EP1362089B1 - Verminderung von unangenehmen gerüchen von wäsche - Google Patents

Verminderung von unangenehmen gerüchen von wäsche Download PDF

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Publication number
EP1362089B1
EP1362089B1 EP02711783A EP02711783A EP1362089B1 EP 1362089 B1 EP1362089 B1 EP 1362089B1 EP 02711783 A EP02711783 A EP 02711783A EP 02711783 A EP02711783 A EP 02711783A EP 1362089 B1 EP1362089 B1 EP 1362089B1
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EP
European Patent Office
Prior art keywords
lysostaphin
enzyme
laundry
detergent
malodor
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Expired - Lifetime
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EP02711783A
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English (en)
French (fr)
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EP1362089A1 (de
Inventor
Charlotte Johansen
Signe Munk
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Novozymes AS
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Novozymes AS
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Publication date
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Publication of EP1362089A1 publication Critical patent/EP1362089A1/de
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Publication of EP1362089B1 publication Critical patent/EP1362089B1/de
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Expired - Lifetime legal-status Critical Current

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/0005—Other compounding ingredients characterised by their effect
    • C11D3/0068—Deodorant compositions
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/12—Soft surfaces, e.g. textile

Definitions

  • the invention relates to enzymatic reduction of malodor from laundry.
  • WO 90/09739 discloses compositions including lysostaphin and nisin, which are used for treating bacterial infections.
  • WO 91/10723 discloses a bacteriolytic enzyme from Nocardiopsis dassonvillei and it's use in e.g. detergent compositions.
  • the invention provides a method comprising contacting laundry with an enzyme having lysostaphin activity.
  • composition comprising a surfactant and an enzyme having lysostaphin activity and one or more other enzymes selected from protease, lipase, cutinase, amylase, carbohy-drase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, laccase, and peroxidase.
  • Lysostaphin is a glycyl-glycine endopeptidase from the enzyme class E.C. 3.4.24.75. It hydrolyses the -Gly-Gly- bond in the polyglycine inter-peptide link joining staphylococcal cell wall peptidoglycans. Lysostaphin is commercially available from several suppliers, such as from Sigma-Aldrich, Inc.
  • An enzyme having lysostaphin activity may be a natural or synthetic variant of lysostaphin, wherein amino acid substitutions or deletions have been introduced. It may also be an amino acid fragment with lysostaphin activity, which is optionally fused to one or more other proteins.
  • lysostaphin activity will reduce the turbidity (absorbance at 620 nm) of a suspension of Staphylococcus aureus (ATCC 6538) cells by 50%, when the initial absorbance is approximately 0.250, after 10 minutes at pH 7.5 and 37 degrees celcius.
  • the malodor of the method of the invention thus comprises all body odors present in laundry originating from contact with the human skin.
  • the malodor may be axillary odors, such as the smell of sweat.
  • the malodor may originate from activity of Staphylococcus species (such as S . aureus, S. epidermis, S. intermedius, S. saprophyticus and S. hyicus).
  • Staphylococcus species such as S . aureus, S. epidermis, S. intermedius, S. saprophyticus and S. hyicus.
  • the malodor originates from fabrics which have been in contact with the axilla.
  • the laundry of the method of the invention comprises all kinds of textile items or fabrics suitable for being used as clothes or for personal use in other ways comprising contact with the human skin.
  • the "Malodor index (48 hours)" may be reduced by at least 10% (preferably 20%, more preferably 30%, most preferably 40%, and in particular 50%) compared to laundry which has not been contacted with an enzyme having lysostaphin activity.
  • the method of the invention may also result in killing or inhibiting growth of microbial cells in laundry.
  • the microbial cells are bacteria, such as Staphylococcus species.
  • the method of the invention may result in a reduction in the number of living microbial cells of at least 25%, preferably at least 50%, more preferably at least 90%, and most preferably at least 99%.
  • microbial cells denotes bacterial cells (such as Staphylococcus species), fungal cells or algae, and the term “microorganism” denotes a fungus (including yeasts) or a bacterium
  • the present invention covers use of an enzyme for reducing malodor from laundry items.
  • the enzyme may have lysostaphin activity.
  • the invention may also be used for reducing the number of living bacteria in laundry; for reducing allergens in laundry; or for sterilizing laundry.
  • Lysostaphin may be added to and thus become a component of a detergent composition.
  • the detergent composition of the invention may for example be formulated as a hand or machine laundry detergent composition including a laundry additive composition suitable for pre-treatment of stained fabrics and a rinse added fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations.
  • the invention provides a detergent additive comprising lysostaphin.
  • the detergent additive as well as the detergent composition comprises one or more other enzymes selected from protease, lipase, cutinase, amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, laccase and peroxidase.
  • the properties of the chosen enzyme(s) should be compatible with the selected detergent, (i.e. pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.
  • proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included.
  • the protease may be a serine protease or a metallo protease, preferably an alkaline microbial protease or a trypsin-like protease.
  • alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279).
  • trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270 and WO 94/25583.
  • Examples of useful proteases are the variants described in WO 92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially the variants with substitutions in one or more of the following positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235 and 274.
  • Preferred commercially available protease enzymes include AlcalaseTM, SavinaseTM, PrimaseTM, EverlaseTM, EsperaseTM, and KannaseTM (Novozymes A/S), MaxataseTM, MaxacalTM, MaxapemTM, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).
  • Lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa ( T. lanuginosus) as described in EP 258 068 and EP 305 216 or from H . insolens as described in WO 96/13580, a Pseudomonas lipase, e.g. from P. alcaligenes or P . pseudoalcaligenes (EP 218 272), P . cepacia (EP 331 376), P . stutzeri (GB 1,372,034), P .
  • lipase variants such as those described in WO 92/05249, WO 94/01541, EP 407 225, EP 260 105, WO 95/35381, WO 96/00292, WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202.
  • Preferred commercially available lipase enzymes include LipolaseTM, Lipolase UltraTM and LipoprimeTM(Novozymes A/S).
  • Amylases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, ⁇ -amylases obtained from Bacillus, e.g. a special strain of B . licheniformis, described in more detail in GB 1,296,839.
  • Examples of useful amylases are the variants described in WO 94/02597, WO 94/18314, WO 96/23873, and WO 97/43424, especially the variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 181, 188, 190, 197, 202, 208, 209, 243, 264, 304, 305, 391, 408, and 444.
  • amylases are DuramylTM, TermamylTM, FungamylTM and BANTM (Novozymes A/S), RapidaseTM and PurastarTM (Genencor International Inc.).
  • Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g. the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757 and WO 89/09259.
  • cellulases are the alkaline or neutral cellulases having colour care benefits.
  • Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940.
  • Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95/24471, WO 98/12307 and PCT/DK98/00299.
  • cellulases include CelluzymeTM, and CarezymeTM (Novozymes A/S), ClazinaseTM, and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (Kao Corporation).
  • Peroxidases/Oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g. from C . cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.
  • the detergent enzyme(s) may be included in a detergent composition by adding separate additives containing one or more enzymes, or by adding a combined additive comprising all of these enzymes.
  • a detergent additive of the invention i.e. a separate additive or a combined additive, can be formulated e.g. as a granulate, a liquid, a slurry, etc.
  • Preferred detergent additive formulations are granulates, in particular non-dusting granulates, liquids, in particular stabilized liquids, or slurries.
  • Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and 4,661,452 and may optionally be coated by methods known in the art.
  • waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids.
  • film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591.
  • Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods.
  • Protected enzymes may be prepared according to the method disclosed in EP 238,216.
  • the detergent composition of the invention may be in any convenient form, e.g., a bar, a tablet, a powder, a granule, a paste or a liquid.
  • a liquid detergent may be aqueous, typically containing up to 70 % water and 0-30 % organic solvent, or nonaqueous.
  • the detergent composition comprises one or more surfactants, which may be non-ionic including semi-polar and/or anionic and/or cationic and/or zwitterionic.
  • the surfactants are typically present at a level of from 0.1 % to 60% by weight.
  • the detergent When included therein the detergent will usually contain from about 1 % to about 40% of an anionic surfactant such as linear alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid or soap.
  • an anionic surfactant such as linear alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid or soap.
  • the detergent When included therein the detergent will usually contain from about 0.2% to about 40% of a non-ionic surfactant such as alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, or N-acyl N-alkyl derivatives of glucosamine (“glucamides").
  • a non-ionic surfactant such as alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, or N-acyl N-alkyl derivatives of glucosamine (“glucamides”).
  • glucamides N-acyl N-alkyl derivatives of glucosamine
  • the detergent may contain 0-65 % of a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, carbonate, citrate, nitrilotriacetic acid, ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, alkyl- or alkenylsuccinic acid, soluble silicates or layered silicates (e.g. SKS-6 from Hoechst).
  • a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, carbonate, citrate, nitrilotriacetic acid, ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, alkyl- or alkenylsuccinic acid, soluble silicates or layered silicates (e.g. SKS-6 from Hoechst).
  • the detergent may comprise one or more polymers.
  • examples are carboxymethylcellulose, poly(vinylpyrrolidone), poly (ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers.
  • the detergent may contain a bleaching system which may comprise a H 2 O 2 source such as perborate or percarbonate which may be combined with a peracid-forming bleach activator such as tetraacetylethylenediamine or nonanoyloxybenzenesulfonate.
  • a bleaching system may comprise peroxyacids of e.g. the amide, imide, or sulfone type.
  • the enzyme(s) of the detergent composition of the invention may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in e.g. WO 92/19709 and WO 92/19708.
  • a polyol such as propylene glycol or glycerol
  • a sugar or sugar alcohol lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid
  • the detergent may also contain other conventional detergent ingredients such as e.g. fabric conditioners including clays, foam boosters, suds suppressors, anticorrosion agents, soil-suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, or perfumes.
  • fabric conditioners including clays, foam boosters, suds suppressors, anticorrosion agents, soil-suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, or perfumes.
  • any enzyme in particular lysostaphin, may be added in an amount corresponding to 0.01-100 mg of enzyme protein per liter of wash liquor, preferably 0.05-10 mg of enzyme protein per liter of wash liquor, more preferably 0.1-5 mg of enzyme protein per liter of wash liquor, and most preferably 0.1-1 mg of enzyme protein per liter of wash liquor.
  • Lysostaphin may additionally be incorporated in the detergent formulations disclosed in WO 97/07202.
  • the chemicals used in the following examples were commercial products of at least reagent grade.
  • the Malthus Flexi M2060 instrument is available from Malthus Instruments Limited, England.
  • TLB Tryptone Soya Broth
  • lysostaphin is tested in a one-cycle washing trial carried out in a thermostated Terg-O-tometer (available from United States Testing Co, 1415 Park Ave, Hoboken NJ07030).
  • Swatches of 100% polyester or 100% cotton (10 x 14 cm, previously cleaned by solvent extraction - hexane for polyester, chloroform for cotton - using a Soxhlet) are soiled by applying human male axillary sweat and sebum from the armpits and upper body of male runners after extensive exercise.
  • Two swatches (10 x 14 cm) are used for each male - one swatch is made of 100% polyester and one is made of 100% cotton.
  • the left armpit and left part of the upper body is wiped with one swatch, and the right armpit and right part of the upper body is wiped with the other swatch after exercising. This procedure is performed twice before washing. Prior to the washing, each swatch is cut into 12 equally sized pieces and distributed between four Terg-O-tometer wash beakers. Cotton and polyester textiles are kept apart.
  • Washing is done in Terg-O-tometer using phosphate buffer (0.05 M, pH 7.5). Temperature: 32°C Lysostaphin dose: 5 mg/L (Sigma L4402) Wash time: 12 minutes Wash liquid: 1000 mL per wash beaker Rinsing: 15 minutes in running tap water
  • Staphylococcus aureus was grown overnight (TSB; Tryptone Soya Broth) and inoculated to approximately 10 3 Colony forming units/ml (CFU/ml) in diluted TSB (1:1).
  • TSB Tryptone Soya Broth
  • CFU/ml Colony forming units/ml
  • Sterile cotton swatches were inoculated overnight in the diluted TSB allowing S.aureus to grow on the textile.
  • the swatches were rinsed in sterile water for 30 seconds and dried in sterile air for 30 minutes. Swatches were washed in a beaker with stirring at 32°C for 20 minutes in either phosphate buffer (0.05 M, pH 7.5) or in a liquid U.S.
  • Direct Malthus measurements were used when enumerating total survival cells.
  • the cell metabolism was determined by conductance measurements in the growth substrate. The swatches were after enzyme treatment transferred to the Malthus cell. As cells attached to the textile are growing, the cell metabolism will change the conductance in the growth medium. When the conductance change is measurable by the Malthus, a detection time (dt) will be recorded. The dt's were converted to colony counts by use of a calibration curve relating CFU/swatch to dt.
  • Lysostaphin resulted in a reduction of the microbial cell number of approximately 10 1 to 10 2 CFU/swatch.
  • a reduction in cell number was also determined after lysostaphin treatment in detergent, however, the determination of the exact cell number was not possible by using the Malthus. But a delay in outgrowth of the microorganism was observed visually from the swatches washed in detergent with lysostaphin, this delay corresponds to a lower cell number on the swatches compared to the swatches washed without lysostaphin.

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

Claims (8)

  1. Verfahren umfassend das Inkontaktbringen von Waschgut mit einem Enzym mit Lysostaphin-Aktivität.
  2. Verfahren nach Anspruch 1, wobei das Enzym Lysostaphin ist.
  3. Verfahren nach Anspruch 1, welches ein Verfahren zum Reduzieren schlechten Geruchs von Waschgut ist.
  4. Verfahren nach Anspruch 3, wobei der "Index für schlechten Geruch (48 Stunden)" ("malodor index (48 hours)") im Vergleich zu Waschgut, das nicht mit einem Enzym mit Lysostaphin-Aktivität in Kontakt gebracht wurde, um 10 % reduziert wird.
  5. Zusammensetzung umfassend einen oberflächenaktiven Stoff und ein Enzym mit Lysostaphin-Aktivität und ein oder mehrere andere Enzyme ausgewählt aus Protease, Lipase, Cutinase, Amylase, Carbohydrase, Cellulase, Pectinase, Mannanase, Arabinase, Galactanase, Xylanase, Oxidase, Laccase und Peroxidase.
  6. Zusammensetzung von Anspruch 5, wobei das Enzym Lysostaphin ist.
  7. Verwendung eines Enzyms mit Lysostaphin-Aktivität zum Reduzieren schlechten Geruchs von Waschgut.
  8. Verwendung von Lysostaphin zum Reduzieren schlechten Geruchs von Waschgut.
EP02711783A 2001-02-17 2002-02-12 Verminderung von unangenehmen gerüchen von wäsche Expired - Lifetime EP1362089B1 (de)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
DK200100270 2001-02-17
DKPA200100270 2001-02-17
PCT/DK2002/000097 WO2002066591A1 (en) 2001-02-17 2002-02-12 Reduction of malodour from laundry

Publications (2)

Publication Number Publication Date
EP1362089A1 EP1362089A1 (de) 2003-11-19
EP1362089B1 true EP1362089B1 (de) 2007-01-03

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EP (1) EP1362089B1 (de)
JP (1) JP4071632B2 (de)
AT (1) ATE350448T1 (de)
AU (1) AU2002231607B2 (de)
DE (1) DE60217297T2 (de)
WO (1) WO2002066591A1 (de)

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WO2007026331A1 (en) 2005-09-02 2007-03-08 The Procter & Gamble Company Laundry scent customization
DE102006008996A1 (de) * 2006-02-23 2007-09-06 Weber, Lothar Ernst Wilhelm Mittel und Verfahren zur Reinigung der Raumluft von Schadstoffen, Geruchsstoffen und anderen störenden Bestandteilen
CN105441353B (zh) 2006-08-11 2019-01-01 诺维信生物股份有限公司 细菌培养物和包含细菌培养物的组合物
CN107815817A (zh) 2011-02-15 2018-03-20 诺维信生物股份有限公司 清洁机器及清洁方法中的气味的减轻
RU2718554C1 (ru) 2017-09-25 2020-04-08 Георгий Георгиевич Чумбуридзе Термостабильная композиция, обладающая антивирусной и антибактериальной активностью и ее использование
TW201940778A (zh) 2018-01-16 2019-10-16 日商花王股份有限公司 角質汙垢清潔劑、及角質汙垢分解能力之評估方法

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BR9707789A (pt) * 1996-02-29 1999-07-27 Procter & Gamble Composições de limpeza compreendendo endo-dextranase
WO1997043378A1 (en) * 1996-05-15 1997-11-20 The Procter & Gamble Company DETERGENT COMPOSITIONS COMPRISING A COMBINATION OF α-AMYLASES FOR MALODOR STRIPPING
JPH09310092A (ja) * 1996-05-22 1997-12-02 Lion Corp 魚臭除去洗浄剤組成物およびその使用方法
US6080391A (en) * 1997-08-14 2000-06-27 Novo Nordisk A/S Reduction of malodour

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1990009739A1 (en) * 1989-03-01 1990-09-07 The Public Health Research Institute Of The City Of New York, Inc. Novel bacteriocin compositions for use as enhanced broad range bactericides and methods of preventing and treating microbial infection

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DE60217297T2 (de) 2007-10-04
AU2002231607B2 (en) 2008-02-28
JP4071632B2 (ja) 2008-04-02
EP1362089A1 (de) 2003-11-19
WO2002066591A1 (en) 2002-08-29
JP2004527603A (ja) 2004-09-09
ATE350448T1 (de) 2007-01-15
DE60217297D1 (de) 2007-02-15

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