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US20020004958A1 - Dyeing substrates - Google Patents

Dyeing substrates Download PDF

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Publication number
US20020004958A1
US20020004958A1 US09/802,189 US80218901A US2002004958A1 US 20020004958 A1 US20020004958 A1 US 20020004958A1 US 80218901 A US80218901 A US 80218901A US 2002004958 A1 US2002004958 A1 US 2002004958A1
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Prior art keywords
substrate
enzyme
oxidation
amino
peroxidase
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US09/802,189
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Niels Sorensen
Ole Kirk
Rikke Lolck
Torben Desler
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Novozymes AS
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Novozymes AS
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Assigned to NOVOZYMES A/S reassignment NOVOZYMES A/S ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: NOVO NORDISK A/S
Publication of US20020004958A1 publication Critical patent/US20020004958A1/en
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    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61QSPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q5/00Preparations for care of the hair
    • A61Q5/10Preparations for permanently dyeing the hair
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00Cosmetics or similar toiletry preparations
    • A61K8/18Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/40Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing nitrogen
    • A61K8/44Aminocarboxylic acids or derivatives thereof, e.g. aminocarboxylic acids containing sulfur; Salts; Esters or N-acylated derivatives thereof
    • A61K8/445Aminocarboxylic acids or derivatives thereof, e.g. aminocarboxylic acids containing sulfur; Salts; Esters or N-acylated derivatives thereof aromatic, i.e. the carboxylic acid directly linked to the aromatic ring
    • CCHEMISTRY; METALLURGY
    • C09DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
    • C09BORGANIC DYES OR CLOSELY-RELATED COMPOUNDS FOR PRODUCING DYES, e.g. PIGMENTS; MORDANTS; LAKES
    • C09B17/00Azine dyes
    • C09B17/02Azine dyes of the benzene series
    • DTEXTILES; PAPER
    • D06TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06PDYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
    • D06P1/00General 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
    • D06P1/32General 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 oxidation dyes
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/531Production of immunochemical test materials
    • G01N33/532Production of labelled immunochemicals
    • G01N33/535Production of labelled immunochemicals with enzyme label or co-enzymes, co-factors, enzyme inhibitors or enzyme substrates

Definitions

  • the present invention concerns the use of aminobenzoic acid (DABA) as a substitute for e.g. o-phenylendiamine (OPD) in analyses based on peroxidases as well as a dyeing substrate (i.e. a dye precursor) in dyeing compositions, and as an substrate for dyeing natural and synthetic fibres including textiles, thread and yarns.
  • DABA aminobenzoic acid
  • OPD o-phenylendiamine
  • the invention also relates to a composition adapted for dyeing keratinous fibres, e.g. hair, wool, fur and hides, and a method for dyeing such keratinous fibres.
  • ELISA Enzyme Linked Immuno Sorbent Assay
  • the main principle is that in a much diluted solution many antigens will become bound to the surface of plastic. Thus, if a much diluted solution of antigens is incubated for a time in plastic trays it is possible to wash the cavities in a buffer solution and still retain the film of antigens on the surface of the plastic. If it is required to determine the amount of antibodies in, for instance, serum then the trays with their deposits of antigens are incubated with the serum.
  • the antibodies attach themselves to the antigens and, after thorough washing the trays are again incubated this time with a marker, for example anti-immune globulin serum to which there is attached a suitable enzyme by covalent bonding.
  • a marker for example anti-immune globulin serum to which there is attached a suitable enzyme by covalent bonding.
  • peroxidase is used.
  • the peroxidase-marker complex will attach itself to those locations where there is already a deposit of antibodies. After thorough washing to remove all un-combined material the enzyme activity is measured, normally by the use of a suitable colour indicator. Enzyme activity may be determined by the addition of a cromogenetic substrate (i.e. colour producing compound) and hydrogen peroxide. The enzyme catalyses the reduction of the substrate to a coloured compound and the resultant degree of absorbency provides a measure of the enzyme activity. If the serum contains no antibodies there will be no enzyme activity, on the other hand if there is much antibody present there will be very considerable enzyme activity. A standard curve can be drawn showing enzyme activity as a function of the concentration of antibodies. This may be used to estimate the content of antibodies in unknown serum samples by interpolation.
  • peroxidase substrates are aromatic amines and include diaminobenziden (DAB), 3,3′-diamino benzid tetra hydrochloride, 3,3′,5,5′-tetra methyl benzidin (TMD).
  • DAB diaminobenziden
  • TMD 3,3′-diamino benzid tetra hydrochloride
  • TMD 3,3′,5,5′-tetra methyl benzidin
  • OPD o-phenylendiamine
  • OPD In addition to being used as a substrate in immuno-chemical assays OPD is used to dye hair. In this connection too it is desirable to substitute a dangerous material with one less dangerous so that the user is not exposed to danger by coming into contact with it. To protect the hands against the dangerous material it is normal for gloves to be used while the hair dye is being applied. Gloves cannot, of course, protect the scalp of the person to whom the dye is applied.
  • the temporary hair dyes are only intended to change the natural hair colour for a short period of time and usually functions by depositing dyes on the surface of the hair. Such hair dyes are easy to remove with normal shampooing.
  • the colour of the dyed hair can survive for five or more shampooings. This is achieved by using dyes having a high affinity for hair keratin and which is able penetrate into the interior of the hair shaft.
  • Permanent hair dyes are very durable to sunlight, shampooing and other hair treatments and need only to be refreshed once a month as new hair grows out. With these dyeing systems the dyes are created directly in and on the hair.
  • Small aromatic colourless dye precursors e.g. p-phenylene-diamine, o-aminophenol, o-phenylendiamine (OPD)
  • OPD o-phenylendiamine
  • modifiers or couplers
  • a number of hair colour tints can be obtained.
  • Cathecol and Resorcinol are examples of such modifiers.
  • H 2 O 2 is used as the oxidizing agent (colour builder), but also as a bleaching agent.
  • Dyeing compositions comprising H 2 O 2 are often referred to as “lightening dyes” due to this lightening effect of H 2 O 2 .
  • H 2 O 2 damages the hair. Further, oxidative dyeing often demands high pH (normally around pH 9-10), which also inflicts damage on the hair and on the skin. Consequently, if using dye compositions comprising H 2 O 2 it is not recommendable to dye the hair often.
  • U.S. Pat. No. 3,251,742 (Revlon) describes a method for dyeing human hair by dye formation in situ (i.e. on the hair).
  • An oxidation enzyme is used for the colour formation reactions at a substantially neutral pH (7-8.5). Laccases, tyrosinases, polyphenolases and catacolases are mentioned as suitable oxidation enzymes.
  • the hair colour pigment is formed by controlled oxidation of various quinone-forming compounds and mono or poly aromatic amines having the amino groups on the aromatic rings to form natural appearing pigments.
  • dye precursors are 2-amino-4-nitrophenol, p-phenylene diamine, m-phenylene diamine, o-phenylene diamine, 2-amino-1,4-naphthoquenone, m-aminophenol, p-aminophenol, o-aminophenol, 2-amino resorcinol, 1,2,4-benzene triamine, nitro-p-phenylene diamine, 2-amino-5-diethyl amino toluene.
  • EP patent no. 504.005 (Perma S.A.) concerns dyeing compositions for keratinous fibres, in particular hair, which do not require the presence of H 2 O 2 (hydrogen peroxide).
  • the composition comprises an enzyme capable of catalysing the formation of the polymeric dyes and also dye precursors, such as bases and couplers, in a buffer solution wherein the pH of said composition is between 6.5 and 8 and said enzyme has an optimal activity in the pH range between 6.5 and 8.
  • Rhizoctonia praticola laccase and Rhus vernicifera laccase are exemplified as the oxidation enzyme to oxidize the dye precursor(s).
  • dye precursors are specifically mentioned: p-phenylene diamine, o-aminophenol, p-methylaminophenol, p-aminophenol, p-toluylenediamine and N-phenyl-p-phenylene diamine.
  • the aim of the present invention is to use the present findings to make available a substrate which to all intents and purposes is non-toxic, non-mutagenic and/or non-carcinogenic and which may be used in immuno-chemical assays, for the dying of keratinous fibres, in particular hair and for dying both natural and synthetic fibres, e.g. textiles.
  • This aim is achieved by utilising the discovery of a substrate which includes the group with the general formulae shown in 1.
  • R is an amino, mono- or a distributed amino or OR′, where R is H, alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl or substituted phenyl.
  • X, Y and Z may each be any one of the following: alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl, substituted phenyl, amino, hydroxy or mercapto with the proviso that at least one of the groups X, Y and Z is an amino group or an amino salt.
  • a substrate is made available which includes a connection with formula 1 where R′ is a methyl, ethyl or isopropyl group.
  • the substrate is a benzoic acid ester, in particular 3,4-diaminobenzoic acid methyl ester (DABA-Me), 3,4-diaminibenzoic acid ethyl ester and 3,4-diamino benzoic acid isopropyl ester.
  • DABA-Me 3,4-diaminobenzoic acid methyl ester
  • ethyl ester 3,4-diaminibenzoic acid ethyl ester
  • 3,4-diamino benzoic acid isopropyl ester isopropyl ester.
  • PABA p-amino benzoic acid
  • 3,4-DABA is a considerably poorer substrate for peroxidase than is OPD.
  • 3,4-DABA has a higher K m -value at the same V max when compared with OPD.
  • This effect can be countered by modifying the carboxyl group, for example by esterification with an alcohol.
  • the preferred alcohols are methanol, ethanol and isopropanol.
  • Methyl, ethyl and isopropyl esters were examined in connection with enzymes and the materials were shown to have significantly improved properties than 3,4-DABA.
  • ethyl ester was found to have a very high V max , i.e. at the same concentration it gives a very much higher reaction speed than OPD.
  • the product of oxidation is also an amino phenazine.
  • the oxidation product is 4,7-dicarboxy-1,2-diamino phenazine as shown in the following equation.
  • the substrate should have two amino groups at the 3,4-location for the reaction to take place.
  • substrates which have the amino groups at either the 2,3-location or the 2,3,4-location may be used but only if the carboxyl group does not hinder the reaction.
  • Substrates which have the amino group at the para location may also be used to produce a coloured product.
  • An example of this is 3,6-DABA.
  • Compounds with the general formulae 1 are preferably dissolved in DMF (Dimethyl formamide) but other organic solvents may be used for this purpose. If a compound with the general formulae 1 is in the form of a salt it can be dissolved in water and this is preferred when using organic solvents.
  • DMF Dimethyl formamide
  • the invention in another aspect relates to a method for quantitative and/or qualitative analysis of a material of biological interest.
  • a peroxidase enzyme together with a marker is bound to the compound in question.
  • Hydrogen peroxide is then converted with a cromogenetic substrate (i.e. colour forming compound) in the presence of the peroxidase, the substrate includes a bond with the general formulae 1.
  • one of the following substrates are used: the methyl, propyl or isopropyl ester of amino benzoic acid.
  • the coloured product produced by the method of the invention is especially suited to the dying of textiles, thread, yarn, wool, hides and skins and human hair.
  • Other natural fibres such as cotton and silk may also be dyed with the product as may synthetic fibres such as polyamides, polyurethane and polyester.
  • the coloured product may either be made immediately before it is to be used for dying or it may be synthesised in the immediate vicinity of the substance to be dyed. For example this may be done by mixing the substrate and the oxidation system in a person's hair.
  • the dying process may be carried out rinsing the person's hair with a mixture of the substrate of the invention and hydrogen peroxide or an oxidation enzyme. A peroxidase is then added and distributed in the hair. When the desired degree of colouring has been obtained the hair is rinsed with water.
  • the substrate may be mixed with the oxidation system before it is applied to the hair.
  • the substrate may be oxidised with hydrogen peroxide or an oxidation enzyme generating hydrogen peroxidase in the presence of a peroxidase.
  • Peroxidases belongs to the group of enzymes which is known as the oxidoreductases.
  • the group also includes the classes of enzymes dehydrogenase, oxygenase, oxidase, laccase and related enzymes. These enzymes may also be used for as an oxidation system/agent for e.g. dyeing keratinous fibres, such as hair, wool, fur and hides and the like. Dyeing composition and preferred oxidation enzymes will be described further below.
  • oxygen donor is hydrogen peroxide which is used as an electron acceptor.
  • Oxidases employ oxygen as an electron acceptor.
  • Suitable oxidases include catecholoxidase, laccase and o-amino phenoloxidase.
  • Oxidation systems which may be used for the oxidation of the substrate in this connection therefore include peroxidase and hydrogen peroxide as well as oxidases, laccases and related enzymes and oxygen.
  • peroxidase and hydrogen peroxide as well as oxidases, laccases and related enzymes and oxygen.
  • oxygen When the system consists of only an oxidase and oxygen it is only necessary to add the oxidase to the substrate as the oxygen in the air is used as an oxidant.
  • the invention relates to a composition in particular adapted for dyeing keratinous fibres comprises, e.g. hair, fur, hide or wool.
  • a composition in particular adapted for dyeing keratinous fibres comprises, e.g. hair, fur, hide or wool.
  • a preferred use of the composition is as a permanent dye for the dyeing of human hair.
  • the oxidation enzyme is as also indicated above an oxidoreductase, i.e. an enzyme classified under the Enzyme Classification number E.C. 1 (Oxidoreductases) in accordance with the Recommendations (1992) of the International Union of Biochemistry and Molecular Biology (IUBMB)) which catalyses oxidoreduction reactions.
  • E.C. 1 Oxidoreductases
  • oxidoreductase enzymes which catalyse the oxidation of a substrate (an electron or hydrogen donor) by acting on oxygen (O 2 ) and/or a peroxide as the acceptor.
  • Such enzymes include enzymes classified within the enzyme classes comprising oxidases, including E.C. 1.1.3. E.C. 1.2.3, E.C. 1.3.3, E.C. 1.4.3, E.C. 1.5.3, E.C. 1.7.3, E.C. 1.8.3 and E.C. 1.9.3, laccases and related enzymes in E.C. 1.10.3, and peroxidases in E.C. 1.11.
  • Laccases or related enzymes which act on molecular oxygen and yield water (H 2 O) without any need for peroxide (e.g. H 2 O 2 ),
  • Oxidases which act on molecular oxygen (O 2 ) and yield peroxide (H 2 O 2 ), and
  • Peroxidases which act on peroxide (e.g. H 2 O 2 ) and yield water (H 2 O).
  • enzyme systems which comprise a combination of more than one enzyme from a single class or from different classes among the three types of enzymes are contemplated.
  • a single enzyme for the sake of simplicity, it is to be understood that the description is generally applicable to such combinations of more than one enzyme.
  • the invention is generally described in terms of the preferred aspect relating to the dyeing of hair, it is to be understood that the description is generally applicable to compositions according to the invention adapted for dyeing of other types of keratinous fibres.
  • laccases and related enzymes are laccases and related enzymes, the term “laccases and related enzymes” including enzymes comprised by the enzyme classification E.C. 1.10.3.2 (laccases) and catechol oxidase enzymes comprised by E.C. 1.10.3.1, bilirubin oxidase enzymes comprised by the enzyme classification E.C. 1.3.3.5 and mono-phenol mono-oxygenase enzymes comprised by the enzyme classification E.C. 1.14.99.1. Laccases are multi-copper containing enzymes that catalyze the oxidation of phenols and aromatic amines.
  • Laccase-mediated oxidation results in the production of aryloxy-radical intermediates from suitable phenolic substrates; the ultimate coupling of the intermediates so produced provides a combination of dimeric, oligomeric, and polymeric reaction products. Certain reaction products can be used to form dyes suitable for dyeing hair.
  • the laccase employed may be derived from a strain of Polyporus sp., in particular a strain of P. pinsitus or P. versicolor , a strain of Myceliophthora sp., e.g. M. thermophila, a strain of Rhizoctonia sp., in particular a strain of Rh. praticola or Rh. solani, a strain of a Rhus sp., in particular Rhus vernicifera, a strain of Pyricularia sp, in particular P. oryzae, or a strain of Scytalidium, such as S. thermophilium.
  • the oxidoreductase is a laccase such as a Polyporus sp. laccase, especially the Polyporus pinisitus laccase (also called Trametes villosa laccase) described in WO 96/00290 (from Novo Nordisk Biotec Inc.) or a Myceliophthora sp. laccase, especially the Myceliophthora thermophila laccase described in WO 95/33836 (from Novo Nordisk Biotech Inc.).
  • a laccase such as a Polyporus sp. laccase, especially the Polyporus pinisitus laccase (also called Trametes villosa laccase) described in WO 96/00290 (from Novo Nordisk Biotec Inc.) or a Myceliophthora sp. laccase, especially the Myceliophthora thermophila laccase described in WO 95/33836 (from Novo Nordisk Biotech Inc.).
  • the laccase may be a Scytalidium sp. laccase such as the S. thermophilium laccase described in WO 95/33837 and WO 97/19998 (from Novo Nordisk Biotech Inc.), the contents of which is incorporated herein by reference, or a Pyricularia sp. laccase, such as the Pyricularia oryzae laccase which can be purchased from SIGMA under the trade name SIGMA No. L5510, or a Coprinus sp. laccase, such as a C. cinereus laccase, especially a C. cinereus IFO 30116 laccase, or a Rhizoctonia sp. laccase, such as a Rh. solani laccase, especially the neutral Rh. solani laccase described WO 95/07988 (from Novo Nordisk A/S) having a pH optimum in the range from 6.0 to 8.5.
  • a Pyricularia sp. laccase such as the Pyricularia oryzae laccase which can be
  • the laccase may also be derived from a fungus such as Collybia, Fomes, Lentinus, Pleurotus, Aspergillus, Neurospora, Podospora, Phlebia, e.g. P. radiata (WO 92/01046), Coriolus sp., e.g. C. hirsitus (JP 2-238885), or Botrytis.
  • a fungus such as Collybia, Fomes, Lentinus, Pleurotus, Aspergillus, Neurospora, Podospora, Phlebia, e.g. P. radiata (WO 92/01046), Coriolus sp., e.g. C. hirsitus (JP 2-238885), or Botrytis.
  • Bilirubin oxidase may preferably be derived from a strain of Myrothecium sp., such as M. verrucaria.
  • the substrates i.e. dye precursors
  • the substrates may according to the dyeing composition of the invention be any of the above within the definition of the general formulae 1.
  • Preferred dye precursors are benzoic acid esters, especially diamino benzoic acid esters, in particular 3,4-diamino benzoic acid methyl ester (DABA-Me), 3,4-diamino benzoic acid ethyl ester and 3,4-diamino benzoic acid isopropyl ester.
  • DABA-Me 3,4-diamino benzoic acid methyl ester
  • ethyl ester 3,4-diamino benzoic acid isopropyl ester.
  • the substrate may also be oxidised by a number of inorganic compounds, among these are compounds which include hypochlorite (ClO ⁇ ), hypobromite (BrO ⁇ ), permanganate (MnO 4 ⁇ ) dicromate (Cr 2 O 7 2 ⁇ ) and the iron ion (Fe 3+ ).
  • inorganic compounds among these are compounds which include hypochlorite (ClO ⁇ ), hypobromite (BrO ⁇ ), permanganate (MnO 4 ⁇ ) dicromate (Cr 2 O 7 2 ⁇ ) and the iron ion (Fe 3+ ).
  • Oxidation systems are taken to be either an oxidant per se or a combination of an enzyme and an oxidant.
  • Modifiers typically incorporation in a dye compositions include m-aromatic diamines, m-aminophenols, polyphenols, amino naphthalines or naphthols.
  • the modifier reacts with the dye precursor in the presence of the oxidative enzyme or the like, converting it into a coloured compound.
  • Couplers examples include m-phenylene-diamine, 2,4-diaminoanisole, 1-hydroxynaphthalene ( ⁇ -naphthol), 1,4-dihydroxybenzene(hydroquinone), 1,5-dihydroxynapthalene, 1,2-dihydroxybenzene(pyrocatechol), 1,3-dihydroxybenzene (resorcinol), 1,3-dihydroxy-2-methylbenzene, 1,3-dihydroxy-4-chlorobenzene(4-chlororesorcinol), 1,2,3,trihydroxybenzene, 1,2,4-trihydroxybenzene, 1,2,4-trihydroxy-5-methylbenzene, and 1,2,4-trihydroxytoluene.
  • the invention relates to a method for dyeing keratinous fibres, in particular hair, fur, hide and wool, using a composition as described above.
  • the dyeing method can be conducted with one or more dye precursors (i.e. substrates of the invention) and optionally in combination with one or more modifiers.
  • the amount of dye precursor(s) and other ingredients used in the composition of the invention for this purpose are in accordance with usual commercial amounts and therefore known for the skilled person.
  • Hair dyeing is typically carried out at or near room temperature, preferably around the optimum temperature of the enzyme being used, and at a pH in the range of from 3.0 to 9.0, preferably 4.0 to 8.5, especially 6.0 to 8.0.
  • Dye precursors (i.e. substrates of the invention) and optional modifiers are described above.
  • esters were made starting from 4-amino-3-nitrotoluene, followed by the esterification and reduction of 4-amino-3-nitrobenzoicacid esters to 3,4-diamino benzoic acidester. The reactions are shown below.
  • methyl ester may be prepared by bubbling hydrochloric acid gas through a solution of 3,4-DABA containing methanol. This last method finds only limited use in the production of the ethyl ester and cannot be used to produce the isopropyl ester.
  • UV spectra were taken of OPD as well as the methyl, ethyl and isopropyl esters.
  • esters absorb at the same wavelength. At 237.5 nm there is a slight increase in extinction with increasing molecular weight of the alkyl group. 3,4-DABA-esters show a typical maximum at 277.5 nm. This maximum is not found in OPD because of the ester carbonyl group.
  • Absorbancy at 492 nm was used as a measure of the course of the reaction. The initial velocity was taken to be the absorbancy at 492 nm two minutes after the addition of the peroxidase to a mixture of the substrate and hydrogen peroxide in a buffer with a pH of 5.0.
  • the wavelength of 492 nm was chosen because it is employed in the standard assay procedures for OPD. None of the substrates has a specially high absorption at this wavelength.
  • V init V max 1 + K m [ S ]
  • K m is defined as the concentration of the substrate at V max /2. A small K m value will therefore be characteristic for an enzyme system where a low concentration of the substrates produces saturation of the enzyme.
  • the peroxidase system has an extremely complicated energy balance (Arnoa et al. (1990)) for short periods of less than a minute the system may nevertheless be described in terms of the above given formulae.
  • a 50 mM phosphate/citrate buffer with a pH of 5.0 was made by mixing a 50 mm Na 2 HPO 4 solution and a 50 mm solution of citric acid. The pH was measured while mixing was in progress.
  • the stabilizing buffer for peroxidase i.e. a buffer which stabilizes the enzyme, was prepared according to the method of Olsen and Little (1983). A 0.1M Na-acetate buffer, which was 0.5M in terms of CaCl 2 was adjusted to pH 5.6.
  • the standard peroxidase solution was diluted to 1:1000 with the 10 ml assay-buffer solution in 10 ⁇ l standard solution.
  • the standard solutions were diluted by 1:10 with the assay buffer. Before being used the substrate solutions were diluted by 1:10. 0.5 ml of the standard solution was thinned down with 4.5 ml of the assay buffer.
  • the total volume is then as follows: 300 ⁇ I DMF and substrate solution, 1550 ⁇ l buffer, 100 ⁇ l bench solution of peroxidase and 50 ⁇ l hydrogen peroxide solution. That is 2000 ⁇ l in total.
  • TABLE 4 Substrate ⁇ l substrate ⁇ l 10% DMF- concentration solution solution ( ⁇ mol/l) 0 300 0 5 295 25 10 290 50 15 285 75 20 280 100 25 275 125 30 270 150 35 265 175 40 260 200 50 250 250 60 240 300 80 220 400 100 200 500 150 150 750 200 100 1000 300 0 1500
  • Table 5 contains information about the values measured for K m , V max and K kat for the five compounds. TABLE 5 K m V max K kat Substrate ( ⁇ mol/ ⁇ l) (min ⁇ 1 ) (1*mol ⁇ 1 *min ⁇ 1 ) OPD 47.35 0.16 1.6 * 10 8 3,4-DABA 251.22 0.20 2.0 * 10 8 methyl 125.97 0.22 2.2 * 10 8 ester ethyl 212.39 0.27 2.7 * 10 8 ester isopropyl 118.46 0.22 2.2 * 10 8 ester
  • FIG. 1 +L-5 is a graphic representation of the result of the measurement of initial velocity on OPD, 3,4-DABA, 3,4-DABA-methyl ester, 3,4-DABA-ethyl ester, 3,4-DABA-isopropyl ester.
  • the Ames test (Maron and Ames (1983)) was used to determine the mutagenic properties of the compounds. Nutrient media were prepared in the manner described by Venitt and Parry (1984). To 3 ⁇ 2 ml melted agar at 45° C. were added 100 ⁇ l of 50, 100 and 200 mM of solutions of the compounds dissolved in DMSO. By means of a pipette 100 ⁇ l of a well-grown culture of Salmonella tphimurium TA 98 (BIO-TEST gl. skolevej 47, 6731 Tiaereborg) were added to the same test-tube.
  • the bacteria contain a frameshift mutation on the histinol-dehydrogenase gene and require histidin in order to grow. Mutagenic aromatic amines can cause the bacteria to mutate to His+ and they can then grow on the nutrient medium. The number of colonies after incubation therefore give a quantitative measure of the ability of the added compound to cause mutation. In all trials spontaneous mutations take place in the absence of a mutagen. These provide a measure of “background” mutation.
  • OPD is not a direct mutagen, it must first be activated by the liver enzyme system P450. All trials were therefore carried out both with and without the addition of “S9-mix” from the livers of rats, this contains the P450 system. 0.5 ml of “59-mix” was added to each test-tube. The criteria for mutation are that increasing concentrations of the compound under investigation give a marked increase in the number of His+ mutants. The results of these trial are given in FIG. 7 +L-11. It may be seen from this figure that only OPD has mutagenic properties.
  • Dye precursor solutions were prepared by mixing the indicated modifier so that the final concentration in the dyeing solution was 0.1% w/w with respect to dye precursor (i.e. substrate of the invention) and 0.1% w/w with respect to modifier.
  • the hair tresses were then rinsed with running water, washed with shampoo, rinsed with water, combed, and air dried.
  • the keratinous fibers can be dyed using DABA-Me and a modifier.

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Abstract

The invention relates to substrates, which develops colour on oxidation of the general formula 1
Figure US20020004958A1-20020117-C00001
The invention also relates to the use of said substrates for dyeing e.g. keratinous fibers, in particular hair, dyeing textiles, a dyeing composition and a method for dyeing keratinous fibers.

Description

    FIELD OF THE INVENTION
  • The present invention concerns the use of aminobenzoic acid (DABA) as a substitute for e.g. o-phenylendiamine (OPD) in analyses based on peroxidases as well as a dyeing substrate (i.e. a dye precursor) in dyeing compositions, and as an substrate for dyeing natural and synthetic fibres including textiles, thread and yarns. The invention also relates to a composition adapted for dyeing keratinous fibres, e.g. hair, wool, fur and hides, and a method for dyeing such keratinous fibres. [0001]
  • BACKGROUND OF THE INVENTION
  • Immuno-chemical Assays [0002]
  • Several different substrates are known in the part to be used for enzyme systems in connection with peroxidase-based immuno- hemical assays, for example ELISA. These substrates are often toxic, mutagenic or carcinogenic. [0003]
  • ELISA (Enzyme Linked Immuno Sorbent Assay) is a method used to assess the amount of antibody in serum. The main principle is that in a much diluted solution many antigens will become bound to the surface of plastic. Thus, if a much diluted solution of antigens is incubated for a time in plastic trays it is possible to wash the cavities in a buffer solution and still retain the film of antigens on the surface of the plastic. If it is required to determine the amount of antibodies in, for instance, serum then the trays with their deposits of antigens are incubated with the serum. The antibodies attach themselves to the antigens and, after thorough washing the trays are again incubated this time with a marker, for example anti-immune globulin serum to which there is attached a suitable enzyme by covalent bonding. In this particular case peroxidase is used. [0004]
  • The peroxidase-marker complex will attach itself to those locations where there is already a deposit of antibodies. After thorough washing to remove all un-combined material the enzyme activity is measured, normally by the use of a suitable colour indicator. Enzyme activity may be determined by the addition of a cromogenetic substrate (i.e. colour producing compound) and hydrogen peroxide. The enzyme catalyses the reduction of the substrate to a coloured compound and the resultant degree of absorbency provides a measure of the enzyme activity. If the serum contains no antibodies there will be no enzyme activity, on the other hand if there is much antibody present there will be very considerable enzyme activity. A standard curve can be drawn showing enzyme activity as a function of the concentration of antibodies. This may be used to estimate the content of antibodies in unknown serum samples by interpolation. [0005]
  • Many of the peroxidase substrates are aromatic amines and include diaminobenziden (DAB), 3,3′-diamino benzid tetra hydrochloride, 3,3′,5,5′-tetra methyl benzidin (TMD). Another peroxidase substrate, which does not belong to the group of aromatic amines, is 2,2-azino-di (3-ethyl-benzo thiazolin-6-sulphonic acid) (ABTS), this has been used as a standard for the establishment of the activity of peroxidase preparations. According to Voogd, Van der Stel and Jacobs (1980) this material is also a mutagent. [0006]
  • o-phenylendiamine (OPD) is another peroxidase substrate which is widely used in hospital and development laboratories. OPD is known to be both mutagenic and carcinogenic. [0007]
  • The staff of laboratories in which analyses involving the use of toxic, mutagenic or carcinogenic materials are carried out are exposed to a significant degree of risk of coming into direct contact with these materials. In order to provide a safe working environment considerable efforts are now made to substitute these dangerous materials with less dangerous ones. [0008]
  • Hair Dyeing Composition [0009]
  • In addition to being used as a substrate in immuno-chemical assays OPD is used to dye hair. In this connection too it is desirable to substitute a dangerous material with one less dangerous so that the user is not exposed to danger by coming into contact with it. To protect the hands against the dangerous material it is normal for gloves to be used while the hair dye is being applied. Gloves cannot, of course, protect the scalp of the person to whom the dye is applied. [0010]
  • In general hair dyeing compositions on the market today can be divided into three main groups: [0011]
  • temporary hair dyes, [0012]
  • semi-permanent hair dyes, and [0013]
  • permanent oxidative hair dyes. [0014]
  • The temporary hair dyes are only intended to change the natural hair colour for a short period of time and usually functions by depositing dyes on the surface of the hair. Such hair dyes are easy to remove with normal shampooing. [0015]
  • When using semi-permanent hair dyes the colour of the dyed hair can survive for five or more shampooings. This is achieved by using dyes having a high affinity for hair keratin and which is able penetrate into the interior of the hair shaft. [0016]
  • Permanent hair dyes are very durable to sunlight, shampooing and other hair treatments and need only to be refreshed once a month as new hair grows out. With these dyeing systems the dyes are created directly in and on the hair. Small aromatic colourless dye precursors (e.g. p-phenylene-diamine, o-aminophenol, o-phenylendiamine (OPD)) penetrate deep into the hair where said dye precursors are oxidised by an oxidising agent into coloured polymeric compounds. These coloured compounds are larger than the dye precursors and can not be washed out of the hair. [0017]
  • By including compounds referred to as modifiers (or couplers) in the hair dyeing composition a number of hair colour tints can be obtained. Cathecol and Resorcinol are examples of such modifiers. [0018]
  • Some of the today most widely used dye precursors such as OPD are known to be both mutagenic and carcinogenic. [0019]
  • Further, traditionally H[0020] 2O2 is used as the oxidizing agent (colour builder), but also as a bleaching agent. Dyeing compositions comprising H2O2 are often referred to as “lightening dyes” due to this lightening effect of H2O2.
  • The use of H[0021] 2O2 in dyeing compositions have some disadvantages as H2O2 damages the hair. Further, oxidative dyeing often demands high pH (normally around pH 9-10), which also inflicts damage on the hair and on the skin. Consequently, if using dye compositions comprising H2O2 it is not recommendable to dye the hair often.
  • To overcome the disadvantages of using H[0022] 2O2 it has been suggested to use oxidation enzymes to replace H2O2.
  • U.S. Pat. No. 3,251,742 (Revlon) describes a method for dyeing human hair by dye formation in situ (i.e. on the hair). An oxidation enzyme is used for the colour formation reactions at a substantially neutral pH (7-8.5). Laccases, tyrosinases, polyphenolases and catacolases are mentioned as suitable oxidation enzymes. The hair colour pigment is formed by controlled oxidation of various quinone-forming compounds and mono or poly aromatic amines having the amino groups on the aromatic rings to form natural appearing pigments. Specifically mentioned dye precursors are 2-amino-4-nitrophenol, p-phenylene diamine, m-phenylene diamine, o-phenylene diamine, 2-amino-1,4-naphthoquenone, m-aminophenol, p-aminophenol, o-aminophenol, 2-amino resorcinol, 1,2,4-benzene triamine, nitro-p-phenylene diamine, 2-amino-5-diethyl amino toluene. [0023]
  • EP patent no. 504.005 (Perma S.A.) concerns dyeing compositions for keratinous fibres, in particular hair, which do not require the presence of H[0024] 2O2 (hydrogen peroxide). The composition comprises an enzyme capable of catalysing the formation of the polymeric dyes and also dye precursors, such as bases and couplers, in a buffer solution wherein the pH of said composition is between 6.5 and 8 and said enzyme has an optimal activity in the pH range between 6.5 and 8. Rhizoctonia praticola laccase and Rhus vernicifera laccase are exemplified as the oxidation enzyme to oxidize the dye precursor(s). The following dye precursors are specifically mentioned: p-phenylene diamine, o-aminophenol, p-methylaminophenol, p-aminophenol, p-toluylenediamine and N-phenyl-p-phenylene diamine.
  • The aim of the present invention is to use the present findings to make available a substrate which to all intents and purposes is non-toxic, non-mutagenic and/or non-carcinogenic and which may be used in immuno-chemical assays, for the dying of keratinous fibres, in particular hair and for dying both natural and synthetic fibres, e.g. textiles. This aim is achieved by utilising the discovery of a substrate which includes the group with the general formulae shown in 1. [0025]
    Figure US20020004958A1-20020117-C00002
  • wherein [0026]
  • R is an amino, mono- or a distributed amino or OR′, where R is H, alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl or substituted phenyl. X, Y and Z may each be any one of the following: alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl, substituted phenyl, amino, hydroxy or mercapto with the proviso that at least one of the groups X, Y and Z is an amino group or an amino salt. [0027]
  • In a special embodiment of the invention a substrate is made available which includes a connection with formula 1 where R′ is a methyl, ethyl or isopropyl group. [0028]
  • In an preferred embodiment the substrate is a benzoic acid ester, in particular 3,4-diaminobenzoic acid methyl ester (DABA-Me), 3,4-diaminibenzoic acid ethyl ester and 3,4-diamino benzoic acid isopropyl ester. [0029]
  • Comparison of the very toxic aniline with the carboxyl acid derivative of aniline, p-amino benzoic acid (PABA) shows that the toxicity of the molecule is radically altered by the addition of the carboxyl group. PABA is generally considered to be non-toxic and, among other applications, is used as an ultra violet filter in sun lotions. If the substrate OPD is thought of along the same lines it can be seen that a possible analogue is 3,4-diamino benzoic acid (3,4-DABA). This material is comparatively cheap and readily obtainable. [0030]
    Figure US20020004958A1-20020117-C00003
  • Investigation using enzymes showed that 3,4-DABA is a considerably poorer substrate for peroxidase than is OPD. In other words 3,4-DABA has a higher K[0031] m-value at the same Vmax when compared with OPD. This is apparently due to the carboxyl group's inductive (deactivating) effect upon the aromatic ring. This effect can be countered by modifying the carboxyl group, for example by esterification with an alcohol. The preferred alcohols are methanol, ethanol and isopropanol. Methyl, ethyl and isopropyl esters were examined in connection with enzymes and the materials were shown to have significantly improved properties than 3,4-DABA. Especially the ethyl ester was found to have a very high Vmax, i.e. at the same concentration it gives a very much higher reaction speed than OPD.
  • The reaction mechanism for the oxidation of OPD with, for instance, hydrogen peroxide, both with and without an enzyme, is described by the following equations: [0032]
    Figure US20020004958A1-20020117-C00004
  • It may be seen from this that the product of oxidation is 2,3-diamino phenazin. [0033]
  • When one of the compounds described here is employed the product of oxidation is also an amino phenazine. In the case of 3,4-DABA the oxidation product is 4,7-dicarboxy-1,2-diamino phenazine as shown in the following equation. [0034]
    Figure US20020004958A1-20020117-C00005
  • The substrate should have two amino groups at the 3,4-location for the reaction to take place. However, substrates which have the amino groups at either the 2,3-location or the 2,3,4-location may be used but only if the carboxyl group does not hinder the reaction. [0035]
  • Substrates which have the amino group at the para location may also be used to produce a coloured product. An example of this is 3,6-DABA. [0036]
  • In order to counteract the carboxyl groups inductive effect (i.e. deactivation of the aromatic ring caused by the groups attractive effect upon electrons) esterification of the carboxyl group was investigated using electron donating groups to see if deactivation could be counteracted while at the same time retaining non-mutagenic attributes. To investigate the effect of different alkyl groups on the material's enzymatic properties as well as possible mutagenic properties the methyl, ethyl and isopropyl esters of 3,4-DABA were synthesised. [0037]
  • Compounds with the general formulae 1 are preferably dissolved in DMF (Dimethyl formamide) but other organic solvents may be used for this purpose. If a compound with the general formulae 1 is in the form of a salt it can be dissolved in water and this is preferred when using organic solvents. [0038]
  • In another aspect the invention relates to a method for quantitative and/or qualitative analysis of a material of biological interest. In this case a peroxidase enzyme together with a marker is bound to the compound in question. Hydrogen peroxide is then converted with a cromogenetic substrate (i.e. colour forming compound) in the presence of the peroxidase, the substrate includes a bond with the general formulae 1. [0039]
  • In a preferred embodiment of the method of the invention one of the following substrates are used: the methyl, propyl or isopropyl ester of amino benzoic acid. [0040]
  • In those cases where the material of biological interest is an antigen the associated antibody is used. In this connection other combinations will suggest themselves to the skilled person. [0041]
  • The coloured product produced by the method of the invention is especially suited to the dying of textiles, thread, yarn, wool, hides and skins and human hair. Other natural fibres such as cotton and silk may also be dyed with the product as may synthetic fibres such as polyamides, polyurethane and polyester. [0042]
  • The coloured product may either be made immediately before it is to be used for dying or it may be synthesised in the immediate vicinity of the substance to be dyed. For example this may be done by mixing the substrate and the oxidation system in a person's hair. [0043]
  • The dying process may be carried out rinsing the person's hair with a mixture of the substrate of the invention and hydrogen peroxide or an oxidation enzyme. A peroxidase is then added and distributed in the hair. When the desired degree of colouring has been obtained the hair is rinsed with water. [0044]
  • The substrate may be mixed with the oxidation system before it is applied to the hair. As stated above the substrate may be oxidised with hydrogen peroxide or an oxidation enzyme generating hydrogen peroxidase in the presence of a peroxidase. [0045]
  • Peroxidases belongs to the group of enzymes which is known as the oxidoreductases. The group also includes the classes of enzymes dehydrogenase, oxygenase, oxidase, laccase and related enzymes. These enzymes may also be used for as an oxidation system/agent for e.g. dyeing keratinous fibres, such as hair, wool, fur and hides and the like. Dyeing composition and preferred oxidation enzymes will be described further below. [0046]
  • In oxidation reactions which are catalysed by the enzyme peroxidase the oxygen donor is hydrogen peroxide which is used as an electron acceptor. Oxidases employ oxygen as an electron acceptor. [0047]
  • Examples of suitable oxidases include catecholoxidase, laccase and o-amino phenoloxidase. [0048]
  • Oxidation systems which may be used for the oxidation of the substrate in this connection therefore include peroxidase and hydrogen peroxide as well as oxidases, laccases and related enzymes and oxygen. When the system consists of only an oxidase and oxygen it is only necessary to add the oxidase to the substrate as the oxygen in the air is used as an oxidant. [0049]
  • Dyeing Composition [0050]
  • In an aspect the invention relates to a composition in particular adapted for dyeing keratinous fibres comprises, e.g. hair, fur, hide or wool. Comprising 1) at least one oxidation enzyme 2) at least one substrate as defined by the formulae 1 and optionally 3) at least one modifier. [0051]
  • A preferred use of the composition is as a permanent dye for the dyeing of human hair. [0052]
  • The oxidation enzyme is as also indicated above an oxidoreductase, i.e. an enzyme classified under the Enzyme Classification number E.C. 1 (Oxidoreductases) in accordance with the Recommendations (1992) of the International Union of Biochemistry and Molecular Biology (IUBMB)) which catalyses oxidoreduction reactions. [0053]
  • Within the class of oxidoreductase enzymes are preferred enzymes which catalyse the oxidation of a substrate (an electron or hydrogen donor) by acting on oxygen (O[0054] 2) and/or a peroxide as the acceptor. Such enzymes include enzymes classified within the enzyme classes comprising oxidases, including E.C. 1.1.3. E.C. 1.2.3, E.C. 1.3.3, E.C. 1.4.3, E.C. 1.5.3, E.C. 1.7.3, E.C. 1.8.3 and E.C. 1.9.3, laccases and related enzymes in E.C. 1.10.3, and peroxidases in E.C. 1.11.
  • According to the invention three types of oxidoreductases are specifically contemplated: [0055]
  • a) Laccases or related enzymes, which act on molecular oxygen and yield water (H[0056] 2O) without any need for peroxide (e.g. H2O2),
  • b) Oxidases, which act on molecular oxygen (O[0057] 2) and yield peroxide (H2O2), and
  • c) Peroxidases, which act on peroxide (e.g. H[0058] 2O2) and yield water (H2O).
  • Also, enzyme systems which comprise a combination of more than one enzyme from a single class or from different classes among the three types of enzymes are contemplated. In the present specification, although reference will often be made to a single enzyme for the sake of simplicity, it is to be understood that the description is generally applicable to such combinations of more than one enzyme. Further, although the invention is generally described in terms of the preferred aspect relating to the dyeing of hair, it is to be understood that the description is generally applicable to compositions according to the invention adapted for dyeing of other types of keratinous fibres. [0059]
  • Particularly preferred enzymes are laccases and related enzymes, the term “laccases and related enzymes” including enzymes comprised by the enzyme classification E.C. 1.10.3.2 (laccases) and catechol oxidase enzymes comprised by E.C. 1.10.3.1, bilirubin oxidase enzymes comprised by the enzyme classification E.C. 1.3.3.5 and mono-phenol mono-oxygenase enzymes comprised by the enzyme classification E.C. 1.14.99.1. Laccases are multi-copper containing enzymes that catalyze the oxidation of phenols and aromatic amines. Laccase-mediated oxidation results in the production of aryloxy-radical intermediates from suitable phenolic substrates; the ultimate coupling of the intermediates so produced provides a combination of dimeric, oligomeric, and polymeric reaction products. Certain reaction products can be used to form dyes suitable for dyeing hair. [0060]
  • Preferably, the laccase employed may be derived from a strain of Polyporus sp., in particular a strain of [0061] P. pinsitus or P. versicolor, a strain of Myceliophthora sp., e.g. M. thermophila, a strain of Rhizoctonia sp., in particular a strain of Rh. praticola or Rh. solani, a strain of a Rhus sp., in particular Rhus vernicifera, a strain of Pyricularia sp, in particular P. oryzae, or a strain of Scytalidium, such as S. thermophilium.
  • In specific embodiments of the invention the oxidoreductase is a laccase such as a Polyporus sp. laccase, especially the [0062] Polyporus pinisitus laccase (also called Trametes villosa laccase) described in WO 96/00290 (from Novo Nordisk Biotec Inc.) or a Myceliophthora sp. laccase, especially the Myceliophthora thermophila laccase described in WO 95/33836 (from Novo Nordisk Biotech Inc.).
  • Further, the laccase may be a Scytalidium sp. laccase such as the [0063] S. thermophilium laccase described in WO 95/33837 and WO 97/19998 (from Novo Nordisk Biotech Inc.), the contents of which is incorporated herein by reference, or a Pyricularia sp. laccase, such as the Pyricularia oryzae laccase which can be purchased from SIGMA under the trade name SIGMA No. L5510, or a Coprinus sp. laccase, such as a C. cinereus laccase, especially a C. cinereus IFO 30116 laccase, or a Rhizoctonia sp. laccase, such as a Rh. solani laccase, especially the neutral Rh. solani laccase described WO 95/07988 (from Novo Nordisk A/S) having a pH optimum in the range from 6.0 to 8.5.
  • The laccase may also be derived from a fungus such as Collybia, Fomes, Lentinus, Pleurotus, Aspergillus, Neurospora, Podospora, Phlebia, e.g. [0064] P. radiata (WO 92/01046), Coriolus sp., e.g. C. hirsitus (JP 2-238885), or Botrytis.
  • Bilirubin oxidase may preferably be derived from a strain of Myrothecium sp., such as [0065] M. verrucaria.
  • The substrates (i.e. dye precursors) may according to the dyeing composition of the invention be any of the above within the definition of the general formulae 1. [0066]
  • Preferred dye precursors (i.e. substrates) are benzoic acid esters, especially diamino benzoic acid esters, in particular 3,4-diamino benzoic acid methyl ester (DABA-Me), 3,4-diamino benzoic acid ethyl ester and 3,4-diamino benzoic acid isopropyl ester. [0067]
  • Other Oxidation Agents [0068]
  • The substrate may also be oxidised by a number of inorganic compounds, among these are compounds which include hypochlorite (ClO[0069] ), hypobromite (BrO), permanganate (MnO4 ) dicromate (Cr2O7 2−) and the iron ion (Fe3+).
  • Oxidation systems are taken to be either an oxidant per se or a combination of an enzyme and an oxidant. [0070]
  • Modifiers [0071]
  • Modifiers typically incorporation in a dye compositions include m-aromatic diamines, m-aminophenols, polyphenols, amino naphthalines or naphthols. The modifier (coupler) reacts with the dye precursor in the presence of the oxidative enzyme or the like, converting it into a coloured compound. Examples of specific modifiers (couplers) include m-phenylene-diamine, 2,4-diaminoanisole, 1-hydroxynaphthalene (α-naphthol), 1,4-dihydroxybenzene(hydroquinone), 1,5-dihydroxynapthalene, 1,2-dihydroxybenzene(pyrocatechol), 1,3-dihydroxybenzene (resorcinol), 1,3-dihydroxy-2-methylbenzene, 1,3-dihydroxy-4-chlorobenzene(4-chlororesorcinol), 1,2,3,trihydroxybenzene, 1,2,4-trihydroxybenzene, 1,2,4-trihydroxy-5-methylbenzene, and 1,2,4-trihydroxytoluene. [0072]
  • Method of Dyeing Keratinous Fibres [0073]
  • In a further aspect the invention relates to a method for dyeing keratinous fibres, in particular hair, fur, hide and wool, using a composition as described above. The dyeing method can be conducted with one or more dye precursors (i.e. substrates of the invention) and optionally in combination with one or more modifiers. The amount of dye precursor(s) and other ingredients used in the composition of the invention for this purpose are in accordance with usual commercial amounts and therefore known for the skilled person. Hair dyeing is typically carried out at or near room temperature, preferably around the optimum temperature of the enzyme being used, and at a pH in the range of from 3.0 to 9.0, preferably 4.0 to 8.5, especially 6.0 to 8.0. Dye precursors (i.e. substrates of the invention) and optional modifiers are described above. [0074]
  • The invention is further illustrated in the following non-limiting example.[0075]
  • EXAMPLE 1
  • Synthesis of 3,4-diamino Benzoic Acid Esters [0076]
  • The esters were made starting from 4-amino-3-nitrotoluene, followed by the esterification and reduction of 4-amino-3-nitrobenzoicacid esters to 3,4-diamino benzoic acidester. The reactions are shown below. [0077]
    Figure US20020004958A1-20020117-C00006
  • The amino group in 4-amino-3-nitrotoluene is protected by boiling in anhydrous acetic acid in acetic acid. The methyl group is oxidized with permanganate in an aqueous solution containing magnesium sulphate. The acetyl group is removed by boiling with 0.1 hydrochloric acid. After isolation and drying 4-amino-3-nitrobenzoicacid is dissolved in absolute alcohol and concentrated sulphuric acid is added. On boiling for two to five hours the acid groups are esterified. The exact boiling time depends on the type of alcohol. The last stage is the reduction of the isolated product with activated iron and water in boiling benzine for about five hours. [0078]
  • When the reaction was complete the iron particles were filtered out and the residue dried for between 24 to 48 hours over anhydrous sodium sulphate. After filtration and evaporation the ester was recrystallised in a mixture of n-butanol and benzine in the ratio of 1 to 10. [0079]
  • The above procedure was used to produce 3,4-DABA esters for measurement of enzymes and for mutagenetic testing. If larger amounts were to be required at a reasonable price then direct esterification of 3,4-DABA would be preferred. Thus the methyl ester may be prepared by bubbling hydrochloric acid gas through a solution of 3,4-DABA containing methanol. This last method finds only limited use in the production of the ethyl ester and cannot be used to produce the isopropyl ester. [0080]
  • Characterization of 3,4-DABA Esters [0081]
  • Thin Layer Chromatography [0082]
  • The DABA esters that were prepared were analysed and compared with the help of thin layer chromatography (TLC) using silica gel plates of the type MERC 60 F[0083] 254 the stock number of the zone of concentration was 5583. A mixture of chloroform, methanol and acetic acid in the ratio of 90:5:5 on a volumetric basis was used as a solvent For the purpose of comparison OPD and 3,4-DABA were analyzed on the same plate. The Rf values obtained are shown in Table 1.
    TABLE 1
    Chemical bond Rf-value
    3,4-DABA 0.15
    OPD 0.19
    Methyl ester 0.29
    Ethyl ester 0.31
    Isopropyl ester 0.33
  • It can be seen from table 1 that the bigger alkyl groups give a measurably greater displacement in the solvent which contains chloroform. The least displacement is seen, as might be expected, with 3,4-DABA which contains a free carboxyl group. All the combinations tested moved in the form of patches which is an indication of their purity. [0084]
  • The fact that the 3,4-DABA esters are lipeds gives no problems with regard to solubility in water when making up solutions of substrates. A standard solution of dimethyl formamide diluted in an aqueous buffer with a pH of 5.0. At high concentrations of substrate oxidation products formed by the action of enzymes may cause slight turbidity in the solution. By reducing the pH to about 1 with 1M sulphuric acid a completely clear solution is produced. This is due to the addition of protons to the amino groups. [0085]
  • Determination of Melting Points [0086]
  • To verify that the materials synthesised were identical with those described in the literature their melting points were determined and compared with values given in a table on page 1532 of Chapman and Hall's Dictionary of Organic Compounds, Fifth Edition, Volume 2. Melting points were determined by the use of the capillary tube method using a silicone oil bath. [0087]
  • Melting points are given in Table 2. [0088]
    TABLE 2
    Material Measured melting point Value from literature
    methyl ester 108-109° C. 108-109° C.
    ethyl ester 112-113° C. 112-113° C.
    isopropyl ester 73-74° C.
  • It can be seen from the above table that there is close agreement between the melting points determined by experiment and the melting points as given in the literature. It may, therefore, reasonably be assumed that the synthesised material are identical with those described in the literature. It was not possible to find a value for the isopropyl ester in the literature. [0089]
  • Ultraviolet Spectroscopy [0090]
  • UV spectra were taken of OPD as well as the methyl, ethyl and isopropyl esters. [0091]
  • Scanning was done from 360 nm to 210 nm using a solution of the compounds in methanol. The concentration was 0.1 /1. Table 3 shows the absorption maxima and the extinction coefficients for the compounds investigated. [0092]
    TABLE 3
    Material Absorption max. Extinction coefficient
    OPD 290.0 nm 2000 M−1
    231.3 nm 3400 M−1
    methyl ester 310.0 nm 6000 M−1
    277.5 nm 6000 M−1
    232.5 nm 8400 M−1
    ethyl ester 310.0 nm 6200 M−1
    277.5 nm 6000 M−1
    232.5 nm 8600 M−1
    isopropyl 310.0 nm 6500 M−1
    ester 277.5 nm 6200 M−1
    232.5 nm 8700 M−1
  • As can be seen from the above table all three esters absorb at the same wavelength. At 237.5 nm there is a slight increase in extinction with increasing molecular weight of the alkyl group. 3,4-DABA-esters show a typical maximum at 277.5 nm. This maximum is not found in OPD because of the ester carbonyl group. [0093]
  • In order to investigate the properties of 3,4-DABA and the three esters with respect to oxidation catalyzed by peroxidase a series of measurements were carried out on the enzymatic reactions initial velocity with increasing concentration of the substrate. Measurements were carried out on OPD,3,4-DABA, 3,4-DABA-methyl ester, 3,4-DABA-ethyl ester, and 3,4-DABA isopropyl ester. [0094]
  • Absorbancy at 492 nm was used as a measure of the course of the reaction. The initial velocity was taken to be the absorbancy at 492 nm two minutes after the addition of the peroxidase to a mixture of the substrate and hydrogen peroxide in a buffer with a pH of 5.0. The wavelength of 492 nm was chosen because it is employed in the standard assay procedures for OPD. None of the substrates has a specially high absorption at this wavelength. [0095]
  • By varying the concentration of the substrate and at the same time measuring the initial velocity of the reaction it is posible to apply the Michaelis/Menten equation to the system. [0096]
  • Under ideal conditions the values determined experimentally will approach the value of the expression: [0097] V init = V max 1 + K m [ S ]
    Figure US20020004958A1-20020117-M00001
  • where [S] is the concentration of the substrate, V[0098] max is the maximum initial concentration which is reached in the particular assay. Km is defined as the concentration of the substrate at Vmax/2. A small Km value will therefore be characteristic for an enzyme system where a low concentration of the substrates produces saturation of the enzyme.
  • The expression implies that the initial velocity will increase with increasing concentration of the substrate, but the curve for the velocity will flatten out and approach V[0099] max for very high concentrations of the substrate. In actual fact the parameter Kkat be calculated as Vmax/[E] where [E] is the molar concentration of the enzyme in the reaction. Kkat is the same as min−1 and reflects the activity of the enzyme in a saturated solution upon the substrate.
  • The peroxidase system has an extremely complicated energy balance (Arnoa et al. (1990)) for short periods of less than a minute the system may nevertheless be described in terms of the above given formulae. [0100]
  • EXAMPLE 2
  • Enzymatic Determination [0101]
  • The following solutions were prepared for use in the enzyme assay: [0102]
  • a) Assay buffer [0103]
  • A 50 mM phosphate/citrate buffer with a pH of 5.0 was made by mixing a 50 mm Na[0104] 2HPO4 solution and a 50 mm solution of citric acid. The pH was measured while mixing was in progress.
  • b) DMF diluted 1:10 [0105]
  • By means of pipette 10 ml were placed in a graduated flask which was then topped up to 100 ml with assay buffer. [0106]
  • c) Solution of hydrogen peroxide 0.018% [0107]
  • 15 μl of a 30% solution of hydrogen peroxide (PERHYDROL, Merck) was thinned down with 25 ml of the assay buffer. [0108]
  • d) Stabilizing buffer for peroxidase [0109]
  • The stabilizing buffer for peroxidase, i.e. a buffer which stabilizes the enzyme, was prepared according to the method of Olsen and Little (1983). A 0.1M Na-acetate buffer, which was 0.5M in terms of CaCl[0110] 2 was adjusted to pH 5.6.
  • 37.5 mg N-acetyl-trimethyl-ammonium-bromide was dissolved in 75 ml of the buffer. To this solution 25 ml of glycerol was added. The enzyme activity is maintained in this buffer because the molecules of the enzyme are prevented from aggregating. [0111]
  • e) Standard solution of peroxidase [0112]
  • 10 mg of horseradish peroxidase type VI-A (Sigma no. 6782) were dissolved in 10 ml of the stabilizing buffer. This was stored at −15° C. This will keep for several months (Olsen and Little (1983). [0113]
  • f) Bench solution of peroxidase [0114]
  • The standard peroxidase solution was diluted to 1:1000 with the 10 ml assay-buffer solution in 10 μl standard solution. [0115]
  • g) Standard solutions of the substrates [0116]
  • 0.5 mmol of each substrate in 5 ml DMF. These solutions will keep for several weeks at −15° C. [0117]
  • h) Bench solutions of the substrates [0118]
  • The standard solutions were diluted by 1:10 with the assay buffer. Before being used the substrate solutions were diluted by 1:10. 0.5 ml of the standard solution was thinned down with 4.5 ml of the assay buffer. [0119]
  • Measurement of the Velocity of Reaction as a Function of the Concentration of the Substrates [0120]
  • For each of the compounds OPD, 3,4-DABA-, and the methyl, ethyl, and isopropyl esters of 3,4-DABA 15 measurements were carried out and absorbency was measured twice in each case at 492 nm one minute after the addition of 100 μl dilute peroxidase solution (bench solution). The concentration of the peroxidase was held constant at 50 ng/ml during the whole investigation. By using the volume of substrate and the volumes of 10 vol-% DMF solution as given in table 4 it was possible to employ a constant reaction volume and a constant concentration of DMF. For all measurements there was used 1550 μl buffer and 50 μl bench solution of peroxidase. The total volume is then as follows: 300 μI DMF and substrate solution, 1550 μl buffer, 100 μl bench solution of peroxidase and 50 μl hydrogen peroxide solution. That is 2000 μl in total. [0121]
    TABLE 4
    Substrate
    μl substrate μl 10% DMF- concentration
    solution solution (μmol/l)
    0 300 0
    5 295 25
    10 290 50
    15 285 75
    20 280 100
    25 275 125
    30 270 150
    35 265 175
    40 260 200
    50 250 250
    60 240 300
    80 220 400
    100 200 500
    150 150 750
    200 100 1000
    300 0 1500
  • Table 5 contains information about the values measured for K[0122] m, Vmax and Kkat for the five compounds.
    TABLE 5
    Km Vmax Kkat
    Substrate (μmol/μl) (min−1) (1*mol−1*min−1)
    OPD 47.35 0.16 1.6 * 108
    3,4-DABA 251.22 0.20 2.0 * 108
    methyl 125.97 0.22 2.2 * 108
    ester
    ethyl 212.39 0.27 2.7 * 108
    ester
    isopropyl 118.46 0.22 2.2 * 108
    ester
  • The results of the measurements of initial velocities are stated in units of absorbency and not in molar units. In order to be able to measure the “true” velocity of reaction it is necessary to isolate the oxidation product for each substrate and determine the molar extinction coefficient. The value of Kkat is worked out from 1 mole of peroxidase of 50,000 g/mol. [0123]
  • FIG. [0124] 1 +L-5 is a graphic representation of the result of the measurement of initial velocity on OPD, 3,4-DABA, 3,4-DABA-methyl ester, 3,4-DABA-ethyl ester, 3,4-DABA-isopropyl ester.
  • As is shown by Table 5 and FIGS. 1 to 6 the carboxyl esters of 3,4-DABA are effective substrates in a peroxidase/hydrogen peroxide system. It is possible to obtain much higher initial velocities with these compounds than with OPD. K[0125] m per se is a poor indicator of the effectiveness in enzyme assays of the substrates in question as it actually only shows the sensitivity of the system at low concentrations of substrate. In practice substrate concentrations would be chosen to allow maximum and linear colour development with different concentrations of enzymes. In other words Vmax and Kkat are more relevant parameters for the comparison of different substrates. It was found that, for all the esters investigated, the values of Vmax and Kkat were considerably larger than the comparable values for OPD.
  • All reaction velocities are expressed as absorption units, this is partly because most practical enzyme essays are based on the measurement of absorption and partly because the products of reaction are not isolated from the reaction mixture. [0126]
  • EXAMPLE 3
  • Determination of the Mutagenicity of the Compounds [0127]
  • The Ames test (Maron and Ames (1983)) was used to determine the mutagenic properties of the compounds. Nutrient media were prepared in the manner described by Venitt and Parry (1984). To 3×2 ml melted agar at 45° C. were added 100 μl of 50, 100 and 200 mM of solutions of the compounds dissolved in DMSO. By means of a pipette 100 μl of a well-grown culture of [0128] Salmonella tphimurium TA 98 (BIO-TEST gl. skolevej 47, 6731 Tiaereborg) were added to the same test-tube. The bacteria contain a frameshift mutation on the histinol-dehydrogenase gene and require histidin in order to grow. Mutagenic aromatic amines can cause the bacteria to mutate to His+ and they can then grow on the nutrient medium. The number of colonies after incubation therefore give a quantitative measure of the ability of the added compound to cause mutation. In all trials spontaneous mutations take place in the absence of a mutagen. These provide a measure of “background” mutation.
  • OPD is not a direct mutagen, it must first be activated by the liver enzyme system P450. All trials were therefore carried out both with and without the addition of “S9-mix” from the livers of rats, this contains the P450 system. 0.5 ml of “59-mix” was added to each test-tube. The criteria for mutation are that increasing concentrations of the compound under investigation give a marked increase in the number of His+ mutants. The results of these trial are given in FIG. [0129] 7 +L-11. It may be seen from this figure that only OPD has mutagenic properties.
  • EXAMPLE 4
  • Dyeing Effect of Dye Precursors of the Invention [0130]
  • The permanent oxidative dyeing effect of different dye precursors using 0.05 mg active enzyme protein [0131] Myceliophthora thermophila laccase (available from Novo Nordisk and described in WO 95/33836) per ml reaction mixture were tested.
  • The dye precursors tested were [0132]
  • 0.1% w/w 3,4 diamino benzoic acid (DABA) in 0.1M K-phosphatebuffer, pH 7.0. [0133]
  • [0134] 0.1% w/w 3,4-diaminobenzoic acid methyl ester (DABA-Me) in 0.1M K-phosphatebuffer, pH 7.0.
  • Modifier used [0135]
  • 0.1% w/w m-phenylenediamine (MPD) in 0.1M K-phosphatebuffer, pH 7.0. [0136]
  • Dye precursor solutions were prepared by mixing the indicated modifier so that the final concentration in the dyeing solution was 0.1% w/w with respect to dye precursor (i.e. substrate of the invention) and 0.1% w/w with respect to modifier. [0137]
  • Hair Dyeing [0138]
  • 1 gram 6″ De Meo Virgin natural white hair tresses (De Meo Brothers Inc. USA) were used. [0139]
  • 4 ml dye precursor solution (including modifier) was mixed with 1 ml laccase on a Whirley mixer, applied to the hair tresses and incubated at 30° C. for 30 minutes. [0140]
  • The hair tresses were then rinsed with running water, washed with shampoo, rinsed with water, combed, and air dried. [0141]
  • a*, b* and L* were determined on the Chroma Meter and ΔE* was then calculated as described below. [0142]
  • Hair tress samples treated without enzyme were used as a blind. [0143]
  • The result of the test is shown in Table 6. [0144]
    TABLE 6
    DABA and DABA-Me
    0.1% w/w dye with/without MPD
    precursor/modifier ΔL Δa Δb ΔE Assessment
    DABA −4.27 −0.63 −2.55 5.01 no colour
    DABA + MPD −23 −2.21 −18.29 29.47 grayish
    DABA-Me −7.58 6.53 −2.14 10.23 light orange
    DABA-Me + MPD −32.31 2.35 −25.07 40.96 grayish
    violet
  • Assessment of the Hair Colour [0145]
  • The quantitative colour of the hair tresses was determined on a Minolta CR200 Chroma Meter by the use the parameters L* (“0”=black and “100”=white), a* (“−”=green and “+”=red) and b* (“−” blue and “+” yellow). [0146]
  • ΔL*, Δa* and Δb* are the delta values of L*, a* and b* respectively compared to L*, a* and b* of untreated hair (e.g. ΔL*=L*[0147] sample−L*untreated hair).
  • ΔE* was calculated as ΔE*=square root(ΔL*[0148] 2+Δa*2+Δb*2) and is an expression for the total quantitative colour change.
  • EXAMPLE 5
  • Dyeing Effect of DAB-Me and Various Modifiers [0149]
  • Using the procedure described in Example 4 the permanent dyeing effect of the dye precursor (i.e. substrates) DABA-Me with various modifiers were tested, except that 0.2% w/w dye precursor and 0.2% modifier were used. [0150]
    TABLE 2
    0.2% DABA-Me and
    0.2% w/w modifier ΔL* Δa* Δb* ΔE* Assessment
    4-chlor-resorcinol −22.36 1.19 −6.28 23.26 Gray-green
    5-amino-o-cresol −14.1 5.69 −2.1 15.35 light
    orange
    m-phenylene-diamine −33.25 2.17 −23.71 40.9 Grey
    (Bluish)
    pyrogallol −29.47 5.74 −7.69 30.99 Brown
    4-methoxy-1,3-phenyl- −39.24 2.33 −19.73 43.98 Brown-gray/
    enediamine black
  • As can be seen the keratinous fibers can be dyed using DABA-Me and a modifier. [0151]

Claims (20)

1. A substrate, which develops colour on oxidation characterized by the inclusion of an amino benzoic acid compound with the general formula 1
Figure US20020004958A1-20020117-C00007
wherein
R is an amino, mono- or a distributed amino or OR′, where R is H, alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl or substituted phenyl, X, Y and Z may each independently be hydrogen alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl, substituted phenyl, amino, hydroxy or mercapto with the proviso that at least one of the groups X, Y and Z is an amino group or an salt thereof.
2. The substrate according to claim 1, wherein R′ is a methyl, ethyl or isopropyl ester.
3. The use of amino benzoic acid compounds with the general formula 1 as well as the salt thereof as a colour producing substrate in analysis based on the use of peroxidase.
4. The use of amino benzoic acid compounds with the general formula 1 as well as the salt thereof as a colour producing substrate in hair dyeing compositions as well as for compositions for dying of natural and synthetic fibres including textiles, thread and yarns.
5. Use according to claims 3 or 4 wherein the compound is selected from the group of methyl, ethyl or isopropyl esters of amino benzoic acid.
6. Method for quantitative and/or qualitative analysis of a material of biological interest, wherein a peroxidase enzyme together with a marker is bound to the compound of interest, hydrogen peroxide is then converted with a colour producing substrate in the presence of the peroxidase, characterized by the use of a substrate selected from the group made up of amino benzoic acid compounds with the general formula 1 as well as its salts.
7. The method according to claim 8 wherein the compound is selected from the group of methyl, ethyl or isopropyl esters of amino benzoic acid as well as its salts.
8. The method according to claim 6 wherein the peroxidase marker is capable of forming an immunological link to the materiel of biological interest.
9. The method according to claim 6 wherein the materiel of biological interest is an antigen and the marker is an antibody to the antigen.
10. Method for producing a colored product wherein the substrate according to claim 1 or 2 is converted by means of an oxidation system.
11. The method according to claim 10, wherein the oxidation system comprises an inorganic compound, preferably one of the compound hypochlorite, hypobromite, permanganate, dichromate, or iron as Fe3+).
12. The method according to claim 10, wherein the oxidation system includes an enzyme and an electron acceptor.
13. The method according to claim 12, wherein the enzyme is a peroxidase and the electron acceptor is hydrogen peroxide or that the enzyme is oxidase and the electron acceptor is oxygen.
14. The method according to claim 13, wherein the oxidase is chosen from the group catechol oxidase, laccase and related enzymes o-amino phenoloxidase.
15. A composition adapted for dyeing of keratinous fibres, comprising 1) at least one oxidation enzyme, 2) at least one substrate according to any of claims 1 or 2, and optionally 3) at least one modifier.
16. The composition according to claim 15, wherein the oxidation enzyme is an oxidoreductase selected from laccases and related enzymes, oxidases or peroxidases.
17. The composition of claim 16, wherein the oxidation enzyme is a laccase, in particular a laccase derived from a strain of Polyporus sp., in particular a strain of P. pinsitus or P. versicolor, a strain of Myceliophthora sp., in particular M. thermophila, a strain of Rhizoctonia sp., in particular Rh. praticola or Rh. solani, a strain of a Rhus sp., in particular Rhus vernicifera, or a strain of Scytalidium, in particular S. thermophilium, a strain of Pyricularia sp., in particular P. oryzae.
18. A method for dyeing keratinous fibres, comprising contacting the fibers with a composition comprising 1) at least one oxidation enzyme, 2) at least one substrate according to claims 1 or 2, and optionally 3) at least one modifier, for a period of time and under conditions sufficient to permit oxidation of the substrate to a colored compound.
19. The method of claim 18, wherein the dyeing is carried out at a pH in the range from 3.0 to 9.0, preferably 4.0 to 8.5, especially 6.0 to 8.0.
20. The method of claims 18 or 19, wherein the composition is as defined in any of claims 15 to 17.
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Families Citing this family (543)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP2302043A3 (en) 1998-11-27 2011-07-20 Novozymes A/S Lipolytic enzyme variants
US6572843B1 (en) 1998-12-01 2003-06-03 Novozymes, A/S Method for treating hair
EP1137391B1 (en) * 1998-12-01 2004-11-03 Novozymes A/S Method for treating hair
ATE504651T1 (en) 1998-12-18 2011-04-15 Novozymes As SUBTILASE ENZYMES OF THE I-S1 AND I-S2 SUBGROUPS WITH AN ADDITIONAL AMINO ACID RESIDUE IN AN ACTIVE LOOP REGION
DK2011864T3 (en) 1999-03-31 2015-04-07 Novozymes As Polypeptides with alkaline alpha-amylase activity and nucleic acids encoding them
EP1169434B1 (en) 1999-03-31 2009-02-11 Novozymes A/S Polypeptides having alkaline alpha-amylase activity and nucleic acids encoding same
WO2000071685A1 (en) 1999-05-20 2000-11-30 Novozymes A/S Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additional amino acid residue between positions 132 and 133
AU4393000A (en) 1999-05-20 2000-12-12 Novozymes A/S Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additionalamino acid residue between positions 128 and 129
EP1183341B2 (en) 1999-05-20 2012-05-02 Novozymes A/S Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additional amino acid residue between positions 127 and 128
ATE408678T1 (en) 1999-05-20 2008-10-15 Novozymes As SUBTILASE ENZYMES OF THE I-S1 AND I-S2 SUBGROUPS WITH AT LEAST ONE ADDITIONAL AMINO ACID BETWEEN POSITIONS 129 AND 130
WO2000071691A1 (en) 1999-05-20 2000-11-30 Novozymes A/S Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additional amino acid residue between positions 125 and 126
WO2000071688A1 (en) 1999-05-20 2000-11-30 Novozymes A/S Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additional amino acid residue between positions 126 and 127
WO2001016285A2 (en) 1999-08-31 2001-03-08 Novozymes A/S Novel proteases and variants thereof
US7106925B2 (en) 2000-01-06 2006-09-12 Polatis Limited Optical fibre switching assembly
AU7961401A (en) 2000-08-21 2002-03-04 Novozymes As Subtilase enzymes
AU2002210379A1 (en) 2000-10-13 2002-04-22 Novozymes A/S Subtilase variants
US20040091994A1 (en) 2000-10-13 2004-05-13 Carsten Andersen Alpha-amylase variant with altered properties
EP2264160A3 (en) 2001-05-15 2011-08-31 Novozymes A/S Alpha-amylase variant with altered properties
EP1421224B1 (en) 2001-06-26 2012-10-17 Novozymes A/S Polypeptides having cellobiohydrolase i activity and polynucleotides encoding same
DK200101090A (en) 2001-07-12 2001-08-16 Novozymes As Subtilase variants
WO2003080827A2 (en) 2002-03-27 2003-10-02 Novozymes A/S Granules with filamentous coatings
AU2003266941A1 (en) 2002-10-01 2004-04-23 Novozymes A/S Family gh 61 polypeptides
TWI319007B (en) 2002-11-06 2010-01-01 Novozymes As Subtilase variants
CN1729287A (en) 2002-12-20 2006-02-01 诺维信公司 Polypeptide having cellobiohydrolase II activity and polynucleotide encoding it
JP2006517990A (en) 2003-01-27 2006-08-03 ノボザイムス アクティーゼルスカブ Stabilization of granules
EP1622921B1 (en) 2003-05-02 2010-06-16 Novozymes Inc. Variants of beta-glucosidases
AU2004252572B2 (en) 2003-06-25 2011-09-08 Novozymes A/S Polypeptides having alpha-amylase activity and polypeptides encoding same
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JP2007509603A (en) 2003-10-10 2007-04-19 ノボザイムス アクティーゼルスカブ Protease variant
EP1678296B1 (en) 2003-10-23 2011-07-13 Novozymes A/S Protease with improved stability in detergents
ES2437198T3 (en) 2003-10-28 2014-01-09 Novozymes Inc. Polypeptides with beta-glucosidase activity and isolated polynucleotides encoding the polypeptides
WO2005066339A2 (en) 2004-01-06 2005-07-21 Novozymes A/S Polypeptides of alicyclobacillus sp.
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US7148404B2 (en) 2004-05-04 2006-12-12 Novozymes A/S Antimicrobial polypeptides
ES2380105T3 (en) 2004-06-21 2012-05-08 Novozymes A/S Nocardiopsis proteases
US20080193999A1 (en) 2004-07-05 2008-08-14 Novozymes A/S Alpha-Amylase Variants With Altered Properties
DE602005026541D1 (en) 2004-09-21 2011-04-07 Novozymes As SUBTILASES
WO2006032277A1 (en) 2004-09-21 2006-03-30 Novozymes A/S Subtilases
EP2261329A3 (en) 2004-09-21 2011-01-19 Novozymes A/S Subtilases
EP2298872A3 (en) 2004-09-30 2011-08-10 Novozymes A/S Polypeptides having lipase activity and polynucleotides encoding same
DE602006010051D1 (en) 2005-04-27 2009-12-10 Novozymes Inc POLYPEPTIDES WITH ENDOGLUCANASE ACTIVITY AND POLYNUCLEOTIDE CODING THEREFOR
EP1904628B1 (en) 2005-07-08 2011-10-19 Novozymes A/S Subtilase variants
EP1920052A2 (en) 2005-08-16 2008-05-14 Novozymes A/S Polypeptides of strain bacillus sp. p203
WO2007019858A2 (en) 2005-08-16 2007-02-22 Novozymes A/S Subtilases
CN101278047B (en) 2005-09-30 2012-12-12 诺维信公司 Immobilization of enzymes
NZ589570A (en) 2005-09-30 2012-06-29 Novozymes Inc Methods for enhancing the degradation or conversion of cellulosic material
WO2007098756A1 (en) 2006-03-02 2007-09-07 Novozymes A/S High capacity encapsulation process
WO2007107573A1 (en) 2006-03-22 2007-09-27 Novozymes A/S Use of polypeptides having antimicrobial activity
EP2383330A1 (en) 2006-03-31 2011-11-02 Novozymes A/S A stabilized liquid enzyme composition
BRPI0714870A2 (en) 2006-07-21 2013-05-28 Novozymes Inc Method for producing a secreted polypeptide having biological activity, isolated fusion protein, isolated polynucleotide, fusion protein construct, expression vector, authentic host cell, methods for degrading or converting a cellulosic material and for producing a substance
CN103122327B (en) 2006-08-11 2015-11-18 诺维信生物股份有限公司 Bacterial cultures and the composition comprising bacterial cultures
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WO2008088493A2 (en) 2006-12-21 2008-07-24 Danisco Us, Inc., Genencor Division Compositions and uses for an alpha-amylase polypeptide of bacillus species 195
EP2126089A2 (en) 2007-03-09 2009-12-02 Danisco US, INC., Genencor Division Alkaliphilic bacillus species a-amylase variants, compositions comprising a-amylase variants, and methods of use
CN101679087B (en) 2007-03-23 2012-08-15 诺维信生物股份有限公司 Preventing and reducing biofilm formation and planktonic proliferation
DE102007016139A1 (en) 2007-03-30 2008-10-02 Jenabios Gmbh Method for regioselective oxygenation of N-heterocycles
DK2215202T4 (en) 2007-11-05 2025-01-02 Danisco Us Inc VARIANTS OF BACILLUS sp. TS-23 ALPHA-AMYLASE WITH ALTERED PROPERTIES
JP2011505121A (en) 2007-11-05 2011-02-24 ダニスコ・ユーエス・インク Alpha-amylase with modified properties
DK2245130T3 (en) 2008-02-04 2021-01-18 Danisco Us Inc TS23 -ALPHA AMYLASE VARIANTS WITH CHANGED PROPERTIES
CN101960007A (en) * 2008-02-29 2011-01-26 宝洁公司 Detergent composition comprising lipase
CN102112602A (en) * 2008-02-29 2011-06-29 宝洁公司 Detergent composition comprising lipase
MX2010011721A (en) 2008-04-30 2010-11-30 Danisco Inc New chimeric alpha-amylase variants.
BRPI0913402B1 (en) 2008-06-06 2019-07-02 Danisco Us Inc. ALPHA AMYLASES (AMYS) VARIANTS OF GEOBACILLUS STEAROTHERMOPHILUS WITH IMPROVED PROPERTIES
EP2297313B1 (en) 2008-06-06 2015-03-11 Danisco US Inc. Variant alpha-amylases from bacillus subtilis and methods of use, thereof
JP5599113B2 (en) 2008-06-06 2014-10-01 ダニスコ・ユーエス・インク Saccharification enzyme composition and saccharification method thereof
CA2726630A1 (en) 2008-06-06 2009-12-10 Danisco Us Inc. Production of glucose from starch using alpha-amylases from bacillus subtilis
GB0810881D0 (en) 2008-06-16 2008-07-23 Unilever Plc Improvements relating to fabric cleaning
EP2149786A1 (en) 2008-08-01 2010-02-03 Unilever PLC Improvements relating to detergent analysis
WO2010028941A1 (en) 2008-09-12 2010-03-18 Unilever Plc Dispenser and pretreater for viscous liquids
BRPI0920891B1 (en) 2008-09-25 2023-01-10 Danisco Us Inc ALPHA-AMYLASE MIXTURE AND METHOD FOR PRODUCING A FERMENTABLE SUGAR
EP2857515B1 (en) 2008-11-20 2018-02-21 Novozymes Inc. Polypeptides having amylolytic enhancing activity and polynucleotides encoding same
WO2010065830A1 (en) 2008-12-04 2010-06-10 Novozymes, Inc. Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
WO2010068650A1 (en) 2008-12-12 2010-06-17 Novozymes, Inc. Polypeptides having lipase activity and polynucleotides encoding same
EP2202290A1 (en) 2008-12-23 2010-06-30 Unilever PLC A flowable laundry composition and packaging therefor
EP2406373B1 (en) 2009-03-10 2014-05-28 Danisco US Inc. Bacillus megaterium strain dsm90-related alpha-amylases, and methods of use, thereof
CN102378813B (en) 2009-04-01 2014-05-14 丹尼斯科美国公司 Compositions and methods comprising alpha-amylase variants with altered properties
US8877479B2 (en) 2009-04-08 2014-11-04 Danisco Us Inc. Halomonas strain WDG195-related alpha-amylases, and methods of use, thereof
EP2427540B1 (en) 2009-05-05 2015-11-25 Unilever PLC Shading composition
EP2451919A1 (en) 2009-07-09 2012-05-16 The Procter & Gamble Company Method of laundering fabric using a liquid laundry detergent composition
EP2451923A1 (en) 2009-07-09 2012-05-16 The Procter & Gamble Company Method of laundering fabric using a liquid laundry detergent composition
WO2011005905A1 (en) 2009-07-09 2011-01-13 The Procter & Gamble Company A mildly alkaline, low-built, solid fabric treatment detergent composition comprising phthalimido peroxy caproic acid
EP2451922A1 (en) 2009-07-09 2012-05-16 The Procter & Gamble Company Method of laundering fabric using a compacted liquid laundry detergent composition
EP2478096B1 (en) 2009-09-17 2017-05-24 Novozymes, Inc. Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
EP2480650B1 (en) 2009-09-25 2017-03-22 Novozymes A/S Subtilase variants
AU2010299800B2 (en) 2009-09-25 2014-08-07 Novozymes A/S Use of protease variants
CA2775358A1 (en) 2009-09-29 2011-04-07 Novozymes A/S Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
EP2977382A3 (en) 2009-09-30 2016-05-11 Novozymes Inc. Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
CA2775244A1 (en) 2009-09-30 2011-04-07 Novozymes A/S Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
MX2012004091A (en) 2009-10-08 2012-04-20 Unilever Nv Shading composition.
BR112012007757B1 (en) 2009-10-13 2019-08-27 Unilever Nv fabric wash treatment composition and domestic method of fabric treatment
AU2010309968B2 (en) 2009-10-23 2014-01-16 Unilever Global Ip Limited Dye polymers
CN102803481A (en) 2009-10-23 2012-11-28 丹尼斯科美国公司 Methods for reducing blue saccharide
EP2501792A2 (en) 2009-12-29 2012-09-26 Novozymes A/S Gh61 polypeptides having detergency enhancing effect
CN102753672B (en) 2010-01-07 2014-11-12 荷兰联合利华有限公司 Natural shading agents
CN102844324B (en) 2010-01-22 2015-10-07 杜邦营养生物科学有限公司 The method of the amino slycolipid compounds replaced of preparation
ES2477518T3 (en) 2010-02-09 2014-07-17 Unilever Nv Coloring polymers
MX342388B (en) 2010-02-10 2016-09-28 Novozymes As Variants and compositions comprising variants with high stability in presence of a chelating agent.
EP2357220A1 (en) 2010-02-10 2011-08-17 The Procter & Gamble Company Cleaning composition comprising amylase variants with high stability in the presence of a chelating agent
EP2534237B1 (en) 2010-02-12 2014-11-12 Unilever PLC Laundry treatment composition comprising bis-azo shading dyes
WO2011100667A1 (en) 2010-02-14 2011-08-18 Ls9, Inc. Surfactant and cleaning compositions comprising microbially produced branched fatty alcohols
WO2011102933A1 (en) 2010-02-18 2011-08-25 Danisco Us Inc. Amylase from nesterenkonia and methods of use, thereof
EP2539447B1 (en) 2010-02-25 2017-07-26 Novozymes A/S Variants of a lysozyme and polynucleotides encoding same
EP2377914B1 (en) 2010-04-19 2016-11-09 The Procter & Gamble Company Mildly alkaline, low-built, solid fabric treatment detergent composition comprising perhydrolase
EP2365054A1 (en) 2010-03-01 2011-09-14 The Procter & Gamble Company Solid laundry detergent composition comprising secondary alcohol-based detersive surfactant
EP2363456A1 (en) 2010-03-01 2011-09-07 The Procter & Gamble Company Solid laundry detergent composition comprising brightener in micronized particulate form
EP2380957A1 (en) 2010-04-19 2011-10-26 The Procter & Gamble Company Solid laundry detergent composition having a dynamic in-wash ph profile
EP2365059A1 (en) 2010-03-01 2011-09-14 The Procter & Gamble Company Solid laundry detergent composition comprising C.I. fluorescent brightener 260 in alpha-crystalline form
EP2365058A1 (en) 2010-03-01 2011-09-14 The Procter & Gamble Company Solid laundry detergent composition having an excellent anti-encrustation profile
WO2011107397A1 (en) 2010-03-02 2011-09-09 Unilever Nv Laundry detergent compositions comprising amino silicone antifoam agent
US20110257069A1 (en) 2010-04-19 2011-10-20 Stephen Joseph Hodson Detergent composition
US8889612B2 (en) 2010-04-19 2014-11-18 The Procter & Gamble Company Method of laundering fabric using a compacted liquid laundry detergent composition
US20110257062A1 (en) 2010-04-19 2011-10-20 Robert Richard Dykstra Liquid laundry detergent composition comprising a source of peracid and having a ph profile that is controlled with respect to the pka of the source of peracid
US20110257060A1 (en) 2010-04-19 2011-10-20 Robert Richard Dykstra Laundry detergent composition comprising bleach particles that are suspended within a continuous liquid phase
BR112012027594A2 (en) 2010-04-29 2016-08-09 Unilever Nv laundry treatment composition and method of treating a textile for clothing
EP2395070A1 (en) 2010-06-10 2011-12-14 The Procter & Gamble Company Liquid laundry detergent composition comprising lipase of bacterial origin
EP2395071A1 (en) 2010-06-10 2011-12-14 The Procter & Gamble Company Solid detergent composition comprising lipase of bacterial origin
EP2585573A1 (en) 2010-06-23 2013-05-01 The Procter and Gamble Company Product for pre-treatment and laundering of stained fabric
US20130118532A1 (en) 2010-08-30 2013-05-16 Novozymes A/S Two-Soak Wash
JP2013541356A (en) 2010-08-30 2013-11-14 ノボザイムス アクティーゼルスカブ Concentrated immersion cleaning
EP2616483A1 (en) 2010-09-16 2013-07-24 Novozymes A/S Lysozymes
GB201015672D0 (en) 2010-09-20 2010-10-27 Unilever Plc Improvements relating to fabric treatment compositions comprising targeted benefit agents
EP2622070B1 (en) 2010-09-30 2016-08-03 Novozymes, Inc. Variants of polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
US10246691B2 (en) 2010-09-30 2019-04-02 Novozymes, Inc. Variants of polypeptides having cellulolytic enhancing activity and polynucleotides encoding same
EP2441820A1 (en) 2010-10-14 2012-04-18 Unilever Plc, A Company Registered In England And Wales under company no. 41424 of Unilever House Laundry detergent particles
IN2013MN00626A (en) 2010-10-14 2015-06-12 Unilever Plc
WO2012048910A1 (en) 2010-10-14 2012-04-19 Unilever Plc Packaged particulate detergent composition
PL2627755T3 (en) 2010-10-14 2016-03-31 Unilever Nv Packaged particulate detergent composition
BR112013009135B1 (en) 2010-10-14 2021-01-05 Unilever N.V. packed product
EP2441822A1 (en) 2010-10-14 2012-04-18 Unilever Plc, A Company Registered In England And Wales under company no. 41424 of Unilever House Laundry detergent particles
BR112013009125B1 (en) 2010-10-14 2021-01-05 Unilever N.V. particulate detergent composition packaged in a packaging
EP2441825A1 (en) 2010-10-14 2012-04-18 Unilever Plc, A Company Registered In England And Wales under company no. 41424 of Unilever House Process for preparing laundry detergent particles
CN103282477B (en) 2010-10-14 2015-04-01 荷兰联合利华有限公司 Top-loading laundry vessel method
EP2627577B1 (en) 2010-10-14 2016-06-15 Unilever PLC Package comprising a laundry composition and method for washing using said package.
PL2627754T3 (en) 2010-10-14 2017-06-30 Unilever N.V. Laundry detergent particles
AU2011315793B2 (en) 2010-10-14 2014-03-06 Unilever Plc Laundry detergent particles
AU2011315790B2 (en) 2010-10-14 2014-03-06 Unilever Plc Laundry detergent particles
PL2627748T3 (en) 2010-10-14 2015-04-30 Unilever Nv Particulate detergent compositions containing a fluorescer
CN103154230B (en) 2010-10-14 2015-01-21 荷兰联合利华有限公司 Laundry detergent particles
EP2627749B1 (en) 2010-10-14 2015-03-04 Unilever PLC Laundry detergent particles
WO2012049032A1 (en) 2010-10-14 2012-04-19 Unilever Plc Refill and refillable packages of concentrated particulate detergent compositions
PL2627753T3 (en) 2010-10-14 2017-05-31 Unilever N.V. Laundry detergent particle
WO2012049034A1 (en) 2010-10-14 2012-04-19 Unilever Plc Packaging and dispensing of detergent compositions
BR112013009456B1 (en) 2010-10-22 2021-11-30 Unilever Ip Holdings B.V. STRUCTURED AQUEOUS LIQUID DETERGENT COMPOSITION AND PROCESS TO MANUFACTURE A STRUCTURED AQUEOUS LIQUID DETERGENT
CN103168095A (en) 2010-11-01 2013-06-19 荷兰联合利华有限公司 A detergent composition having shading dyes and lipase
DK2640833T3 (en) 2010-11-18 2016-11-28 Novozymes Inc Chimeric polypeptides having cellulolytic enhancing ACTIVITY AND POLYNUCLEOTIDES ENCODING THEM
WO2012098046A1 (en) 2011-01-17 2012-07-26 Unilever Plc Dye polymer for laundry treatment
WO2012104159A1 (en) 2011-01-31 2012-08-09 Unilever Plc Alkaline liquid detergent compositions
EP2675891B1 (en) 2011-02-15 2018-06-20 Novozymes Biologicals, Inc. Mitigation of odor in cleaning machines and cleaning processes
JP2014506945A (en) 2011-02-16 2014-03-20 ノボザイムス アクティーゼルスカブ Detergent composition containing metalloprotease
CN103502418A (en) 2011-02-16 2014-01-08 诺维信公司 Detergent compositions comprising metalloproteases
US20140024103A1 (en) 2011-02-16 2014-01-23 Astrid Benie Detergent Compositions Comprising Metalloproteases
MX2013007997A (en) 2011-02-23 2013-08-21 Novozymes Inc Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same.
WO2012119859A1 (en) 2011-03-10 2012-09-13 Unilever Plc Dye polymer
WO2012130492A1 (en) 2011-03-25 2012-10-04 Unilever Plc Dye polymer
US9410136B2 (en) 2011-03-31 2016-08-09 Novozymes, Inc. Methods for enhancing the degradation or conversion of cellulosic material
EP2476743B1 (en) 2011-04-04 2013-04-24 Unilever Plc, A Company Registered In England And Wales under company no. 41424 of Unilever House Method of laundering fabric
AR085845A1 (en) 2011-04-08 2013-10-30 Danisco Us Inc COMPOSITIONS
DK2702162T3 (en) 2011-04-29 2020-05-18 Novozymes Inc PROCEDURES FOR IMPROVING THE DEGRADATION OR CONVERSION OF CELLULOSE SUBSTANCES
CN103517975B (en) 2011-05-13 2015-11-25 荷兰联合利华有限公司 Water-based concentrates laundry detergent composition
EP2522714A1 (en) 2011-05-13 2012-11-14 Unilever Plc, A Company Registered In England And Wales under company no. 41424 of Unilever House Aqueous concentrated laundry detergent compositions
EP2522715A1 (en) 2011-05-13 2012-11-14 Unilever Plc, A Company Registered In England And Wales under company no. 41424 of Unilever House Aqueous concentrated laundry detergent compositions
CN103562370B (en) 2011-05-26 2016-08-17 荷兰联合利华有限公司 Liquid laundry composition
EP3354792A1 (en) 2011-06-01 2018-08-01 Unilever PLC, a company registered in England and Wales under company no. 41424 of Liquid detergent composition containing dye polymer
US20120324655A1 (en) 2011-06-23 2012-12-27 Nalini Chawla Product for pre-treatment and laundering of stained fabric
CN103620029B (en) 2011-06-24 2017-06-09 诺维信公司 Polypeptide and their polynucleotides of coding with proteinase activity
ES2692544T3 (en) 2011-06-30 2018-12-04 Novozymes A/S Variants of alpha-amylase
EP2540824A1 (en) 2011-06-30 2013-01-02 The Procter & Gamble Company Cleaning compositions comprising amylase variants reference to a sequence listing
BR122020009747B1 (en) 2011-06-30 2021-07-20 Novozymes A/S POLYPEPTIDE AND ALPHA-AMYLASE VARIANTS, DETERGENT COMPOSITION, AND, USE OF AN ALPHA-AMYLASE VARIANT
ES2550051T3 (en) 2011-07-21 2015-11-04 Unilever N.V. Liquid composition for laundry
EP2551335A1 (en) 2011-07-25 2013-01-30 The Procter & Gamble Company Enzyme stabilized liquid detergent composition
CN103748219A (en) 2011-08-15 2014-04-23 诺维信公司 Polypeptides having cellulase activity and polynucleotides encoding same
WO2013026796A1 (en) 2011-08-19 2013-02-28 Novozymes A/S Polypeptides having protease activity
CN104204200B (en) 2011-09-22 2017-06-09 诺维信公司 Polypeptide and their polynucleotides of coding with proteinase activity
EP4345161A3 (en) 2011-10-28 2024-06-12 Danisco Us Inc Variant maltohexaose-forming alpha-amylase variants
US10351834B2 (en) 2011-11-21 2019-07-16 Novozymes, Inc. GH61 polypeptide variants and polynucleotides encoding same
ES2631605T3 (en) 2011-11-25 2017-09-01 Novozymes A/S Polypeptides with lysozyme activity and polynucleotides encoding them
US20140342433A1 (en) 2011-11-25 2014-11-20 Novozymes A/S Subtilase Variants and Polynucleotides Encoding Same
WO2013087027A1 (en) 2011-12-16 2013-06-20 Novozymes, Inc. Polypeptides having laccase activity and polynucleotides encoding same
ES2587861T3 (en) 2011-12-20 2016-10-27 Unilever N.V. Isotropic liquid detergents comprising soil release polymer
EP2607468A1 (en) 2011-12-20 2013-06-26 Henkel AG & Co. KGaA Detergent compositions comprising subtilase variants
MX2014007446A (en) 2011-12-20 2014-08-01 Novozymes As Subtilase variants and polynucleotides encoding same.
EP2794866A1 (en) 2011-12-22 2014-10-29 Danisco US Inc. Compositions and methods comprising a lipolytic enzyme variant
BR112014015421A2 (en) 2011-12-22 2019-09-24 Danisco Us Inc Variant alpha-amylases and methods of use
MX358963B (en) 2011-12-28 2018-09-11 Novozymes As Polypeptides having protease activity.
EP3382003B1 (en) 2011-12-29 2021-07-14 Novozymes A/S Detergent compositions with lipase variants
AU2013213601B8 (en) 2012-01-26 2018-01-18 Novozymes A/S Use of polypeptides having protease activity in animal feed and detergents
EP2628785B1 (en) 2012-02-17 2016-05-18 Henkel AG & Co. KGaA Detergent compositions comprising subtilase variants
WO2013120948A1 (en) 2012-02-17 2013-08-22 Novozymes A/S Subtilisin variants and polynucleotides encoding same
CN104704102A (en) 2012-03-07 2015-06-10 诺维信公司 Detergent composition and substitution of optical brighteners in detergent compositions
EP2639291A1 (en) 2012-03-13 2013-09-18 Unilever PLC Packaged particulate detergent composition
WO2013139702A1 (en) 2012-03-21 2013-09-26 Unilever Plc Laundry detergent particles
BR112014020539B1 (en) 2012-04-03 2021-10-05 Unilever Ip Holdings B.V. COATED DETERGENT PARTICLE AND PACKAGED DETERGENT FORMULATION
CN104185676B (en) 2012-04-03 2017-09-22 荷兰联合利华有限公司 Laundry detergent particle
EP2834336B1 (en) 2012-04-03 2019-09-11 Unilever PLC, a company registered in England and Wales under company no. 41424 Laundry detergent particles
CA2866936C (en) 2012-04-03 2020-01-07 Stephen Norman Batchelor Laundry detergent particle
CN104379716A (en) 2012-04-23 2015-02-25 荷兰联合利华有限公司 Structured aqueous liquid detergent
EP2841567B1 (en) 2012-04-27 2017-07-26 Novozymes, Inc. Gh61 polypeptide variants and polynucleotides encoding same
CN104271723B (en) 2012-05-07 2021-04-06 诺维信公司 Polypeptides having xanthan degrading activity and nucleotides encoding same
US8945889B2 (en) 2012-05-11 2015-02-03 Danisco Us Inc. Method of using alpha-amylase from Aspergillus clavatus for saccharification
ES2909509T3 (en) 2012-06-08 2022-05-06 Danisco Us Inc Alpha-amylases variant with higher activity on starch polymers
WO2013189972A2 (en) 2012-06-20 2013-12-27 Novozymes A/S Use of polypeptides having protease activity in animal feed and detergents
PT2875179T (en) 2012-07-18 2018-04-23 Novozymes As Method of treating polyester textile
CA2878988A1 (en) 2012-08-16 2014-02-20 Danisco Us Inc. Method of using alpha-amylase from aspergillus clavatus and pullulanase for saccharification
PT3553172T (en) 2012-08-16 2023-01-27 Novozymes As Method for treating textile with endoglucanase
MX2015002211A (en) 2012-08-22 2015-05-08 Novozymes As Metalloprotease from exiguobacterium.
US9315791B2 (en) 2012-08-22 2016-04-19 Novozymes A/S Metalloproteases from alicyclobacillus
WO2014029820A1 (en) 2012-08-22 2014-02-27 Novozymes A/S Detergent compositions comprising metalloproteases
ES2614037T3 (en) 2012-09-25 2017-05-29 Unilever N.V. Laundry detergent particles
AR093330A1 (en) 2012-11-01 2015-06-03 Novozymes As METHOD FOR DNA REMOVAL
US20180112203A1 (en) 2012-11-20 2018-04-26 Danisco Us Inc. Amylase with maltogenic properties
CN110628528B (en) 2012-12-07 2021-09-14 诺维信公司 Preventing adhesion of bacteria
EP3321353A1 (en) 2012-12-11 2018-05-16 Danisco US Inc. Yeast host cells epxressing a glucoamylase from aspergillus fumigatus and methods of use thereof
EP2931911A1 (en) 2012-12-14 2015-10-21 Danisco US Inc. Method of using alpha-amylase from aspergillus fumigatus and isoamylase for saccharification
WO2014099415A1 (en) 2012-12-20 2014-06-26 Danisco Us Inc. Method of using alpha-amylase from aspergillus terreus and pullulanase for saccharification
WO2014099525A1 (en) 2012-12-21 2014-06-26 Danisco Us Inc. Paenibacillus curdlanolyticus amylase, and methods of use, thereof
BR112015014396B1 (en) 2012-12-21 2021-02-02 Novozymes A/S COMPOSITION, NUCLEIC ACID CONSTRUCTION OR EXPRESSION VECTOR, RECOMBINANT MICROORGANISM, METHODS OF IMPROVING THE NUTRITIONAL VALUE OF ANIMAL FEED, ANIMAL FEED ADDITIVE, AND USE OF ONE OR MORE PROTEASES
CN104884614A (en) 2012-12-21 2015-09-02 丹尼斯科美国公司 Alpha-amylase variants
WO2014106593A1 (en) 2013-01-03 2014-07-10 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same
CA2903027A1 (en) 2013-03-11 2014-10-09 Danisco Us Inc. Alpha-amylase combinatorial variants
EP2970830B1 (en) 2013-03-14 2017-12-13 Novozymes A/S Enzyme and inhibitor contained in water-soluble films
EP3569611A1 (en) 2013-04-23 2019-11-20 Novozymes A/S Liquid automatic dish washing detergent compositions with stabilised subtilisin
EP2992076B1 (en) 2013-05-03 2018-10-24 Novozymes A/S Microencapsulation of detergent enzymes
US20160083703A1 (en) 2013-05-17 2016-03-24 Novozymes A/S Polypeptides having alpha amylase activity
CN105264058B (en) 2013-06-06 2022-03-29 诺维信公司 Alpha-amylase variants and polynucleotides encoding same
PE20160799A1 (en) 2013-06-12 2016-09-03 Earth Alive Clean Tech Inc DUST SUPPRESSOR
WO2014200656A1 (en) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase from streptomyces umbrinus
WO2014200657A1 (en) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase from streptomyces xiamenensis
WO2014200658A1 (en) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase from promicromonospora vindobonensis
EP3011020A1 (en) 2013-06-17 2016-04-27 Danisco US Inc. Alpha-amylase from bacillaceae family member
US20160145596A1 (en) 2013-06-27 2016-05-26 Novozymes A/S Subtilase Variants and Polynucleotides Encoding Same
US10378001B2 (en) 2013-06-27 2019-08-13 Novozymes A/S Subtilase variants and compositions comprising same
RU2015156280A (en) 2013-07-04 2017-08-09 Новозимс А/С POLYEPEPTIDES HAVING AN EFFECT AGAINST RESETITATION AND POLYNUCLEOTIDES CODING THEM
US20160160197A1 (en) 2013-07-19 2016-06-09 Danisco Us Inc. Compositions and Methods Comprising a Lipolytic Enzyme Variant
EP3027747B1 (en) 2013-07-29 2018-02-07 Novozymes A/S Protease variants and polynucleotides encoding same
RU2670946C9 (en) 2013-07-29 2018-11-26 Новозимс А/С Protease variants and polynucleotides encoding them
EP2832853A1 (en) 2013-07-29 2015-02-04 Henkel AG&Co. KGAA Detergent composition comprising protease variants
EP3052622B1 (en) 2013-10-03 2018-09-19 Danisco US Inc. Alpha-amylases from a subset of exiguobacterium, and methods of use, thereof
US20160160199A1 (en) 2013-10-03 2016-06-09 Danisco Us Inc. Alpha-amylases from exiguobacterium, and methods of use, thereof
WO2015049370A1 (en) 2013-10-03 2015-04-09 Novozymes A/S Detergent composition and use of detergent composition
EP3071691B1 (en) 2013-11-20 2019-10-23 Danisco US Inc. Variant alpha-amylases having reduced susceptibility to protease cleavage, and methods of use, thereof
MX373205B (en) 2013-12-16 2020-05-04 Nutrition & Biosciences Usa 4 Inc USE OF POLY-ALPHA-1,3-GLUCAN ETHERS AS VISCOSITY MODIFIERS.
EP3083705B1 (en) 2013-12-18 2020-09-30 DuPont Industrial Biosciences USA, LLC Cationic poly alpha-1,3-glucan ethers
WO2015094809A1 (en) 2013-12-19 2015-06-25 Danisco Us Inc. Chimeric fungal alpha-amylases comprising carbohydrate binding module and the use thereof
EP3083954B1 (en) 2013-12-20 2018-09-26 Novozymes A/S Polypeptides having protease activity and polynucleotides encoding same
US20150232785A1 (en) 2014-02-14 2015-08-20 E I Du Pont De Nemours And Company Polysaccharides for viscosity modification
CN106062271A (en) 2014-03-05 2016-10-26 诺维信公司 Compositions and methods for improving properties of cellulosic textile materials with xyloglucan endotransglycosylase
WO2015134729A1 (en) 2014-03-05 2015-09-11 Novozymes A/S Compositions and methods for improving properties of non-cellulosic textile materials with xyloglucan endotransglycosylase
WO2015138283A1 (en) 2014-03-11 2015-09-17 E. I. Du Pont De Nemours And Company Oxidized poly alpha-1,3-glucan as detergent builder
WO2015150457A1 (en) 2014-04-01 2015-10-08 Novozymes A/S Polypeptides having alpha amylase activity
CN112899086A (en) 2014-04-11 2021-06-04 诺维信公司 Detergent composition
EP3878957A1 (en) 2014-05-27 2021-09-15 Novozymes A/S Methods for producing lipases
WO2015181119A2 (en) 2014-05-27 2015-12-03 Novozymes A/S Lipase variants and polynucleotides encoding same
WO2015189371A1 (en) 2014-06-12 2015-12-17 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same
US9714403B2 (en) 2014-06-19 2017-07-25 E I Du Pont De Nemours And Company Compositions containing one or more poly alpha-1,3-glucan ether compounds
US9771548B2 (en) 2014-06-19 2017-09-26 E I Du Pont De Nemours And Company Compositions containing one or more poly alpha-1,3-glucan ether compounds
CN106471110A (en) 2014-07-03 2017-03-01 诺维信公司 Improved non-protein enzyme enzyme stabilization
EP3164486B1 (en) 2014-07-04 2020-05-13 Novozymes A/S Subtilase variants and polynucleotides encoding same
EP3878960A1 (en) 2014-07-04 2021-09-15 Novozymes A/S Subtilase variants and polynucleotides encoding same
EP3194543B1 (en) 2014-09-18 2018-04-04 Unilever Plc. Whitening composition
WO2016079110A2 (en) 2014-11-19 2016-05-26 Novozymes A/S Use of enzyme for cleaning
WO2016079305A1 (en) 2014-11-20 2016-05-26 Novozymes A/S Alicyclobacillus variants and polynucleotides encoding same
WO2016087617A1 (en) 2014-12-04 2016-06-09 Novozymes A/S Subtilase variants and polynucleotides encoding same
EP3227425B1 (en) 2014-12-04 2025-02-12 Novozymes A/S Liquid cleaning compositions comprising protease variants
ES2763235T3 (en) 2014-12-15 2020-05-27 Henkel Ag & Co Kgaa Detergent composition comprising subtilase variants
WO2016096996A1 (en) 2014-12-16 2016-06-23 Novozymes A/S Polypeptides having n-acetyl glucosamine oxidase activity
DK3234123T3 (en) 2014-12-19 2020-08-24 Novozymes As PROTEASE VARIANTS AND POLYNUCLEOTIDES ENCODING THEM
WO2016097352A1 (en) 2014-12-19 2016-06-23 Novozymes A/S Protease variants and polynucleotides encoding same
JP6770519B2 (en) 2014-12-23 2020-10-14 イー・アイ・デュポン・ドウ・ヌムール・アンド・カンパニーE.I.Du Pont De Nemours And Company Cellulose produced by enzymes
EP3242927B1 (en) 2015-01-09 2018-10-10 Unilever PLC, a company registered in England and Wales under company no. 41424 Laundry treatment composition comprising a dye
CN107207998B (en) 2015-02-13 2020-04-10 荷兰联合利华有限公司 Liquid laundry compositions
WO2016133734A1 (en) 2015-02-18 2016-08-25 E. I. Du Pont De Nemours And Company Soy polysaccharide ethers
BR112017019942A2 (en) 2015-04-02 2018-06-12 Unilever Nv liquid laundry detergent composition and polymer release for dirt release
EP3280800A1 (en) 2015-04-10 2018-02-14 Novozymes A/S Detergent composition
US20180112156A1 (en) 2015-04-10 2018-04-26 Novozymes A/S Laundry method, use of polypeptide and detergent composition
US10336971B2 (en) 2015-05-19 2019-07-02 Novozymes A/S Odor reduction
CN107922095A (en) 2015-06-17 2018-04-17 诺维信公司 Container
WO2016202839A2 (en) 2015-06-18 2016-12-22 Novozymes A/S Subtilase variants and polynucleotides encoding same
EP3106508B1 (en) 2015-06-18 2019-11-20 Henkel AG & Co. KGaA Detergent composition comprising subtilase variants
WO2016135351A1 (en) 2015-06-30 2016-09-01 Novozymes A/S Laundry detergent composition, method for washing and use of composition
CN114292829A (en) 2015-07-06 2022-04-08 诺维信公司 Lipase variants and polynucleotides encoding them
ES2794837T3 (en) 2015-09-17 2020-11-19 Henkel Ag & Co Kgaa Detergent Compositions Comprising Polypeptides Having Xanthan Degrading Activity
US20180171315A1 (en) 2015-09-17 2018-06-21 Novozymes A/S Polypeptides having xanthan degrading activity and polynucleotides encoding same
BR112018007017B1 (en) 2015-10-07 2023-11-28 Novozymes A/S DETERGENT COMPOSITION, NUCLEIC ACID CONSTRUCT OR EXPRESSION VECTOR, USE OF A POLYPEPTIDE, RECOMBINANT HOST CELL AND METHOD FOR PRODUCING THE POLYPEPTIDE
EP4324919A3 (en) 2015-10-14 2024-05-29 Novozymes A/S Polypeptide variants
CN108291215A (en) 2015-10-14 2018-07-17 诺维信公司 Polypeptide with proteinase activity and encode their polynucleotides
US10675589B2 (en) 2015-10-14 2020-06-09 Novozymes A/S Cleaning of water filtration membranes
WO2016203064A2 (en) 2015-10-28 2016-12-22 Novozymes A/S Detergent composition comprising protease and amylase variants
EP3374400B1 (en) 2015-11-13 2022-04-13 Nutrition & Biosciences USA 4, Inc. Glucan fiber compositions for use in laundry care and fabric care
US10822574B2 (en) 2015-11-13 2020-11-03 Dupont Industrial Biosciences Usa, Llc Glucan fiber compositions for use in laundry care and fabric care
EP3374488B1 (en) 2015-11-13 2020-10-14 DuPont Industrial Biosciences USA, LLC Glucan fiber compositions for use in laundry care and fabric care
WO2017089366A1 (en) 2015-11-24 2017-06-01 Novozymes A/S Polypeptides having protease activity and polynucleotides encoding same
WO2017093318A1 (en) 2015-12-01 2017-06-08 Novozymes A/S Methods for producing lipases
CN108431220B (en) 2015-12-07 2022-06-07 诺维信公司 Polypeptides having beta-glucanase activity, polynucleotides encoding the same, and uses thereof in cleaning and detergent compositions
DK3387124T3 (en) 2015-12-09 2021-08-23 William Cuevas COMBINATORY ALFA AMYLASE VARIANTS
EP3397061A1 (en) 2015-12-28 2018-11-07 Novozymes BioAG A/S Heat priming of bacterial spores
WO2017114891A1 (en) 2015-12-30 2017-07-06 Novozymes A/S Enzyme variants and polynucleotides encoding the same
EP3190167B1 (en) 2016-01-07 2018-06-06 Unilever PLC Bitter pill
WO2017121714A1 (en) 2016-01-15 2017-07-20 Unilever Plc Dye
EP3408386A1 (en) 2016-01-29 2018-12-05 Novozymes A/S Beta-glucanase variants and polynucleotides encoding same
WO2017133879A1 (en) 2016-02-04 2017-08-10 Unilever Plc Detergent liquid
CN108603139B (en) 2016-02-17 2020-12-04 荷兰联合利华有限公司 Whitening composition
BR112018016674B1 (en) 2016-02-17 2022-06-07 Unilever Ip Holdings B.V. Detergent composition for washing clothes and domestic method of treating a fabric
CN108884415A (en) 2016-03-21 2018-11-23 荷兰联合利华有限公司 laundry detergent composition
US20190048291A1 (en) 2016-03-23 2019-02-14 Novozymes A/S Use of Polypeptide Having DNase Activity for Treating Fabrics
WO2017173190A2 (en) 2016-04-01 2017-10-05 Danisco Us Inc. Alpha-amylases, compositions & methods
WO2017173324A2 (en) 2016-04-01 2017-10-05 Danisco Us Inc. Alpha-amylases, compositions & methods
CN109312270B (en) 2016-04-08 2022-01-28 诺维信公司 Detergent composition and use thereof
MX391044B (en) 2016-04-29 2025-03-21 Novozymes As DETERGENT COMPOSITIONS AND THEIR USES.
EP3452497B1 (en) 2016-05-03 2021-02-17 Novozymes A/S Alpha-amylase variants and polynucleotides encoding the same
JP6985295B2 (en) 2016-05-09 2021-12-22 ノボザイムス アクティーゼルスカブ Mutant polypeptides with improved performance and their use
EP3464538A1 (en) 2016-05-31 2019-04-10 Novozymes A/S Stabilized liquid peroxide compositions
CN109715792A (en) 2016-06-03 2019-05-03 诺维信公司 Subtilase variants and the polynucleotides that it is encoded
US11001787B2 (en) 2016-06-23 2021-05-11 Novozymes A/S Use of enzymes, composition and method for removing soil
CN117721095A (en) 2016-06-30 2024-03-19 诺维信公司 Lipase variants and compositions comprising surfactants and lipase variants
WO2018002261A1 (en) 2016-07-01 2018-01-04 Novozymes A/S Detergent compositions
JP2019522988A (en) 2016-07-05 2019-08-22 ノボザイムス アクティーゼルスカブ Pectate lyase mutant and polynucleotide encoding the same
WO2018007573A1 (en) 2016-07-08 2018-01-11 Novozymes A/S Detergent compositions with galactanase
PL3485010T3 (en) 2016-07-13 2025-01-27 The Procter & Gamble Company Bacillus cibi dnase variants and uses thereof
KR102483218B1 (en) 2016-08-24 2023-01-02 헨켈 아게 운트 코. 카게아아 Detergent composition comprising xanthan lyase variant I
CN109863244B (en) 2016-08-24 2023-06-06 诺维信公司 GH9 endoglucanase variants and polynucleotides encoding them
CN109844110B (en) 2016-08-24 2023-06-06 诺维信公司 Xanthan gum lyase variants and polynucleotides encoding same
WO2018037065A1 (en) 2016-08-24 2018-03-01 Henkel Ag & Co. Kgaa Detergent composition comprising gh9 endoglucanase variants i
US20200140786A1 (en) 2016-09-29 2020-05-07 Novozymes A/S Use of enzyme for washing, method for washing and warewashing composition
CN109996859B (en) 2016-09-29 2021-11-30 诺维信公司 Spore-containing particles
BR112019007851B1 (en) 2016-10-18 2022-10-18 Unilever Ip Holdings B.V. DETERGENT COMPOSITION FOR WASHING CLOTHES AND DOMESTIC FABRIC TREATMENT METHOD
WO2018077938A1 (en) 2016-10-25 2018-05-03 Novozymes A/S Detergent compositions
US11753605B2 (en) 2016-11-01 2023-09-12 Novozymes A/S Multi-core granules
MX2019006425A (en) 2016-12-01 2019-08-14 Basf Se Stabilization of enzymes in compositions.
WO2018108865A1 (en) 2016-12-12 2018-06-21 Novozymes A/S Use of polypeptides
CN110023469A (en) 2016-12-15 2019-07-16 荷兰联合利华有限公司 Laundry detergent composition
ES2965826T3 (en) 2017-02-01 2024-04-17 Procter & Gamble Cleansing compositions comprising amylase variants
US11053483B2 (en) 2017-03-31 2021-07-06 Novozymes A/S Polypeptides having DNase activity
CN110651041A (en) 2017-03-31 2020-01-03 诺维信公司 Polypeptides having DNase activity
EP3601551A1 (en) 2017-03-31 2020-02-05 Novozymes A/S Polypeptides having rnase activity
EP3601553A1 (en) 2017-03-31 2020-02-05 Danisco US Inc. Alpha-amylase combinatorial variants
WO2018185152A1 (en) 2017-04-04 2018-10-11 Novozymes A/S Polypeptide compositions and uses thereof
EP3607041A1 (en) 2017-04-04 2020-02-12 Novozymes A/S Glycosyl hydrolases
EP3607039A1 (en) 2017-04-04 2020-02-12 Novozymes A/S Polypeptides
EP3385361B1 (en) 2017-04-05 2019-03-27 Henkel AG & Co. KGaA Detergent compositions comprising bacterial mannanases
EP3385362A1 (en) 2017-04-05 2018-10-10 Henkel AG & Co. KGaA Detergent compositions comprising fungal mannanases
WO2018184816A1 (en) 2017-04-06 2018-10-11 Novozymes A/S Cleaning compositions and uses thereof
ES2763561T3 (en) 2017-04-06 2020-05-29 Novozymes As Cleaning compositions and their uses
CN110662829B (en) 2017-04-06 2022-03-01 诺维信公司 Cleaning compositions and their uses
WO2018185280A1 (en) 2017-04-06 2018-10-11 Novozymes A/S Cleaning compositions and uses thereof
US20200032170A1 (en) 2017-04-06 2020-01-30 Novozymes A/S Cleaning compositions and uses thereof
EP3607060B1 (en) 2017-04-06 2021-08-11 Novozymes A/S Detergent compositions and uses thereof
US11352591B2 (en) 2017-04-06 2022-06-07 Novozymes A/S Cleaning compositions and uses thereof
WO2018206535A1 (en) 2017-05-08 2018-11-15 Novozymes A/S Carbohydrate-binding domain and polynucleotides encoding the same
US12018235B2 (en) 2017-05-08 2024-06-25 Novozymes A/S Mannanase variants and polynucleotides encoding same
EP3401385A1 (en) 2017-05-08 2018-11-14 Henkel AG & Co. KGaA Detergent composition comprising polypeptide comprising carbohydrate-binding domain
WO2018206300A1 (en) 2017-05-08 2018-11-15 Novozymes A/S Mannanase variants and polynucleotides encoding same
WO2018224544A1 (en) 2017-06-08 2018-12-13 Novozymes A/S Compositions comprising polypeptides having cellulase activity and amylase activity, and uses thereof in cleaning and detergent compositions
EP3642319B1 (en) 2017-06-20 2020-12-30 Unilever N.V. Particulate detergent composition comprising perfume
WO2018234003A1 (en) 2017-06-21 2018-12-27 Unilever Plc Packaging and dispensing of detergent compositions
WO2019002356A1 (en) 2017-06-30 2019-01-03 Novozymes A/S Enzyme slurry composition
BR112020000205B1 (en) 2017-07-07 2023-10-31 Unilever Ip Holdings B.V. CLEANING COMPOSITION FOR WASHING FABRICS AND HOUSEHOLD METHOD OF TREATING A FABRIC
CN110869480B (en) 2017-07-07 2021-08-13 联合利华知识产权控股有限公司 Whitening composition
JP2020528286A (en) 2017-08-18 2020-09-24 ザ プロクター アンド ギャンブル カンパニーThe Procter & Gamble Company Cleaning method
EP3668973A2 (en) 2017-08-18 2020-06-24 Danisco US Inc. Alpha-amylase variants
WO2019035037A1 (en) 2017-08-18 2019-02-21 The Procter & Gamble Company Cleaning kit
WO2019038186A1 (en) 2017-08-24 2019-02-28 Unilever Plc Improvements relating to fabric cleaning
EP3673057A1 (en) 2017-08-24 2020-07-01 Novozymes A/S Xanthan lyase variants and polynucleotides encoding same
WO2019038187A1 (en) 2017-08-24 2019-02-28 Unilever Plc Improvements relating to fabric cleaning
WO2019038059A1 (en) 2017-08-24 2019-02-28 Henkel Ag & Co. Kgaa Detergent compositions comprising gh9 endoglucanase variants ii
US20210130744A1 (en) 2017-08-24 2021-05-06 Henkel Ag & Co. Kgaa Detergent composition comprising xanthan lyase variants ii
CA3070749A1 (en) 2017-08-24 2019-02-28 Novozymes A/S Gh9 endoglucanase variants and polynucleotides encoding same
MX2020002953A (en) 2017-09-20 2020-07-22 Novozymes As Use of enzymes for improving water absorption and/or whiteness.
EP3684899A1 (en) 2017-09-22 2020-07-29 Novozymes A/S Novel polypeptides
US11332725B2 (en) 2017-09-27 2022-05-17 Novozymes A/S Lipase variants and microcapsule compositions comprising such lipase variants
US11746310B2 (en) 2017-10-02 2023-09-05 Novozymes A/S Polypeptides having mannanase activity and polynucleotides encoding same
MX2020003411A (en) 2017-10-02 2020-07-20 Novozymes As Polypeptides having mannanase activity and polynucleotides encoding same.
WO2019076800A1 (en) 2017-10-16 2019-04-25 Novozymes A/S Cleaning compositions and uses thereof
WO2019076833A1 (en) 2017-10-16 2019-04-25 Novozymes A/S Low dusting granules
US20200318037A1 (en) 2017-10-16 2020-10-08 Novozymes A/S Low dusting granules
EP3701001A1 (en) 2017-10-24 2020-09-02 Novozymes A/S Compositions comprising polypeptides having mannanase activity
CN117683748A (en) 2017-10-27 2024-03-12 宝洁公司 Detergent compositions comprising polypeptide variants
BR112020008251A2 (en) 2017-10-27 2020-11-17 Novozymes A/S dnase variants
BR112020008711A2 (en) 2017-11-01 2020-11-10 Novozymes A/S polypeptides and compositions comprising such polypeptides
DE102017125560A1 (en) 2017-11-01 2019-05-02 Henkel Ag & Co. Kgaa CLEANSING COMPOSITIONS CONTAINING DISPERSINE III
DE102017125559A1 (en) 2017-11-01 2019-05-02 Henkel Ag & Co. Kgaa CLEANSING COMPOSITIONS CONTAINING DISPERSINE II
US11505767B2 (en) 2017-11-01 2022-11-22 Novozymes A/S Methods for cleansing medical devices
EP4379029A1 (en) 2017-11-01 2024-06-05 Novozymes A/S Polypeptides and compositions comprising such polypeptides
DE102017125558A1 (en) 2017-11-01 2019-05-02 Henkel Ag & Co. Kgaa CLEANING COMPOSITIONS CONTAINING DISPERSINE I
WO2019105675A1 (en) 2017-11-30 2019-06-06 Unilever Plc Detergent composition comprising protease
US20210071155A1 (en) 2018-02-08 2021-03-11 Novozymes A/S Lipase Variants and Compositions Thereof
US20210123033A1 (en) 2018-02-08 2021-04-29 Novozymes A/S Lipases, Lipase Variants and Compositions Thereof
US20210102184A1 (en) 2018-02-23 2021-04-08 Henkel Ag & Co. Kgaa Detergent composition comprising xanthan lyase and endoglucanase variants
CN111770788B (en) 2018-03-13 2023-07-25 诺维信公司 Microencapsulation using amino sugar oligomers
WO2019180111A1 (en) 2018-03-23 2019-09-26 Novozymes A/S Subtilase variants and compositions comprising same
EP3775190A1 (en) 2018-03-29 2021-02-17 Novozymes A/S Mannanase variants and polynucleotides encoding same
CN112262207B (en) 2018-04-17 2024-01-23 诺维信公司 Polypeptides comprising carbohydrate binding activity in detergent compositions and their use for reducing wrinkles in textiles or fabrics
EP3781680A1 (en) 2018-04-19 2021-02-24 Novozymes A/S Stabilized cellulase variants
EP3781679A1 (en) 2018-04-19 2021-02-24 Novozymes A/S Stabilized cellulase variants
EP3775122A1 (en) 2018-05-17 2021-02-17 Unilever PLC Cleaning composition comprising rhamnolipid and alkyl ether carboxylate surfactants
EP3775127B1 (en) 2018-05-17 2022-07-20 Unilever IP Holdings B.V. Cleaning composition
WO2019238761A1 (en) 2018-06-15 2019-12-19 Basf Se Water soluble multilayer films containing wash active chemicals and enzymes
US12270012B2 (en) 2018-06-28 2025-04-08 Novozymes A/S Detergent compositions and uses thereof
US20210071116A1 (en) 2018-06-29 2021-03-11 Novozymes A/S Detergent Compositions and Uses Thereof
EP3814489A1 (en) 2018-06-29 2021-05-05 Novozymes A/S Subtilase variants and compositions comprising same
CN112352039B (en) 2018-07-02 2022-11-15 诺维信公司 Cleaning composition and use thereof
US20210301223A1 (en) 2018-07-03 2021-09-30 Novozymes A/S Cleaning compositions and uses thereof
WO2020008043A1 (en) 2018-07-06 2020-01-09 Novozymes A/S Cleaning compositions and uses thereof
WO2020008024A1 (en) 2018-07-06 2020-01-09 Novozymes A/S Cleaning compositions and uses thereof
WO2020016097A1 (en) 2018-07-17 2020-01-23 Unilever Plc Use of a rhamnolipid in a surfactant system
WO2020020703A1 (en) 2018-07-27 2020-01-30 Unilever N.V. Laundry detergent
JP7530884B2 (en) 2018-07-31 2024-08-08 ダニスコ・ユーエス・インク Mutant alpha-amylases with amino acid substitutions that reduce general acid PKA
BR112021004507A2 (en) 2018-09-17 2021-06-08 Unilever Ip Holdings B.V. detergent composition, method of treating a substrate with a detergent composition and use of a bacterial lipase enzyme
WO2020070063A2 (en) 2018-10-01 2020-04-09 Novozymes A/S Detergent compositions and uses thereof
WO2020070014A1 (en) 2018-10-02 2020-04-09 Novozymes A/S Cleaning composition comprising anionic surfactant and a polypeptide having rnase activity
WO2020070209A1 (en) 2018-10-02 2020-04-09 Novozymes A/S Cleaning composition
WO2020070011A1 (en) 2018-10-02 2020-04-09 Novozymes A/S Cleaning composition
WO2020070249A1 (en) 2018-10-03 2020-04-09 Novozymes A/S Cleaning compositions
EP3861008A1 (en) 2018-10-03 2021-08-11 Novozymes A/S Polypeptides having alpha-mannan degrading activity and polynucleotides encoding same
EP3864122A1 (en) 2018-10-09 2021-08-18 Novozymes A/S Cleaning compositions and uses thereof
EP3864123A1 (en) 2018-10-09 2021-08-18 Novozymes A/S Cleaning compositions and uses thereof
EP3864124A1 (en) 2018-10-11 2021-08-18 Novozymes A/S Cleaning compositions and uses thereof
US20210355469A1 (en) 2018-10-12 2021-11-18 Danisco Us Inc Alpha-amylases with mutations that improve stability in the presence of chelants
CN112839630A (en) 2018-10-12 2021-05-25 联合利华知识产权控股有限公司 Cleaning compositions comprising foam boosting silicones
EP3647397A1 (en) 2018-10-31 2020-05-06 Henkel AG & Co. KGaA Cleaning compositions containing dispersins iv
ES2981999T3 (en) 2018-10-31 2024-10-14 Henkel Ag & Co Kgaa Cleaning compositions containing dispersins V
CN113056548B (en) 2018-11-20 2023-05-02 联合利华知识产权控股有限公司 Detergent composition
CN113015781B (en) 2018-11-20 2022-09-13 联合利华知识产权控股有限公司 Detergent composition
EP3884022B1 (en) 2018-11-20 2024-06-12 Unilever Global Ip Limited Detergent composition
WO2020104158A1 (en) 2018-11-20 2020-05-28 Unilever Plc Detergent composition
EP3884023B1 (en) 2018-11-20 2024-07-17 Unilever Global Ip Limited Detergent composition
EP3891264A1 (en) 2018-12-03 2021-10-13 Novozymes A/S LOW pH POWDER DETERGENT COMPOSITION
EP3891277A1 (en) 2018-12-03 2021-10-13 Novozymes A/S Powder detergent compositions
WO2020127775A1 (en) 2018-12-21 2020-06-25 Novozymes A/S Detergent pouch comprising metalloproteases
US11959111B2 (en) 2018-12-21 2024-04-16 Novozymes A/S Polypeptides having peptidoglycan degrading activity and polynucleotides encoding same
US20220098525A1 (en) 2019-01-22 2022-03-31 Conopco, Inc., D/B/A Unilever Laundry detergent
US20220098520A1 (en) 2019-01-22 2022-03-31 Conopco, Inc., D/B/A Unilever Laundry detergent
EP3702452A1 (en) 2019-03-01 2020-09-02 Novozymes A/S Detergent compositions comprising two proteases
WO2020186052A1 (en) 2019-03-14 2020-09-17 The Procter & Gamble Company Method for treating cotton
JP7275298B2 (en) 2019-03-14 2023-05-17 ザ プロクター アンド ギャンブル カンパニー Cleaning composition containing enzymes
CN113439116B (en) 2019-03-14 2023-11-28 宝洁公司 Enzyme-containing cleaning compositions
AU2020242303A1 (en) 2019-03-21 2021-06-24 Novozymes A/S Alpha-amylase variants and polynucleotides encoding same
CN113785039B (en) 2019-04-03 2024-06-18 诺维信公司 Polypeptides having beta-glucanase activity, polynucleotides encoding the same, and their use in cleaning and detergent compositions
US12247237B2 (en) 2019-04-10 2025-03-11 Novozymes A/S Polypeptide variants
WO2020208056A1 (en) 2019-04-12 2020-10-15 Novozymes A/S Stabilized glycoside hydrolase variants
WO2020229535A1 (en) 2019-05-16 2020-11-19 Unilever Plc Laundry composition
JP7326497B2 (en) 2019-06-24 2023-08-15 ザ プロクター アンド ギャンブル カンパニー Cleaning compositions containing amylase variants
WO2020260006A1 (en) 2019-06-28 2020-12-30 Unilever Plc Detergent compositions
EP3990602B1 (en) 2019-06-28 2025-02-26 Unilever Global IP Limited Detergent composition
BR112021025430A2 (en) 2019-06-28 2022-02-01 Unilever Ip Holdings B V Surfactant composition, detergent composition for home and personal care use and home method for treating a fabric
CN113906124B (en) 2019-06-28 2024-08-02 联合利华知识产权控股有限公司 Detergent composition
EP3990599B1 (en) 2019-06-28 2023-01-18 Unilever Global Ip Limited Detergent composition
US20220364020A1 (en) 2019-06-28 2022-11-17 Conopco, Inc., D/B/A Unilever Detergent composition
WO2021001400A1 (en) 2019-07-02 2021-01-07 Novozymes A/S Lipase variants and compositions thereof
WO2021009067A1 (en) 2019-07-12 2021-01-21 Novozymes A/S Enzymatic emulsions for detergents
CN114787329A (en) 2019-08-27 2022-07-22 诺维信公司 detergent composition
US20220333038A1 (en) 2019-09-02 2022-10-20 Conopco, Inc., D/B/A Unilever Detergent composition
CN114616312A (en) 2019-09-19 2022-06-10 诺维信公司 detergent composition
CN114423851A (en) 2019-09-19 2022-04-29 联合利华知识产权控股有限公司 detergent composition
US20220340843A1 (en) 2019-10-03 2022-10-27 Novozymes A/S Polypeptides comprising at least two carbohydrate binding domains
AR120142A1 (en) 2019-10-07 2022-02-02 Unilever Nv DETERGENT COMPOSITION
US20220403359A1 (en) 2019-10-24 2022-12-22 Danisco Us Inc Variant maltopentaose/maltohexaose-forming alpha-amylases
WO2021105330A1 (en) 2019-11-29 2021-06-03 Basf Se Compositions and polymers useful for such compositions
EP4077617A1 (en) 2019-12-20 2022-10-26 Novozymes A/S Stabilized liquid boron-free enzyme compositions
EP4077656A2 (en) 2019-12-20 2022-10-26 Novozymes A/S Polypeptides having proteolytic activity and use thereof
US20230024242A1 (en) 2019-12-20 2023-01-26 Henkel Ag & Co. Kgaa Cleaning compositions comprising dispersins viii
KR20220119607A (en) 2019-12-20 2022-08-30 헨켈 아게 운트 코. 카게아아 Cleaning Composition Comprising Dispersin IX
CN114829562A (en) 2019-12-20 2022-07-29 汉高股份有限及两合公司 Cleaning compositions comprising dispersible protein VI
KR20220121235A (en) 2019-12-20 2022-08-31 헨켈 아게 운트 코. 카게아아 Cleaning Composition Comprising Dispersin and Carbohydrase
US20240228913A1 (en) 2019-12-23 2024-07-11 Novozymes A/S Enzyme compositions and uses thereof
MX2022007732A (en) 2019-12-23 2022-07-19 Procter & Gamble Compositions comprising enzymes.
US20230159861A1 (en) 2020-01-23 2023-05-25 Novozymes A/S Enzyme compositions and uses thereof
CN115052981A (en) 2020-01-31 2022-09-13 诺维信公司 Mannanase variants and polynucleotides encoding same
US20250002888A1 (en) 2020-01-31 2025-01-02 Novozymes A/S Mannanase variants and polynucleotides encoding same
EP3892708A1 (en) 2020-04-06 2021-10-13 Henkel AG & Co. KGaA Cleaning compositions comprising dispersin variants
EP4133066A1 (en) 2020-04-08 2023-02-15 Novozymes A/S Carbohydrate binding module variants
EP4139431A1 (en) 2020-04-21 2023-03-01 Novozymes A/S Cleaning compositions comprising polypeptides having fructan degrading activity
EP3907271A1 (en) 2020-05-07 2021-11-10 Novozymes A/S Cleaning composition, use and method of cleaning
EP4158011A1 (en) 2020-05-26 2023-04-05 Novozymes A/S Subtilase variants and compositions comprising same
EP4162018B1 (en) 2020-06-08 2024-01-31 Unilever IP Holdings B.V. Method of improving protease activity
EP4172298A1 (en) 2020-06-24 2023-05-03 Novozymes A/S Use of cellulases for removing dust mite from textile
EP3936593A1 (en) 2020-07-08 2022-01-12 Henkel AG & Co. KGaA Cleaning compositions and uses thereof
BR112023003468A2 (en) 2020-08-25 2023-04-11 Novozymes As VARIANTS OF A XYLOGLUCANASE FROM FAMILY 44
EP4204548A1 (en) 2020-08-28 2023-07-05 Novozymes A/S Polyester degrading protease variants
BR112023002833A2 (en) 2020-08-28 2023-03-14 Unilever Ip Holdings B V DETERGENT COMPOSITION AND TREATMENT METHOD OF A TEXTILE ARTICLE
CN116096703A (en) 2020-08-28 2023-05-09 联合利华知识产权控股有限公司 Surfactant and detergent composition
WO2022043042A1 (en) 2020-08-28 2022-03-03 Unilever Ip Holdings B.V. Detergent composition
EP4204396B1 (en) 2020-08-28 2024-05-29 Unilever IP Holdings B.V. Surfactant and detergent composition
US20230303951A1 (en) 2020-08-28 2023-09-28 Conopco, Inc., D/B/A Unilever Detergent composition
US20240240114A1 (en) 2020-09-22 2024-07-18 Basf Se Improved Combination of Protease and Protease Inhibitor with Secondary Enzyme
CN116507725A (en) 2020-10-07 2023-07-28 诺维信公司 Alpha-amylase variants
EP4232539A2 (en) 2020-10-20 2023-08-30 Novozymes A/S Use of polypeptides having dnase activity
EP4237525A1 (en) 2020-10-28 2023-09-06 Novozymes A/S Use of lipoxygenase
CA3196356A1 (en) 2020-10-29 2022-05-05 Catherine Jones Cleaning compositions containing alginate lyase enzymes
WO2022106400A1 (en) 2020-11-18 2022-05-27 Novozymes A/S Combination of immunochemically different proteases
WO2022106404A1 (en) 2020-11-18 2022-05-27 Novozymes A/S Combination of proteases
EP4256020A1 (en) 2020-12-07 2023-10-11 Unilever IP Holdings B.V. Detergent compositions
US20240010951A1 (en) 2020-12-07 2024-01-11 Conopco Inc., D/B/A Unilever Detergent compositions
EP4263771B1 (en) 2020-12-17 2025-02-12 Unilever IP Holdings B.V. Use of a cleaning composition to improve cold cleaning performance
EP4263773B1 (en) 2020-12-17 2024-06-26 Unilever IP Holdings B.V. Cleaning composition
MX2023006625A (en) 2020-12-23 2023-07-04 Procter & Gamble AMPHIPHYL ALCOXYLATED POLYAMINES AND THEIR USES.
EP4032966A1 (en) 2021-01-22 2022-07-27 Novozymes A/S Liquid enzyme composition with sulfite scavenger
CN116829685A (en) 2021-01-28 2023-09-29 诺维信公司 Lipase with low malodor production
EP4039806A1 (en) 2021-02-04 2022-08-10 Henkel AG & Co. KGaA Detergent composition comprising xanthan lyase and endoglucanase variants with im-proved stability
CN116829709A (en) 2021-02-12 2023-09-29 诺维信公司 Alpha-amylase variants
US20250075152A1 (en) 2021-02-12 2025-03-06 Novozymes A/S Stabilized biological detergents
EP4305146A1 (en) 2021-03-12 2024-01-17 Novozymes A/S Polypeptide variants
WO2022194673A1 (en) 2021-03-15 2022-09-22 Novozymes A/S Dnase variants
JP2023548846A (en) 2021-03-15 2023-11-21 ザ プロクター アンド ギャンブル カンパニー Cleaning compositions containing polypeptide variants
EP4060036A1 (en) 2021-03-15 2022-09-21 Novozymes A/S Polypeptide variants
EP4314222A1 (en) 2021-03-26 2024-02-07 Novozymes A/S Detergent composition with reduced polymer content
MX2023012548A (en) 2021-05-05 2023-11-03 Procter & Gamble Methods for making cleaning compositions and detecting soils.
EP4108767A1 (en) 2021-06-22 2022-12-28 The Procter & Gamble Company Cleaning or treatment compositions containing nuclease enzymes
WO2022268885A1 (en) 2021-06-23 2022-12-29 Novozymes A/S Alpha-amylase polypeptides
WO2023041694A1 (en) 2021-09-20 2023-03-23 Unilever Ip Holdings B.V. Detergent composition
WO2023061928A1 (en) 2021-10-12 2023-04-20 Novozymes A/S Endoglucanase with improved stability
WO2023064749A1 (en) 2021-10-14 2023-04-20 The Procter & Gamble Company A fabric and home care product comprising cationic soil release polymer and lipase enzyme
US20250051745A1 (en) 2021-12-16 2025-02-13 Danisco Us Inc. Variant maltopentaose/maltohexaose-forming alpha-amylases
EP4206309A1 (en) 2021-12-30 2023-07-05 Novozymes A/S Protein particles with improved whiteness
JP2025507704A (en) 2022-02-24 2025-03-21 エボニック オペレーションズ ゲーエムベーハー Bio-based Compositions
EP4234664A1 (en) 2022-02-24 2023-08-30 Evonik Operations GmbH Composition comprising glucolipids and enzymes
JP2025507844A (en) 2022-03-02 2025-03-21 ノボザイムス アクティーゼルスカブ Use of xyloglucanases to improve the sustainability of detergents
EP4486876A1 (en) 2022-03-04 2025-01-08 Novozymes A/S Dnase variants and compositions
CN118974228A (en) 2022-04-08 2024-11-15 诺维信公司 Hexosaminidase variants and compositions
EP4273210A1 (en) 2022-05-04 2023-11-08 The Procter & Gamble Company Detergent compositions containing enzymes
EP4273209A1 (en) 2022-05-04 2023-11-08 The Procter & Gamble Company Machine-cleaning compositions containing enzymes
WO2023247348A1 (en) 2022-06-21 2023-12-28 Novozymes A/S Mannanase variants and polynucleotides encoding same
KR20250033238A (en) 2022-06-28 2025-03-07 에보닉 오퍼레이션스 게엠베하 Composition comprising a biosurfactant and persicomycin
WO2024083819A1 (en) 2022-10-20 2024-04-25 Novozymes A/S Lipid removal in detergents
WO2024115213A1 (en) 2022-11-30 2024-06-06 Evonik Operations Gmbh Detergent compartment pouch comprising biosurfactants
AU2023388516A1 (en) 2022-12-05 2025-04-10 Novozymes A/S Protease variants and polynucleotides encoding same
AU2023393689A1 (en) 2022-12-14 2025-05-01 Novozymes A/S Improved lipase (gcl1) variants
WO2024131880A2 (en) 2022-12-23 2024-06-27 Novozymes A/S Detergent composition comprising catalase and amylase
WO2024156628A1 (en) 2023-01-23 2024-08-02 Novozymes A/S Cleaning compositions and uses thereof
EP4410941A1 (en) 2023-02-01 2024-08-07 The Procter & Gamble Company Detergent compositions containing enzymes
WO2024163584A1 (en) 2023-02-01 2024-08-08 Danisco Us Inc. Subtilisin variants and methods of use
WO2024194190A1 (en) 2023-03-17 2024-09-26 Unilever Ip Holdings B.V. Composition
WO2024194245A1 (en) 2023-03-21 2024-09-26 Novozymes A/S Detergent compositions based on biosurfactants
WO2024213513A1 (en) 2023-04-12 2024-10-17 Novozymes A/S Compositions comprising polypeptides having alkaline phosphatase activity
EP4461795A1 (en) 2023-05-10 2024-11-13 Novozymes A/S Detergent composition comprising laccase
EP4461796A1 (en) 2023-05-10 2024-11-13 Novozymes A/S Detergent composition comprising laccase
EP4481027A1 (en) 2023-06-19 2024-12-25 The Procter & Gamble Company Cleaning compositions containing enzymes
WO2025002934A1 (en) 2023-06-28 2025-01-02 Novozymes A/S Detergent composition comprising lipases
EP4488351A1 (en) 2023-07-03 2025-01-08 The Procter & Gamble Company Compositions containing a porphyrin binding protein
WO2025011933A1 (en) 2023-07-07 2025-01-16 Novozymes A/S Washing method for removing proteinaceous stains
WO2025036643A1 (en) 2023-08-15 2025-02-20 Evonik Operations Gmbh Biosurfactant for washing wool
WO2025071996A1 (en) 2023-09-28 2025-04-03 Danisco Us Inc. Variant cutinase enzymes with improved solubility and uses thereof
WO2025088003A1 (en) 2023-10-24 2025-05-01 Novozymes A/S Use of xyloglucanase for replacement of optical brightener

Family Cites Families (12)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3251742A (en) * 1962-05-14 1966-05-17 Revlon Method for coloring human hair with polyhydric aromatic compound, aromatic amine andan oxidation enzyme
US3957424A (en) * 1971-10-27 1976-05-18 The Procter & Gamble Company Enzyme-activated oxidative process for coloring hair
US3893803A (en) * 1972-10-10 1975-07-08 Procter & Gamble Hair dyeing premixes containing peroxidase enzymes stabilized with heme complexing agents
DD291094A5 (en) * 1989-12-28 1991-06-20 Veb Filmfabrik Wolfen,De ANALYTICAL ELEMENT FOR DETERMINING INVERTASE
FR2673534B1 (en) * 1991-03-08 1995-03-03 Perma COMPOSITION FOR THE ENZYMATIC COLORING OF KERATINIC FIBERS, ESPECIALLY HAIR, AND ITS APPLICATION IN A COLORING PROCESS.
US5380719A (en) * 1992-04-28 1995-01-10 E. R. Squibb & Sons, Inc. Quinoxaline biphenyl angiotensin II inhibitors
JP3522909B2 (en) * 1995-07-21 2004-04-26 大日本印刷株式会社 Thermal transfer sheet
DE69613143T2 (en) * 1995-11-30 2002-03-07 Novozymes As LACCASES WITH IMPROVED COLOR CHARACTERISTICS
US5972042A (en) * 1995-12-22 1999-10-26 Novo Nordisk A/S Method for dyeing a material with a dyeing system which contains an enzymatic oxidizing agent
US6004355A (en) * 1995-12-29 1999-12-21 Procter & Gamble Company Hair coloring compositions comprising a peroxygen oxidizing agent, an organic peroxyacid precursor, and oxidative hair coloring agents
US6022381A (en) * 1995-12-29 2000-02-08 Procter & Gamble Company Oxidative hair coloring compositions which contain a preformed organic peroxyacid oxidizing agent
DE69708276D1 (en) * 1996-04-03 2001-12-20 Novozymes As COLORING KERATINE FIBERS WITH THE ENZYME

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US6231621B1 (en) 2001-05-15
CA2265734A1 (en) 1998-04-16
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EP0963192B1 (en) 2003-01-08
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EP0963192A2 (en) 1999-12-15
AU4452397A (en) 1998-05-05

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