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WO2002008377A1 - Compositions antimicrobiennes - Google Patents

Compositions antimicrobiennes Download PDF

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Publication number
WO2002008377A1
WO2002008377A1 PCT/DK2001/000454 DK0100454W WO0208377A1 WO 2002008377 A1 WO2002008377 A1 WO 2002008377A1 DK 0100454 W DK0100454 W DK 0100454W WO 0208377 A1 WO0208377 A1 WO 0208377A1
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WIPO (PCT)
Prior art keywords
composition
enzymatic
cas
acid
enzyme
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PCT/DK2001/000454
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English (en)
Inventor
Charlotte Johansen
Dorrit Aaslyng
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Novozymes A/S
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Priority to AU2001268953A priority Critical patent/AU2001268953A1/en
Publication of WO2002008377A1 publication Critical patent/WO2002008377A1/fr

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    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
    • A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
    • A01N37/00—Biocides, pest repellants or attractants, or plant growth regulators containing organic compounds containing a carbon atom having three bonds to hetero atoms with at the most two bonds to halogen, e.g. carboxylic acids
    • A01N37/44—Biocides, pest repellants or attractants, or plant growth regulators containing organic compounds containing a carbon atom having three bonds to hetero atoms with at the most two bonds to halogen, e.g. carboxylic acids containing at least one carboxylic group or a thio analogue, or a derivative thereof, and a nitrogen atom attached to the same carbon skeleton by a single or double bond, this nitrogen atom not being a member of a derivative or of a thio analogue of a carboxylic group, e.g. amino-carboxylic acids
    • A01N37/46—N-acyl derivatives
    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
    • A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
    • A01N61/00—Biocides, pest repellants or attractants, or plant growth regulators containing substances of unknown or undetermined composition, e.g. substances characterised only by the mode of action
    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
    • A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
    • A01N63/00—Biocides, pest repellants or attractants, or plant growth regulators containing microorganisms, viruses, microbial fungi, animals or substances produced by, or obtained from, microorganisms, viruses, microbial fungi or animals, e.g. enzymes or fermentates
    • A01N63/50—Isolated enzymes; Isolated proteins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/49—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing heterocyclic compounds
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A61K8/66—Enzymes
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L2/00—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor
    • A61L2/0005—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor for pharmaceuticals, biologicals or living parts
    • A61L2/0082—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor for pharmaceuticals, biologicals or living parts using chemical substances
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L2/00—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor
    • A61L2/16—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor using chemical substances
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q17/00—Barrier preparations; Preparations brought into direct contact with the skin for affording protection against external influences, e.g. sunlight, X-rays or other harmful rays, corrosive materials, bacteria or insect stings
    • A61Q17/005—Antimicrobial preparations
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38654—Preparations containing enzymes, e.g. protease or amylase containing oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/48—Medical, disinfecting agents, disinfecting, antibacterial, germicidal or antimicrobial compositions
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
    • A61K2800/40—Chemical, physico-chemical or functional or structural properties of particular ingredients
    • A61K2800/52—Stabilizers
    • A61K2800/524—Preservatives
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q11/00—Preparations for care of the teeth, of the oral cavity or of dentures; Dentifrices, e.g. toothpastes; Mouth rinses
    • C—CHEMISTRY; METALLURGY
    • C02—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
    • C02F1/00—Treatment of water, waste water, or sewage
    • C02F1/50—Treatment of water, waste water, or sewage by addition or application of a germicide or by oligodynamic treatment
    • 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
    • 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
    • C11D2111/14—Hard surfaces
    • 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
    • C11D2111/14—Hard surfaces
    • C11D2111/20—Industrial or commercial equipment, e.g. reactors, tubes or engines

Definitions

  • compositions with antimicrobial activity comprising an enzymatic component and one or more non-enzymatic biocides.
  • an antimicrobial composition comprising an enzymatic component and one or more non- enzymatic biocides.
  • the present invention provides a method for killing or inhibiting microbial cells comprising treating said microbial cells with an enzymatic component and one or more non-enzymatic biocides.
  • the present invention provides a detergent composition comprising an enzymatic component, one or more non-enzymatic biocides and a surfactant.
  • the present invention is useful at any locus subject to contamination by bacteria, fungi, yeast or algae; for the preservation of food, beverages, cosmetics, deodorants, contact lens products, food ingredients or enzyme compositions; as a disinfection for use, e.g., on human or animal skin, hair, oral cavity, mucous membranes, wounds, bruises or in the eye; for killing microbial cells in laundry; for incorporation in cleaning compositions; and for disinfection of hard surfaces, in the pulp and paper industry, in the oil industry, or for water treatment.
  • the terms "antimicrobial” and “biocidal” are intended to mean that there is a bactericidal and/or a bacteriostatic and/or fungicidal and/or fungistatic effect and/or a virucidal effect, wherein The term “bactericidal” is to be understood as capable of killing bacterial cells.
  • bacteriostatic is to be understood as capable of inhibiting bacterial growth, i.e. inhibiting growing bacterial cells.
  • fungicidal is to be understood as capable of killing fungal cells.
  • fungistatic is to be understood as capable of inhibiting fungal growth, i.e. inhibiting growing fungal cells.
  • virus is to be understood as capable of inactivating virus.
  • microbial cells denotes bacterial cells, fungal cells or algae
  • microorganism denotes a fungus (including yeasts) or a bacterium.
  • the term "inhibiting growth of microbial cells” is intended to mean that the cells are in the non-growing state, i.e., that they are not able to propagate.
  • hard surface as used herein relates to any surface, which is essentially non-permeable for microorganisms.
  • hard surfaces are surfaces made from metal, e.g., stainless steel, plastics, rubber, board, glass, wood, paper, textile, concrete, rock, marble, gypsum and ceramic materials which optionally may be coated, e.g., with paint, enamel and the like.
  • the hard surface can also be a process equipment, e.g., a cooling tower, an osmotic membrane, a water treatment plant, a dairy, a food processing plant, a chemical plant, a pharmaceutical process plant, a pulp and paper plant or an oil processing plant. Accordingly, the composition according to the present invention is useful in a conventional cleaning-in-place (C-l- P) system.
  • biocide includes disinfectants and preservatives, such as bactericides, fungicides, and algaecides.
  • the term "disinfectant” is defined as a compound which is capable of reducing the number of living cells of Escherichia coli (DSM 1576) to 1/100 after 10 min. incubation at 20°C in an aqueous solution of 50%(w/w); preferably in an aqueous solution of 40%(w/w); more preferably in an aqueous solution of 25%(w/w); even more preferably in an aqueous solution of 10%(w/w); most preferably in an aqueous solution of 5%(w/w); and in particular in an aqueous solution of 1%(w/w).
  • preservative is defined as a compound which is capable of inhibiting the outgrowth of Escherichia coli (DSM1576) for 24 hours at 25°C in a microbial growth substrate, when added in a concentration of 1000 ppm; preferably when added in a concentration of 500 ppm; more preferably when added in a concentration of 250 ppm; even more preferably when added in a concentration of 100 ppm; most preferably when added in a concentration of 50 ppm; and in particular when added in a concentration of 25 ppm.
  • the biocides of the composition of the invention may consist of the disinfectants and preservatives defined above.
  • the biocide may be a polypeptide having from 2 to 50 amino acid residues, preferably having from 2 to 40 amino acid residues, more preferably having from 2 to 30 amino acid residues, most preferably having from 5 to 30 amino acid residues, and in particular having from 5 to 20 amino acid residues.
  • the biocide may not have any enzymatic activity as defined by any enzyme class, such as an enzyme class selected from the group consisting of EC 1.-.-.-, EC 2.-.-.-, EC 3.-.-.-, EC 4.-.-.-, EC 5.-.-.-, and EC 6.-.-.-.
  • the biocide may not be a polypeptide having more than 50 amino acid residues; preferably the biocide may not be a polypeptide having more than 30 amino acid residues; more preferably the biocide may not be a polypeptide having more than 10 amino acid residues; and most preferably the biocide is not a polypeptide.
  • the biocide is not a substrate for the enzyme(s) included in the composition of the invention. In another embodiment, the biocide is not capable of reacting with the enzyme(s) included in the composition of the invention. In yet another embodiment, the biocide is not a substrate of, or capable of reacting with, an oxidoreductase. In yet another embodiment, the biocide is not a substrate of, or capable of reacting with, a hydrolase as defined in the enzyme class EC 3.-.-.-.
  • the biocides may also be selected from the group consisting of quaternary ammonium compounds, aldehydes, triclosan, organometals, biguanides, phenolics, halogenated organic compounds, inorganics, iodophors and amphoterics.
  • Preferred biocides are those selected from the group consisting of Benzoic acid (CAS 65-85-0), Sodium benzoate (CAS 532-32-1), Benzylalcohol (CAS 100-51-6), Bronopol (CAS 52-51-7), Chlorhexidine (CAS 55-56-1), Chlorhexidine digluconate (CAS 18472-51-0), Chlorhexidine diacetate (56-95-1), chlorhexidine di-hydrochloride
  • Methylisothiazolinone (CAS 2682-20-4), methylparaben (CAS 99-76-3), ethylparabens (CAS 120-47-8), propylparabens (CAS 94-13-3), Butylparabens (CAS 94-26-8), Isopropylparabens (CAS 4191-73-5), Isobutylparabens (CAS 4247-02-3), Benzylparabens (CAS 94-18-8), Phenethyl alcohol (CAS 60-12-8), Phenoxyethanol (CAS 122-99-6), Quatemium-15 (CAS 51229-78-8), Sorbic acid (CAS 110-44-1),
  • chelating agents like EDTA (CAS 60-00-4), polyphosphates, Pentetic acids (CAS 67- 43-6), Hydroxyethyl ethylenediamine triacetic acid (CAS 150-39-0) and Etidronic acid (CAS 2809-21-4).
  • Enzymatic component EDTA (CAS 60-00-4), polyphosphates, Pentetic acids (CAS 67- 43-6), Hydroxyethyl ethylenediamine triacetic acid (CAS 150-39-0) and Etidronic acid (CAS 2809-21-4).
  • the enzymatic component comprise one or more enzymes, such as proteases, lipases, cutinases, amylases, carbohydrases, cellulases, pectinases, mannanases, arabinases, galactanases, xylanases and/or oxidoreductases; preferably the enzymatic component comprise at least an oxidoreductase.
  • the enzyme is a hydrolase as defined in the enzyme class EC 3.-.-.-.
  • Oxidoreductases are defined as the enzyme class EC 1.-.-.-.
  • Preferred oxidoreductases are phenol oxidizing enzymes, such as oxidases (e.g. laccases) and peroxidases (e.g. haloperoxidases); more preferred oxidoreductases are laccases, peroxidases and haloperoxidases; most preferred oxidoreductases are haloperoxidases. It is to be understood that oxidoreductase variants (e.g. produced by recombinant techniques) are included within the meaning of the term "oxidoreductase".
  • the enzymatic component comprise an oxidoreductase and one or more other enzymes, such as proteases, lipases, cutinases, amylases, carbohydrases, cellulases, pectinases, mannanases, arabinases, galactanases and/or xylanases.
  • enzymes such as proteases, lipases, cutinases, amylases, carbohydrases, cellulases, pectinases, mannanases, arabinases, galactanases and/or xylanases.
  • the enzymatic component comprises a lytic enzyme capable of degrading a microbial cell envelope. In another embodiment, the enzymatic component does not comprise a lytic enzyme capable of degrading a microbial cell envelope.
  • the enzymatic component may comprise compounds known in the art necessary to obtain the desired enzymatic activity, such as oxygen (O 2 ) in the case of laccases, a source of hydrogen peroxide (H 2 O 2 ) in the case of peroxidases, and a source of halide (chloride, bromide, iodide) in the case of haloperoxidases.
  • the enzymatic component consists of a haloperoxidase, a source of hydrogen peroxide and a source of halide.
  • the enzymatic component may also comprise compounds capable of enhancing the enzymatic activity (enhancing agents), and other conventional additives known in the art for stabilizing the enzyme(s), such as polyethylene glycol (PEG) and polymers like polyacrylate or polyvinyl pyrrolidone.
  • concentration of the enzyme(s) in the final antimicrobial composition is typically in the range of 0.01-100 ppm, preferably 0.05-50 ppm, more preferably 0.1-20 ppm, and most preferably 0.5-10 ppm.
  • the enzymatic component may be capable of reducing the number of living cells (killing) of E. coll (DSM1576) to less than 95% (preferably less than 90%, more preferably less than 75%, most preferably less than 50%), when incubated 10 min.
  • the enzymatic component may also be capable of increasing the time before outgrowth (inhibiting) of E. coli (DSM1576) at 25°C in a microbial growth substrate containing 1 mg/L of the enzymatic component by at least 5%, preferably at least 10%, more preferably at least 25%, and most preferably at least 50%.
  • Preferred commercially available proteases include AlcalaseTM, SavinaseTM, PrimaseTM, EverlaseTM, EsperaseTM, and KannaseTM (Novo Nordisk A/S), MaxataseTM, axacalTM, MaxapemTM, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, FN3TM, and FN4TM (Genencor International Inc.).
  • Preferred commercially available lipase enzymes include LipolaseTM, Lipolase UltraTM and LipoprimeTM (Novo Nordisk A/S).
  • Preferred commercially available amylases are DuramylTM, TermamylTM,
  • Preferred commercially available cellulases include CelluzymeTM, and CarezymeTM (Novo Nordisk A/S), ClazinaseTM, and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (Kao Corporation).
  • Compounds possessing laccase activity may be any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom, exhibiting laccase activity.
  • Preferred laccase enzymes and/or laccase related enzymes are enzymes of microbial origin.
  • the enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts).
  • Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes,
  • Suitable examples from bacteria include a laccase derivable from a strain of Bacillus.
  • a laccase derived from Coprinus, Myceliophthora, Polyporus, Scytalidium or Rhizoctonia is preferred; in particular a laccase derived from Coprinus cinereus, Myceliophthora thermophila, Polyporus pinsitus, Scytalidium thermophilum or Rhizoctonia solani.
  • the laccase or the laccase related enzyme may furthermore be one which is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding said laccase as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the laccase, in a culture medium under conditions permitting the expression of the laccase enzyme, and recovering the laccase from the culture.
  • LACU Laccase Activity
  • Laccase activity (particularly suitable for Polyporus laccases) may be determined from the oxidation of syringaldazin under aerobic conditions.
  • the violet colour produced is photometered at 530 nm.
  • the analytical conditions are 19 mM syringaldazin, 23 mM acetate buffer, pH 5.5, 30°C, 1 min. reaction time.
  • LACU laccase unit
  • LAMU Laccase Activity
  • Laccase activity may be determined from the oxidation of syringaldazin under aerobic conditions. The violet colour produced is measured at 530 nm. The analytical conditions are 19 mM syringaldazin, 23 mM Tris/maleate buffer, pH 7.5, 30°C, 1 min. reaction time. 1 laccase unit (LAMU) is the amount of enzyme that catalyses the conversion of
  • Peroxidases and Compounds possessing Peroxidase Activity may be any peroxidase enzyme comprised by the enzyme classification (EC 1.11.1.7), or any fragment derived therefrom, exhibiting peroxidase activity.
  • compounds possessing peroxidase activity comprise peroxidase enzymes and peroxidase active fragments derived from cytochromes, haemoglobin or peroxidase enzymes.
  • the peroxidase employed in the composition of the invention is producible by plants (e.g. horseradish or soybean peroxidase) or microorganisms such as fungi or bacteria.
  • Some preferred fungi include strains belonging to the subdivision Deuteromycotina, class Hyphomycetes, e.g., Fusarium, Humicola, Trichoderma, Myrothecium, Ve icillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium or Dreschlera, in particular Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma resii, Myrothecium verrucaria (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago, Ulocladium chartarum, Embellisia alii or Dreschlera halodes.
  • DSM 2672 Fusarium oxysporum
  • Humicola insolens Trichoderma resii
  • Myrothecium verrucaria IFO 6113
  • fungi include strains belonging to the subdivision Basidiomycotina, class Basidiomycetes, e.g., Coprinus, Phanerochaete, Coriolus or Trametes, in particular Coprinus cinereus f. microsporus (IFO 8371), Coprinus macrorhizus,
  • Phanerochaete chrysosporium e.g. NA-12
  • Trametes previously called Polyporus
  • T. versicolor e.g. PR428-A
  • fungi include strains belonging to the subdivision Zygomycotina, class Mycoraceae, e.g., Rhizopus or Mucor, in particular Mucor hiemalis.
  • Some preferred bacteria include strains of the order Actinomycetales, e.g. Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. verticillium.
  • Actinomycetales e.g. Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. verticillium.
  • Bacillus pumilus ATCC 12905
  • Bacillus stearothermophilus Rhodobacter sphaeroides
  • Rhodomonas palustri Streptococcus lactis
  • Pseudomonas purrocinia ATCC 15958
  • Pseudomonas fluorescens NRRL B- 11
  • Further preferred bacteria include strains belonging to Myxococcus, e.g., M. virescens.
  • the peroxidase may furthermore be one which is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding said peroxidase as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the peroxidase, in a culture medium under conditions permitting the expression of the peroxidase and recovering the peroxidase from the culture.
  • a recombinantly produced peroxidase is a peroxidase derived from a
  • Coprinus sp. in particular C. macrorhizus or C. cinereus according to WO 92/16634.
  • POXU peroxidase unit
  • Haloperoxidases such as chromo-, bromo- and/or iodoperoxidases are suitable enzymes in the composition of the invention.
  • Haloperoxidases form a class of enzymes, which are able to oxidize halides (CI-, Br-, I-) in the presence of hydrogen peroxide or a hydrogen peroxide generating system to the corresponding hypohalous acids according to: H 2 O 2 + X- + H+ -> H 2 O + HOX wherein X- is a halide and HOX is a hypohalous acid.
  • haloperoxidases There are three types of haloperoxidases, classified according to their specificity for halide ions: Chloroperoxidases (E.C. 1.11.1.10) which catalyse formation of hypo- chlorit from chloride ions, hypo-bromit from bromide ions and hypo-iodit from iodide ions; Bromoperoxidases which catalyse formation of hypo-bromit from bromide ions and hypo-iodit from iodide ions; and iodoperoxidases (E.G.
  • hypoiodit from iodide ions.
  • Hypoiodit undergoes spontanous disproportionation to iodine and thus iodine is the observed product.
  • hypo-halit compounds may subsequently react with other compounds forming halogenated compounds.
  • Haloperoxidases have been isolated from various organisms: mammals, marine animals, plants, algae, a lichen, fungi and bacteria. It is generally accepted that haloperoxidases are the enzymes responsible for the formation of halogenated compounds in nature, although other enzymes may be involved. Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • a haloperoxidase obtainable from Curvularia in particular C. verruculosa is preferred such as C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70.
  • Curvularia haloperoxidase and recombinant production hereof is described in WO 97/04102.
  • Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.
  • the haloperoxidase is derivable from Curvularia sp., in particular C. verruculosa and C. inaequalis.
  • the haloperoxidase is a vanadium haloperoxidase derivable from a strain of Curvularia inaequalis such as C. inaequalis CBS 102.42 as described in WO 95/27046, e.g. a vanadium haloperoxidase encoded by the DNA sequence of WO 95/27046, figure 2 all incorporated by reference.
  • the haloperoxidase is a vanadium haloperoxidase derivable from a strain selected from Drechslera hartlebii, Dendryphiella salina, Phaeotrichoconis crotalarie and Geniculosporium sp..
  • the vanadium haloperoxidase is more preferably derivable from Drechslera hartlebii (DSM 13444), Dendryphiella salina (DSM 13443), Phaeotrichoconis crotalarie (DSM 13441) and Geniculosporium sp. (DSM 13442).
  • the concentration of the haloperoxidase is typically in the range of 0.01-100 ppm enzyme protein, preferably 0.05-50 ppm enzyme protein, more preferably 0.1-20 ppm enzyme protein, and most preferably 0.5-10 ppm enzyme protein.
  • Microtiter assays are performed by mixing 100 ⁇ l of haloperoxidase sample (about 0.2 ⁇ g/ml) and 100 ⁇ l of 0.3 M sodium phosphate pH 7 buffer - 0.5 M potassium bromide - 0.008% phenol red, adding the solution to 10 ⁇ l of 0.3% H 2 O 2) and measuring the absorption at 595 nm as a function of time.
  • Assays are performed in 0.1 M sodium phosphate or 0.1 M sodium acetate, 50 ⁇ M monochlorodimedone, 10 mM KBr/KCI, and 1 mM H 2 O 2 using a haloperoxidase concentration of about 1 ⁇ g/ml.
  • One HU is defined as 1 micromol of monochlorodimedone chlorinated or brominated per minute at pH 5 and 30°C.
  • the hydrogen peroxide needed for the reaction with the haloperoxidase may be achieved in many different ways: It may be hydrogen peroxide or a hydrogen peroxide precursor, such as, e.g., percarbonate or perborate, or a peroxycarboxylic acid or a salt thereof, or it may be a hydrogen peroxide generating enzyme system, such as, e.g., an oxidase and its substrate.
  • Useful oxidases may be, e.g., a glucose oxidase, a glycerol oxidase or an amino acid oxidase.
  • the hydrogen peroxide source needed for the reaction with the haloperoxidase may be added in a concentration corresponding to a hydrogen peroxide concentration in the range of from 0.01-1000 mM, preferably in the range of from 0.1-100 mM.
  • the halide source needed for the reaction with the haloperoxidase may be achieved in many different ways, e.g., by adding a halide salt: It may be sodium chloride, potassium chloride, sodium bromide, potassium bromide, sodium iodide, or potassium iodide.
  • the concentration of the halide source will typically correspond to 0.01-1000 mM, preferably in the range of from 0.05-500 mM.
  • Enhancing Agents Compounds which, when used in combination with oxidoreductases, are capable of enhancing the antimicrobial effect of the composition of the invention include organic enhancers and inorganic enhancers.
  • organic enhancers for various purposes are known in the art (e.g. from WO 94/12620, WO 94/12621 , WO 95/01626 and WO 96/00179) and may suitably be employed in accordance with the present invention.
  • phenolic compounds alkylsyringates
  • Such enhancers may suitably be present in the composition in an amount between 0.00001-500 mM, preferably 0.0001-5 mM, e.g. 0.001-0.050 mM.
  • Another preferred group of well performing organic enhancers comprises a -
  • B is the same as A, or B is H, or C 1 -C 16 branched or unbranched alkyl wherein said alkyl may contain hydroxy, ether or ester groups, and R2, R3, R4, R5 and R6 are H, OH, NH 2 , COOH, S0 3 H, C C ⁇ 2 branched or unbranched alkyl, acyl, N0 2 , CN, Cl, CF 3 , NOH-CO-phenyl, d-Ce-CO-NOH-A, CO-NOH-A, COR12, phenyl-CO-NOH-
  • N,N'-dihydroxy-N,N'-diphenylterephthalamide decanoic acid-N-hydroxyanilide
  • the enhancer may also be one of the compounds disclosed in WO 96/18770 such as N-hydroxy compounds, in particular aliphatic, cycloaliphatic, heterocyclic or aromatic compounds containing NO-, N(OH)-, or N(OH)(R ⁇ ), especially N-hydroxy benzotriazol (HOBT), Violuric acid, or N-hydroxyacetanilide (HAA).
  • N-hydroxy compounds in particular aliphatic, cycloaliphatic, heterocyclic or aromatic compounds containing NO-, N(OH)-, or N(OH)(R ⁇ ), especially N-hydroxy benzotriazol (HOBT), Violuric acid, or N-hydroxyacetanilide (HAA).
  • HOBT N-hydroxy benzotriazol
  • HAA N-hydroxyacetanilide
  • the enhancer is a compound of the general formula (V):
  • R 1 , R 2 , R 3 , R 4 are individually selected from the group consisting of hydrogen, halogen, hydroxy, formyl, carboxy and salts and esters thereof, amino, nitro, C ⁇ -C ⁇ 2 alkyl, alkoxy, carbonyl(C ⁇ -C- ⁇ 2 alkyl), aryl, in particular phenyl, sulpho, aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and esters thereof, wherein the R 1 , R 2 , R 3 , R 4 may be substituted with R 5 , wherein R 5 represents hydrogen, halogen, hydroxy, formyl, carboxy and salts and esters thereof, amino, nitro, C ⁇ -C ⁇ 2 alkyl, CI-C ⁇ alkoxy, carbonyl(C ⁇ -C ⁇ 2 alkyl), aryl, in particular phenyl, sulpho, aminosulfonyl, carbamoyl,
  • R 1 , R 2 , R 3 , R 4 are individually selected from the group consisting of hydrogen, halogen, hydroxy, formyl, carboxy and salts and esters thereof, amino, nitro, C ⁇ -C ⁇ 2 alkyl, C-i-C ⁇ alkoxy, carbonyl(C ⁇ -C ⁇ 2 alkyl), aryl, in particular phenyl, sulpho, aminosulfonyl, carbamoyl, phosphono, phosphonooxy, and salts and esters thereof, wherein the R 1 , R 2 , R 3 , R 4 may be substituted with R 5 , wherein R 5 represents hydrogen, halogen, hydroxy, formyl, carboxy and salts and esters thereof, amino, nitro, C C 12 alkyl, C ⁇ -C 6 alkoxy, carbonyl(C ⁇ -C ⁇ 2 alkyl), aryl, in particular phenyl, sulpho, aminosulfonyl, carbamoyl,
  • heterocyclic compounds including five-membered nitrogen- containing heterocycles, in particular pyrrol, pyrazole and imidazole and their hydrogenated counterparts (e.g. pyrrolidine) as well as triazoles, such as 1 ,2,4- triazole; six-membered nitrogen-containing heterocycles, in particular mono-, di- and triazinanes (such as piperidine and piperazine), morpholine and their unsaturated counterparts (e.g. pyridine and pyrimidine); and condensed heterocycles containing the above heterocycles as substructures, e.g. indole, benzothiazole, quinoline and benzoazepine.
  • Examples of preferred enhancers from these classes of compounds are pyridine aldoximes; N-hydroxypyrrolidinediones such as N-hydroxysuccinimide and N-hydroxyphthalimide; 3,4-dihydro-3-hydroxybenzo[1 ,2,3]triazine-4-one; formaldoxime trimer (N,N',N"-trihydroxy-1 ,3,5-triazinane); and violuric acid (1 ,3- diazinane-2,4,5,6-tetrone-5-oxime).
  • Still further enhancers which may be applied in the invention include oximes of oxo- and formyl-derivatives of aromatic compounds, such as benzoquinone dioxime and salicylaldoxime (2-hydroxybenzaldehyde oxime), and N-hydroxyamides and N- hydroxyanilides, such as N-hydroxyacetanilide.
  • aromatic compounds such as benzoquinone dioxime and salicylaldoxime (2-hydroxybenzaldehyde oxime)
  • N-hydroxyamides and N- hydroxyanilides such as N-hydroxyacetanilide.
  • Preferred enhancers are selected from the group consisting of 1- hydroxybenzotriazole; 1-hydroxybenzotriazole hydrate; 1-hydroxybenzotriazole sodium salt; 1-hydroxybenzotriazole potassium salt; 1-hydroxybenzotriazole lithium salt; 1-hydroxybenzotriazole ammonium salt; 1-hydroxybenzotriazole calcium salt; 1- hydroxybenzotriazole magnesium salt; and 1-hydroxybenzotriazole-6-sulphonic acid.
  • a particularly preferred enhancer is 1-hydroxybenzotriazole.
  • the enhancer of the invention may be the corresponding N-oxyl free radical to any of the compounds disclosed in WO 96/18770 such as TEMPO (2,2,6,6-tetramethylpiperidinoxyl).
  • the organic enhancers may suitably be present in the paint composition in 5 concentrations from 1 to 1000 ⁇ M, preferably from 5 to 500 ⁇ M.
  • an improved haloperoxidase effect may be obtained using an enhancer, preferably an ammonium enhancer, preferably in combination with a halide enhancer or an organic enhancer.
  • the ammonium enhancer may be o compounds of the formula:
  • R1 and R2 may be identical or different.
  • R1 and R2 may suitably be any of the following groups: hydrogen, halide, sulphate, phenyl, a straight or branched chain alkyl having from 1 to 14 carbon atoms, or a substituted straight or 5 branched alkyl group having from 1 to 14 carbon atoms where the substituent group is located at C-i-Cu and represent any of the following radicals: hydroxy, halogen, formyl, carboxy, carboxy esters, carboxy salts, carbamoyl, sulfo, sulfo esters, sulfo salts, sulfamoyl, nitro, amino, phenyl, C ⁇ -C 5 -alkoxy, carbonyi-Ci-Cs-alkyl, aryl-Ci-C ⁇ -alkyl.
  • R1 and/or R2 includes groups selected from carbamoyl, sulfamoyl, and amino 0 groups these groups may furthermore be unsubstituted or substituted once or twice with a substituent group R3, Where R1 and/or R2 includes a phenyl group it may furthermore be unsubstituted or substituted with one or more substituent groups R3. Where R1 and/or R2 includes groups selected from CrC 5 -alkoxy, carbonyl-CrC 5 - alkyl, and aryl-C-i-Cs-alkyl these groups may be saturated or unsaturated, branched 5 or unbranched, and may furthermore be unsubstituted or substituted with one or more substituent groups R3.
  • R3 represents any of the following groups: halogen, hydroxy, formyl, carboxy, carboxy esters, carboxy salts, carbamoyl, sulfo, sulfo esters, sulfo salts, sulfamoyl, nitro, amino, phenyl, aminoalkyl, piperidino, piperazinyl, pyrrolidin-1-yl, C C 5 -alkyl, CrCs-alkoxy.
  • R3 includes groups selected from 0 carbamoyl, sulfamoyl, and amino these groups may furthermore be unsubstituted or substituted once or twice with hydroxy, C-i-C ⁇ -alkyl, CrCs-alkoxy.
  • R3 includes phenyl this group may furthermore be substituted with one or more of the following groups: halogen, hydroxy, amino, formyl, carboxy, carboxy esters, carboxy salts, carbamoyl, sulfo, sulfo esters, sulfo salts, and sulfamoyl.
  • R3 includes groups selected from C ⁇ -C 5 -alkyl, and Ci-Cs-alkoxy these groups may furthermore be saturated or unsaturated, branched or unbranched, and may furthermore be substituted once or twice with any of the following radicals: halogen, hydroxy, amino, formyl, carboxy, carboxy esters, carboxy salts, carbamoyl, sulfo, sulfo esters, sulfo salts, and sulfamoyl.
  • the ammonium enhancer may be in their cationic form.
  • R1 is hydrogen
  • R1 is hydrogen and R2 is an alcohol (amino alcohol), e.g., ethanol amine.
  • ammonium enhancer is an ammonium salt, i.e. any ammonium salt known in the art: e.g., diammonium sulphate, ammonium chloride, ammonium bromide, or ammonium iodide.
  • the ammonium enhancer may suitably be present in the paint composition of the invention in a concentration corresponding to an ammonium concentration in the range of from 0.01-1000 mM, preferably in the range of from 0.05-500 mM.
  • the present invention provides an antimicrobial composition, comprising an enzymatic component and one or more non-enzymatic biocides.
  • the enzymatic component and the non-enzymatic biocides of the composition may be selected so that a synergistic antimicrobial effect is obtained.
  • the enzymatic component and the non-enzymatic biocides of the composition may be selected so that the number of living cells of E. coli (DSM1576), when incubated 10 min. at 20°C in an aqueous solution containing 50% w/w (preferably 25% w/w, more preferably 10% w/w, most preferably 5% w/w) of the biocide and 0.5 ppm (preferably 0.1 ppm) of the enzymatic component, are reduced at least 5% (preferably at least 10%) more than compared to what is obtained by adding the results of separate incubations with the biocides and the enzymatic component alone, i.e. a simple additive effect.
  • DSM1576 E. coli
  • the enzymatic component and the non-enzymatic biocides of the composition may also be selected so that the outgrowth of E. coli (DSM1576) at 25°C in a microbial growth substrate containing 500 ppm (preferably 250 ppm, more preferably 100 ppm, most preferably 50 ppm) of the biocide and 0.5 ppm (preferably 0.1 ppm) of the enzymatic component, are inhibited at least 5% (preferably at least 10%) longer time than compared to what is obtained by adding the results of separate incubations with the biocides and the enzymatic component alone, i.e. a simple additive effect.
  • E. coli E. coli
  • composition may be formulated as a solid, liquid, gel or paste.
  • all components may be mixed together, e.g., as a powder, a granulate or a gelled product.
  • composition of the invention may further comprise auxiliary agents such as wetting agents, thickening agents, buffer, stabilisers, perfume, colourants, fillers and the like.
  • Useful wetting agents are surfactants, i.e., non-ionic, anionic, amphoteric or zwitterionic surfactants.
  • the composition of the invention may be a concentrated product or a ready-to-use product.
  • the concentrated product is typically diluted with water to provide a medium having an effective antimicrobial activity, applied to the object to be disinfected or preserved, and allowed to react with the microorganisms present.
  • the pH of an aqueous solution of the composition is in the range of from pH 2 to 11 , preferably in the range of from pH 4 to 10, more preferably in the range of from pH 5 to 9, and most preferably in the range of from pH 6 to 8.
  • the present invention provides a method for killing or inhibiting microbial cells comprising treating said microbial cells with the antimicrobial composition of the invention.
  • the microbial cells may be treated with the enzymatic component and the non- enzymatic biocides simultaneously, in sequential treatments or even in discrete treatments separated by other process steps.
  • the invention also encompasses various uses of a composition comprising an enzymatic component and one or more non-enzymatic biocides.
  • Said composition is typically useful at any locus subject to contamination by bacteria, fungi, yeast or algae.
  • loci are in aqueous systems such as cooling water systems, laundry rinse water, oil systems such as cutting oils, lubricants, oil fields and the like, where microorganisms need to be killed or where their growth needs to be controlled.
  • the present invention may also be used in all applications for which known antimicrobial compositions are useful, such as protection of wood, latex, adhesive, glue, paper, cardboard, textile, leather, plastics, caulking, and feed.
  • Other uses include preservation of foods, beverages, cosmetics such as lotions, creams, gels, ointments, soaps, shampoos, conditioners, antiperspirants, deodorants, mouth wash, contact lens products, enzyme formulations, or food ingredients.
  • cosmetics such as lotions, creams, gels, ointments, soaps, shampoos, conditioners, antiperspirants, deodorants, mouth wash, contact lens products, enzyme formulations, or food ingredients.
  • composition used in the method of the invention may by useful as a disinfectant, e.g., in the treatment of acne, infections in the eye or the mouth, skin infections; in antiperspirants or deodorants; in foot bath salts; for cleaning and disinfection of contact lenses, hard surfaces, teeth (oral care), wounds, bruises and the like.
  • a disinfectant e.g., in the treatment of acne, infections in the eye or the mouth, skin infections; in antiperspirants or deodorants; in foot bath salts; for cleaning and disinfection of contact lenses, hard surfaces, teeth (oral care), wounds, bruises and the like.
  • the composition of the present invention is useful for cleaning, disinfecting or inhibiting microbial growth on any hard surface.
  • surfaces which may advantageously be contacted with the composition of the invention are surfaces of process equipment used e.g. dairies, chemical or pharmaceutical process plants, water sanitation systems, oil processing plants, paper pulp processing plants, water treatment plants, and cooling towers.
  • the composition of the invention should be used in an amount, which is effective for cleaning, disinfecting or inhibiting microbial growth on the surface in question.
  • the composition of the invention can advantageously be used in a cleaning-in-place (C.I.P.) system for cleaning of process equipment of any kind.
  • C.I.P. cleaning-in-place
  • the method of the invention may additionally be used for cleaning surfaces and cooking utensils in food processing plants and in any area in which food is prepared or served such as hospitals, nursing homes, restaurants, especially fast food restaurants, delicatessens and the like. It may also be used as an antimicrobial in food products and would be especially useful as a surface antimicrobial in cheeses, fruits and vegetables and food on salad bars. It may also be used as a preservation agent or a disinfection agent in water based paints.
  • composition of the present invention is also useful for microbial control of water lines, and for disinfection of water, in particular for disinfection of industrial water.
  • the antimicrobial composition of the invention 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 the antimicrobial composition of the invention and a surfactant.
  • the detergent additive as well as the detergent composition may comprise one or more other enzymes such as a protease, a lipase, a cutinase, an amylase, a carbohydrase, a cellulase, a pectinase, a mannanase, an arabinase, a galactanase, a xylanase, an oxidase, e.g., a laccase, and/or a peroxidase.
  • the properties of the chosen enzyme(s) should be compatible with the selected detergent, (i.e.
  • 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, DuralaseTM, EsperaseTM, and KannaseTM (Novo Nordisk A/S), MaxataseTM, MaxacalTM, MaxapemTM, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).
  • Suitable 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 407225, 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
  • Amylases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, a-amylases obtained from Bacillus, e.g. a special strain of B. licheniformis, described in more detail in GB 1,296,839.
  • amylases are the variants described in WO 94/02597, WO
  • amylases are DuramylTM, TermamylTM, FungamylTM and
  • 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,
  • cellulases are the alkaline or neutral cellulases having colour care benefits.
  • Examples of such cellulases are cellulases described in EP 0 495 257,
  • Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US
  • Peroxidases/Oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
  • peroxidases examples include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and
  • 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 non- aqueous.
  • 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 H202 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.
  • the detergent may also contain other conventional detergent ingredients such as e.g.
  • fabric conditioners including clays, foam boosters, suds suppressors, anti-corrosion agents, soil-suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, or perfumes.
  • any enzyme in particular the haloperoxidase of the invention, may be added in an amount corresponding to 0.01-100 mg of enzyme protein per liter of wash liqour, preferably 0.05-10 mg of enzyme protein per liter of wash liqour, more preferably 0.1-5 mg of enzyme protein per liter of wash liqour, and most preferably 0.1-1 mg of enzyme protein per liter of wash liqour.
  • the antimicrobial composition of the invention may additionally be incorporated in the detergent formulations disclosed in WO 97/07202 which is hereby incorporated as reference. The present invention is further illustrated in the following examples, which are not in any way intended to limit the scope of the invention as claimed.
  • Curvularia verruculosa recombinant peroxidase is available from Novo Nordisk
  • NOPA V0054 powder detergent is available from Nordisk Detergent A/S, Denmark. Brain Heart Infusion Broth (#CM225) and Tryptone Soya Agar (#CM129) is available from Oxoid, England.
  • the buffers (0.0005 M) used are: pH 5: Homopipes (#6047H, Research Organics, U.S.) pH 6: MES (#M2250, Sigma) pH 7: HEPES (#H3375, Sigma) pH 8: HEPES (#H3375, Sigma) pH 9: HEPES (#H3375, Sigma) + CAPS (#C2632, Sigma) pH 10: CAPS (#C2632, Sigma)
  • CFU/ml Colony Forming Units per ml.
  • Antimicrobial activity may be measured in terms of the number of log reductions.
  • log reduction is defined as a logarithmic reduction of the number of living cells, e.g. 1 log reduction corresponds to a reduction in living cell number of Escherichia coli DSM 1576 or Enterococcus faecalis DSM2570 from Y x 10 x CFU/M (CFU: Colony Forming Units, M: ml or g) to Y x 10 x"1 CFU/M, where X can be 1 , 2, 3, 4, 5, 6, 7, 8, 9, 10 or 11 , and Y can be any number from 0 to 10.
  • the number of living bacteria are to be determined as the number of E. coli or E. faecalis, respectively, which can grow on Tryptone Soya Agar plates at 30°C.
  • epidermidis is grown in Brain Heart Infusion Broth (BHI) at 30°C and diluted in the buffers, respectively to a concentration of approximately 10 6 CFU/ml.
  • BHI Brain Heart Infusion Broth
  • the cell suspensions are incubated with the enzyme/biocide system for 15 min at 40°C.
  • the bactericidal activity is determined by incubation in a Malthus instrument.
  • the detection times measured by the Malthus instrument are converted to CFU/ml by a calibration curve.
  • Either direct or indirect Malthus measurements are used when enumerating total survival cells.
  • the cell metabolism is determined by conductance measurements in the growth substrate.
  • indirect measurements 3 ml of growth medium is transferred to the outer chamber of the indirect Malthus cells, and 0.5 ml of sterile KOH (0.1 M) is transferred to the inner chamber.
  • the cell suspensions are after enzyme treatment transferred to the outer chamber of the Malthus cell. As cells are growing in the outer chamber they produce C0 2 which will dissolve in the KOH in the inner chamber and thereby change the conductance of the KOH.
  • the amount of C0 2 formed by the respiring cells surviving the enzyme treatment is used for estimating the number of viable cells.
  • a detection time (dt) will be recorded.
  • the dt ' s are converted to colony counts by use of a calibration curve relating CFU/ml to dt.
  • Antibacterial activity in detergent of haloperoxidase and biocide The antibacterial activity of Curvularia verruculosa haloperoxidase (0.5 mg/l) and methylparaben (0, 50 and 500 ppm), ethylparaben (0, 50 and 500 ppm), methylchloroisothiazolinone (0, 15 and 30 ppm) or benzisothiazolinone (0, 50 and 500 ppm) is tested in NOPA V0054 powder detergent. pH of the detergent is measured as approximately 9.9, antimicrobial activity is evaluated in the detergent at pH 9.9, 9, and 8 where pH is adjusted.
  • Antimicrobial activity of the enzyme/biocide system is determined using KBr (2 and 4 mM) as halide, (NH ) 2 S0 4 (0 and 2 mM) as enhancing agent, and H 2 0 2 (0.5 mM) as oxidizing agent.
  • Microbial cells Escherichia coli DSM 1576 are grown over night in Tryptone

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Abstract

L'invention concerne une composition antimicrobienne comprenant un composant enzymatique et un ou plusieurs biocides non enzymatiques, un procédé servant à tuer ou inhiber des cellules microbiennes, comprenant un traitement avec la composition antimicrobienne, et une composition détergente comprenant la composition antimicrobienne. Grâce à la composition selon l'invention, on obtient un effet antimicrobien amélioré.
PCT/DK2001/000454 2000-07-21 2001-06-29 Compositions antimicrobiennes WO2002008377A1 (fr)

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Cited By (21)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE102005001990A1 (de) * 2005-01-15 2006-07-20 Clariant Gmbh Wässrige fungizide Zubereitungen
WO2006094975A2 (fr) * 2005-03-10 2006-09-14 Novozymes A/S Procedes et compositions sporicides
WO2006133523A2 (fr) * 2005-06-13 2006-12-21 Flen Pharma N.V. Compositions de peroxydase antimicrobiennes ameliorees
WO2007100514A1 (fr) * 2006-02-22 2007-09-07 Buckman Laboratories International, Inc. Traitement par halogénoperoxydase pour contrôler les algues
WO2007104316A1 (fr) * 2006-03-16 2007-09-20 Aalborg Universitet Enrobage de matières glucidiques
WO2009053438A1 (fr) * 2007-10-23 2009-04-30 Novozymes A/S Procédés pour tuer des spores et désinfecter ou stériliser des dispositifs
WO2009134118A1 (fr) * 2008-04-28 2009-11-05 Enhold B.V. Additif antimicrobien pour une utilisation dans l’eau d’un vase à fleurs
WO2010046142A2 (fr) * 2008-10-23 2010-04-29 Getinge Disinfection Ab Procédé d’obtention d’un niveau élevé de désinfection dans un autolaveur et autolaveur
WO2010122100A1 (fr) * 2009-04-22 2010-10-28 Novozymes A/S Procédés pour tuer ou inhiber la croissance de mycobactéries
DE102010013272A1 (de) 2010-03-29 2011-09-29 Beiersdorf Ag Mikrobiologisch stabile anwendungsfreundliche Zubereitung mit Verdickern
DE102010013275A1 (de) 2010-03-29 2011-09-29 Beiersdorf Ag Mikrobiologisch stabile anwendungsfreundliche W/O-Zubereitungen
DE102010013277A1 (de) 2010-03-29 2011-09-29 Beiersdorf Ag Mikrobiologisch stabile anwendungsfreundliche Zubereitung mit degradationsanfälligen Wirkstoffen
WO2011124245A2 (fr) 2010-03-29 2011-10-13 Beiersdorf Ag Préparations microbiologiquement stables et d'utilisation aisée, contenant des principes actifs anioniques ou cationiques
WO2011124241A2 (fr) 2010-03-29 2011-10-13 Beiersdorf Ag Préparations microbiologiquement stables d'utilisation aisée
WO2016057788A1 (fr) * 2014-10-10 2016-04-14 Rochal Industries, Llc Compositions et kits pour le débridement enzymatique et leurs procédés d'utilisation
JP2017001980A (ja) * 2015-06-09 2017-01-05 株式会社リコー 充填用抗菌性水溶液、顔料分散液の製造装置、顔料分散液の製造方法及びインクジェットインク用顔料分散液
US10238719B2 (en) 2014-10-10 2019-03-26 Rochal Industries, Llc Compositions and kits for enzymatic debridement and methods of using the same
CN110409221A (zh) * 2011-09-30 2019-11-05 凯米拉公司 纸浆、纸或板制造方法中淀粉降解的防止
WO2020229202A1 (fr) 2019-05-15 2020-11-19 Purac Biochem B.V. Mélange de lactylates pour système conservateur/antimicrobien
DE102021114332A1 (de) 2021-06-02 2022-12-08 Henkel Ag & Co. Kgaa Stabilisierung von enzymen durch phenoxyethanol
JP7624320B2 (ja) 2021-02-04 2025-01-30 株式会社メニコン 除藻剤及び除藻方法

Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0425016A2 (fr) * 1989-10-27 1991-05-02 The Procter & Gamble Company Méthode antimicrobienne et formulation employant l'endoglycosidase du type II et agent antimicrobien
US5227161A (en) * 1988-09-06 1993-07-13 Symbollon Corporation Method to clean and disinfect pathogens on the epidermis by applying a composition containing peroxidase, iodide compound and surfactant
US5503766A (en) * 1993-04-06 1996-04-02 Natural Chemistry, Inc. Enzymatic solutions containing saponins and stabilizers
WO1999008531A1 (fr) * 1997-08-14 1999-02-25 Novo Nordisk A/S Composition antibicrobienne contenant une haloperoxydase, une source de peroxyde d'hydrogene, une source d'halogenure, et une source d'ammonium
US5998342A (en) * 1998-08-26 1999-12-07 Cottrell International, Llc Foaming enzyme spray cleaning composition and method of delivery
WO2000004138A1 (fr) * 1998-07-17 2000-01-27 Novozymes A/S Conjugue polypeptide-polymeres a efficacite de lavage amelioree

Patent Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5227161A (en) * 1988-09-06 1993-07-13 Symbollon Corporation Method to clean and disinfect pathogens on the epidermis by applying a composition containing peroxidase, iodide compound and surfactant
EP0425016A2 (fr) * 1989-10-27 1991-05-02 The Procter & Gamble Company Méthode antimicrobienne et formulation employant l'endoglycosidase du type II et agent antimicrobien
US5503766A (en) * 1993-04-06 1996-04-02 Natural Chemistry, Inc. Enzymatic solutions containing saponins and stabilizers
WO1999008531A1 (fr) * 1997-08-14 1999-02-25 Novo Nordisk A/S Composition antibicrobienne contenant une haloperoxydase, une source de peroxyde d'hydrogene, une source d'halogenure, et une source d'ammonium
WO2000004138A1 (fr) * 1998-07-17 2000-01-27 Novozymes A/S Conjugue polypeptide-polymeres a efficacite de lavage amelioree
US5998342A (en) * 1998-08-26 1999-12-07 Cottrell International, Llc Foaming enzyme spray cleaning composition and method of delivery

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WO2006074882A1 (fr) * 2005-01-15 2006-07-20 Clariant Produkte (Deutschland) Gmbh Preparations fongicides aqueuses
DE102005001990A1 (de) * 2005-01-15 2006-07-20 Clariant Gmbh Wässrige fungizide Zubereitungen
WO2006094975A2 (fr) * 2005-03-10 2006-09-14 Novozymes A/S Procedes et compositions sporicides
WO2006094975A3 (fr) * 2005-03-10 2007-05-10 Novozymes As Procedes et compositions sporicides
US8679526B2 (en) 2005-06-13 2014-03-25 Flen Pharma N.V. Antimicrobial peroxidase compositions
WO2006133523A2 (fr) * 2005-06-13 2006-12-21 Flen Pharma N.V. Compositions de peroxydase antimicrobiennes ameliorees
WO2006133523A3 (fr) * 2005-06-13 2007-07-19 Flen Pharma N V Compositions de peroxydase antimicrobiennes ameliorees
WO2007100514A1 (fr) * 2006-02-22 2007-09-07 Buckman Laboratories International, Inc. Traitement par halogénoperoxydase pour contrôler les algues
WO2007104316A1 (fr) * 2006-03-16 2007-09-20 Aalborg Universitet Enrobage de matières glucidiques
WO2009053438A1 (fr) * 2007-10-23 2009-04-30 Novozymes A/S Procédés pour tuer des spores et désinfecter ou stériliser des dispositifs
CN101827527A (zh) * 2007-10-23 2010-09-08 诺维信公司 用于杀死孢子和装置消毒或灭菌的方法
JP2011500761A (ja) * 2007-10-23 2011-01-06 ノボザイムス アクティーゼルスカブ 胞子を死滅させるための、及び機器を消毒又は滅菌するための方法
US10519049B2 (en) 2008-04-28 2019-12-31 Enhold B.V. Anti-microbial additive for use in flower vase water
US9963364B2 (en) 2008-04-28 2018-05-08 Enhold B.V. Anti-microbial additive for use in flower vase water
AP2979A (en) * 2008-04-28 2014-09-30 Enhold Bv Anti-microbial additive for use in flower vase water
WO2009134118A1 (fr) * 2008-04-28 2009-11-05 Enhold B.V. Additif antimicrobien pour une utilisation dans l’eau d’un vase à fleurs
WO2010046142A2 (fr) * 2008-10-23 2010-04-29 Getinge Disinfection Ab Procédé d’obtention d’un niveau élevé de désinfection dans un autolaveur et autolaveur
WO2010046142A3 (fr) * 2008-10-23 2010-11-18 Getinge Disinfection Ab Procédé d’obtention d’un niveau élevé de désinfection dans un autolaveur et autolaveur
WO2010122100A1 (fr) * 2009-04-22 2010-10-28 Novozymes A/S Procédés pour tuer ou inhiber la croissance de mycobactéries
WO2011124242A2 (fr) 2010-03-29 2011-10-13 Beiersdorf Ag Préparations eau/huile microbiologiquement stables
WO2011124243A2 (fr) 2010-03-29 2011-10-13 Beiersdorf Ag Préparation microbiologiquement stable et d'utilisation aisée, contenant des épaississants
WO2011124241A2 (fr) 2010-03-29 2011-10-13 Beiersdorf Ag Préparations microbiologiquement stables d'utilisation aisée
WO2011124244A2 (fr) 2010-03-29 2011-10-13 Beiersdorf Ag Préparation microbiologiquement stable et d'utilisation aisée contenant des principes actifs sensibles à la dégradation
DE102010013276A1 (de) 2010-03-29 2011-11-17 Beiersdorf Ag Mikrobiologisch stabile anwendungsfreundliche Zubereitungen mit anionischen oder kationischen Wirkstoffen in Kombination
DE102010013274A1 (de) 2010-03-29 2011-11-17 Beiersdorf Ag Mikrobiologisch stabile anwendungsfreundliche Zubereitungen
WO2011124245A2 (fr) 2010-03-29 2011-10-13 Beiersdorf Ag Préparations microbiologiquement stables et d'utilisation aisée, contenant des principes actifs anioniques ou cationiques
DE102010013277A1 (de) 2010-03-29 2011-09-29 Beiersdorf Ag Mikrobiologisch stabile anwendungsfreundliche Zubereitung mit degradationsanfälligen Wirkstoffen
DE102010013272A1 (de) 2010-03-29 2011-09-29 Beiersdorf Ag Mikrobiologisch stabile anwendungsfreundliche Zubereitung mit Verdickern
DE102010013275A1 (de) 2010-03-29 2011-09-29 Beiersdorf Ag Mikrobiologisch stabile anwendungsfreundliche W/O-Zubereitungen
CN110409221A (zh) * 2011-09-30 2019-11-05 凯米拉公司 纸浆、纸或板制造方法中淀粉降解的防止
CN107106663A (zh) * 2014-10-10 2017-08-29 罗查尔工业有限责任公司 用于酶清创的组合物和试剂盒及其使用方法
US9592280B2 (en) 2014-10-10 2017-03-14 Rochal Industries Llc Compositions and kits for enzymatic debridement and methods of using the same
US10238719B2 (en) 2014-10-10 2019-03-26 Rochal Industries, Llc Compositions and kits for enzymatic debridement and methods of using the same
WO2016057788A1 (fr) * 2014-10-10 2016-04-14 Rochal Industries, Llc Compositions et kits pour le débridement enzymatique et leurs procédés d'utilisation
AU2015330888B2 (en) * 2014-10-10 2021-04-01 Rochal Technologies Llc Compositions and kits for enzymatic debridement and methods of using the same
CN107106663B (zh) * 2014-10-10 2022-12-06 罗查尔科技有限责任公司 用于酶清创的组合物和试剂盒及其使用方法
JP2017001980A (ja) * 2015-06-09 2017-01-05 株式会社リコー 充填用抗菌性水溶液、顔料分散液の製造装置、顔料分散液の製造方法及びインクジェットインク用顔料分散液
WO2020229202A1 (fr) 2019-05-15 2020-11-19 Purac Biochem B.V. Mélange de lactylates pour système conservateur/antimicrobien
JP7624320B2 (ja) 2021-02-04 2025-01-30 株式会社メニコン 除藻剤及び除藻方法
DE102021114332A1 (de) 2021-06-02 2022-12-08 Henkel Ag & Co. Kgaa Stabilisierung von enzymen durch phenoxyethanol

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