propionate, 10-ethyl-4-pheno- thiazine-carboxylic acid, 10-ethylphenothiazine, 10-propyl- phenothiazine, 10-isopropylphenothiazine, methyl-10-pheno- thiazinepropionate, 10-phenylphenothiazine, 10-allylpheno- thiazine, 10- (3- (4-methyl-l-piperazinyl)propyl)phenothiazine, 10- (2-pyrrolidinoethyl)phenothiazine, chlorpromazine, 2-chloro- 10-methylphenothiazine, 2-acetyl-10-methylphenothiazine, 4- carboxy-10-phenothiazine, 10-methylphenoxazine, 10-e
  • the mediator of the invention may be present in concentrations of from 0.01 to 5000 ⁇ M, preferably in concentrations of from 0.1 to 1000 ⁇ M, even more preferably in concentrations of from 1 to 500 ⁇ M.
  • mediators described in the present application may be prepared using methods well known to those skilled in the art; some of the mediators are also commercially available. Some of the mediators may be obtained from Sigma-
  • N-methylated derivatives of phenothiazine and phenoxazine 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.
  • Methylsyringate, ethylsyringate, propylsyringate, butylsyringate, hexylsyringate and octylsyringate may be produced by using the method disclosed in Chem. Ber. 67, 1934, p. 67.
  • Ethyl 3- (4-hydroxy-3, 5-dimethoxyphenyl) acrylate was synthesised from syringaldehyde and triethyl phosphonoacetate in ethanol/sodium ethanolate.
  • the product was after purification characterised by 1 H-NMR and 13 C-NMR (showing spectra as expected) and the melting point was 68-70°C.
  • the reference treatment in each case was a wash under the same conditions with no laccase-mediator system present.
  • test pieces of fabric were thoroughly rinsed in cold tap water and air-dried in the dark overnight.
  • the bleaching effect of any given laccase-mediator system was then evaluated by using a Datacolor Elrepho 2000 (remission measurements at 460 nm) or by using a Minolta Chroma Meter (colourspace XYZ) using D65 as the light source.
  • the mediators used are abbreviated as follows:
  • PPT phenothiazine-10-propionic acid
  • EPC 4-carboxyphenothiazine-10-propionic acid
  • POP phenoxazine-10-propionic acid
  • AS acetosyreingone
  • Laccase preparation obtained in the following way: 800 ml culture broth of Trametes villosa , CBS 678.70, was filtered with filter aid to give a clear filtrate, which was concentrated and washed by ultrafiltration on a membrane with a cut-off of 6-8 kDa.
  • One ml samples of concentrated preparation was applied onto a Q-Sepharose HP column (Pharmacia, Sweden) equilibrated with 0.1 M fosfate pH 7, and the laccase was eluted with a flat NaCl gradient around 0.25 M. Fractions with laccase activity from 10 runs were pooled and concentrated by ultrafiltration.
  • Laccase dossage 1 mg/l washing liquor.
  • Mediator dosage 120 ⁇ M. Mediators predissolved in ethanol.
  • Laccase preparation obtained in the following way: Coprinus cinereus (IFO 30116 - freely available to the public from Institute of Fermentation, Osaka (IFO) under the indicated deposit number) was inoculated from a PDA agar slant (PDA: 39 g/1 potato dextrose agar) into a 100 ml shake flask containing medium A (Medium A is described below) . The culture was cultivated for 6 days at 26°C and 100 rpm. A 10-liter fermentor containing medium A was inoculated with the 100 ml culture broth. The fermentation ran for 6 days at 26°C and 100 rpm. The culture broth was filtrated and concentrated by ultrafiltration.
  • PDA agar slant PDA: 39 g/1 potato dextrose agar
  • medium A Medium A is described below
  • Laccase dosage 1 mg/l washing liquor.
  • Mediator dosage 120 ⁇ M. Mediators predissolved in ethanol.
  • Laccase preparation obtained as described in PCT/US95/06815.
  • Laccase dosage 1 mg/l washing liquor.
  • Peroxidase preparation obtained as described in WO 94/12621 Peroxidase dosage: 0.2 mg/l washing liquor.
  • Mediator dosage 120 ⁇ M. Mediators predissolved in ethanol. Hydrogen peroxide: 0.5 mM.
  • the paprika test pieces of fabric were obtained from Center for Testmaterials, WFK P (P043) .
  • Peroxidase-mediator systems identical to or similar to the ones studied in Example 2 were subjected to a Launder-ometer wash trial to investigate the effects of having a closed system and a different mechanical treatment.
  • the Launder-ometer is a laboratory-scale set-up for simulating conditions in a traditional front-loaded European washing machine.
  • Peroxidase preparation obtained as described Example 2. Peroxidase dosage: 120 ⁇ M. Mediators predissolved in ethanol. Hydrogen peroxide: 0.5 mM.
  • Laccase preparation obtained as described in Example 1. Laccase dosage 1 mg/l washing liquor. Mediator dosage: 120 ⁇ M. Mediators predissolved in ethanol.

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  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Textile Engineering (AREA)
  • Detergent Compositions (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

L'invention a trait à un procédé permettant de blanchir des taches se trouvant sur un tissu, le procédé consistant à mettre en contact dans un milieu aqueux le tissu avec un système enzymatique d'oxydation du phénol et un médiateur pendant un délai suffisant.
PCT/DK1996/000390 1995-09-19 1996-09-13 Blanchiment de taches Ceased WO1997011217A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AU68700/96A AU6870096A (en) 1995-09-19 1996-09-13 Stain bleaching

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
DK1042/95 1995-09-19
DK104295 1995-09-19
DK131795 1995-11-23
DK1317/95 1995-11-23

Publications (1)

Publication Number Publication Date
WO1997011217A1 true WO1997011217A1 (fr) 1997-03-27

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Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/DK1996/000390 Ceased WO1997011217A1 (fr) 1995-09-19 1996-09-13 Blanchiment de taches

Country Status (2)

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AU (1) AU6870096A (fr)
WO (1) WO1997011217A1 (fr)

Cited By (27)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1998051772A1 (fr) * 1997-05-12 1998-11-19 Call, Krimhild Systeme de blanchiment aux enzymes a nouveaux composes renforçant l'action enzymatique
WO1998056899A1 (fr) * 1997-06-10 1998-12-17 Unilever N.V. Procede pour ameliorer l'activite d'une enzyme, composition de blanchiment, composition detergente et procede pour inhiber le transfert de colorant
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
WO2000039263A1 (fr) * 1998-12-23 2000-07-06 Genencor International, Inc. Enzymes de pleurote oxydant le phenol
WO2001000769A1 (fr) * 1999-06-23 2001-01-04 Unilever N.V. Procede et composition permettant d'ameliorer l'activite d'une enzyme
WO2001000768A1 (fr) * 1999-06-23 2001-01-04 Unilever N.V. Compositions de detergents de blanchiment
WO2001021748A1 (fr) * 1999-09-22 2001-03-29 Unilever N.V. Compositions detergentes contenant des enzymes d'oxydation de phenol
US6218350B1 (en) 1997-06-13 2001-04-17 Lever Brothers Company, Division Of Conopco, Inc. Bleaching enzymes
US6384007B1 (en) 1999-11-11 2002-05-07 Unilever Home & Personal Usa Division Of Conopco, Inc. Method and composition for enhancing the activity of an enzyme
US6518231B2 (en) 2000-12-18 2003-02-11 Unilever Home & Personal Care Usa, Division Of Conopco, Inc. Enhancement of air bleaching catalysts
US6818149B2 (en) 2000-12-15 2004-11-16 Unilever Home & Personal Care Usa, Division Of Conopco, Inc. Ligand and complex for catalytically bleaching a substrate
US6866687B2 (en) 2002-09-27 2005-03-15 Unilever Home & Personal Care Usa, A Division Of Conopco, Inc. Composition and method for bleaching a substrate
US7052520B2 (en) 2002-05-23 2006-05-30 Unilever Home & Personal Care Usa, A Division Of Conopco, Inc. Article and process for cleaning fabrics
US7144717B1 (en) 1998-03-24 2006-12-05 Genecor International, Inc. Oxidizing enzymes
US7319112B2 (en) 2000-07-14 2008-01-15 The Procter & Gamble Co. Non-halogenated antibacterial agents and processes for making same
US20080189871A1 (en) * 2006-12-18 2008-08-14 Mcauliffe Joseph C Laccase mediators and methods of use
WO2010075402A1 (fr) 2008-12-24 2010-07-01 Danisco Us Inc. Laccases et procédés d'utilisation de celles-ci à basse température
WO2010135499A1 (fr) * 2009-05-21 2010-11-25 Danisco Us Inc. Détergent de vaisselle comportant des enzymes de blanchiment
WO2011025861A1 (fr) 2009-08-27 2011-03-03 Danisco Us Inc. Abrasion et modification de couleur combinées de textiles
EP2431048A2 (fr) 2002-10-08 2012-03-21 Genencor International, Inc. Peptides de liaison phénolique
WO2012054485A1 (fr) 2010-10-18 2012-04-26 Danisco Us Inc. Modification locale de la couleur de tissus teints au moyen d'un système à laccase
WO2012138474A1 (fr) 2011-04-06 2012-10-11 Danisco Us Inc. Variants de laccase ayant une expression améliorée et/ou une activité améliorée
CN101563500B (zh) * 2006-12-18 2013-11-13 丹尼斯科美国公司 漆酶介质及使用方法
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
WO2016193335A1 (fr) * 2015-06-05 2016-12-08 Henkel Ag & Co. Kgaa Détergent contenant au moins une laccase, dont la performance de lavage est améliorée
EP3444323A1 (fr) * 2017-08-18 2019-02-20 The Procter & Gamble Company Trousse de nettoyage

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1992018683A1 (fr) * 1991-04-12 1992-10-29 Novo Nordisk A/S Procede de blanchiment de textiles colores
WO1994012621A1 (fr) * 1992-12-01 1994-06-09 Novo Nordisk Amelioration de reactions enzymatiques
WO1996012846A1 (fr) * 1994-10-20 1996-05-02 Novo Nordisk A/S Procede de blanchiment consistant a utiliser une enzyme oxydant le phenol, une source de peroxyde d'hydrogene et un agent de renforcement
WO1996012845A1 (fr) * 1994-10-20 1996-05-02 Novo Nordisk A/S Procede de blanchiment consistant a utiliser une enzyme oxydant le phenol, une source de peroxyde d'hydrogene et un agent facilitant

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1992018683A1 (fr) * 1991-04-12 1992-10-29 Novo Nordisk A/S Procede de blanchiment de textiles colores
WO1994012621A1 (fr) * 1992-12-01 1994-06-09 Novo Nordisk Amelioration de reactions enzymatiques
WO1996012846A1 (fr) * 1994-10-20 1996-05-02 Novo Nordisk A/S Procede de blanchiment consistant a utiliser une enzyme oxydant le phenol, une source de peroxyde d'hydrogene et un agent de renforcement
WO1996012845A1 (fr) * 1994-10-20 1996-05-02 Novo Nordisk A/S Procede de blanchiment consistant a utiliser une enzyme oxydant le phenol, une source de peroxyde d'hydrogene et un agent facilitant

Cited By (38)

* 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
WO1998051772A1 (fr) * 1997-05-12 1998-11-19 Call, Krimhild Systeme de blanchiment aux enzymes a nouveaux composes renforçant l'action enzymatique
WO1998056899A1 (fr) * 1997-06-10 1998-12-17 Unilever N.V. Procede pour ameliorer l'activite d'une enzyme, composition de blanchiment, composition detergente et procede pour inhiber le transfert de colorant
US6225275B1 (en) 1997-06-10 2001-05-01 Lever Brothers Company, Division Of Conopco, Inc. Method for enhancing the activity of an enzyme
US6218350B1 (en) 1997-06-13 2001-04-17 Lever Brothers Company, Division Of Conopco, Inc. Bleaching enzymes
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
US7144717B1 (en) 1998-03-24 2006-12-05 Genecor International, Inc. Oxidizing enzymes
US6329332B1 (en) 1998-12-23 2001-12-11 Genencor International, Inc. Pleurotus phenol oxidizing enzymes
WO2000039263A1 (fr) * 1998-12-23 2000-07-06 Genencor International, Inc. Enzymes de pleurote oxydant le phenol
WO2001000768A1 (fr) * 1999-06-23 2001-01-04 Unilever N.V. Compositions de detergents de blanchiment
US6323014B1 (en) 1999-06-23 2001-11-27 Unilever Home & Personal Care Division Of Conopco, Inc. Method and composition for enhancing the activity of an enzyme
WO2001000769A1 (fr) * 1999-06-23 2001-01-04 Unilever N.V. Procede et composition permettant d'ameliorer l'activite d'une enzyme
US6380146B1 (en) 1999-06-23 2002-04-30 Unilever Home & Personal Care Usa A Division Of Conopco, Inc. Bleaching detergent compositions
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