MXPA00001369A - Antimicrobial composition containing a haloperoxidase, a hydrogen peroxide source, a halide source and an ammonium source - Google Patents
Antimicrobial composition containing a haloperoxidase, a hydrogen peroxide source, a halide source and an ammonium sourceInfo
- Publication number
- MXPA00001369A MXPA00001369A MXPA/A/2000/001369A MXPA00001369A MXPA00001369A MX PA00001369 A MXPA00001369 A MX PA00001369A MX PA00001369 A MXPA00001369 A MX PA00001369A MX PA00001369 A MXPA00001369 A MX PA00001369A
- Authority
- MX
- Mexico
- Prior art keywords
- composition according
- source
- haloperoxidase
- ammonium
- composition
- Prior art date
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 75
- MHAJPDPJQMAIIY-UHFFFAOYSA-N hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 title claims abstract description 67
- QGZKDVFQNNGYKY-UHFFFAOYSA-O ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 title claims abstract description 24
- 150000004820 halides Chemical class 0.000 title claims abstract description 23
- 230000000845 anti-microbial Effects 0.000 title claims abstract description 21
- 230000002255 enzymatic Effects 0.000 claims abstract description 6
- 150000003863 ammonium salts Chemical class 0.000 claims abstract description 5
- AVXURJPOCDRRFD-UHFFFAOYSA-N hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 claims abstract description 3
- 239000011780 sodium chloride Substances 0.000 claims description 35
- -1 nitro, amino, phenyl Chemical group 0.000 claims description 33
- 102000004190 Enzymes Human genes 0.000 claims description 26
- 108090000790 Enzymes Proteins 0.000 claims description 26
- FAPWRFPIFSIZLT-UHFFFAOYSA-M sodium chloride Chemical group [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 22
- 150000003839 salts Chemical class 0.000 claims description 21
- 125000001424 substituent group Chemical group 0.000 claims description 18
- 150000002148 esters Chemical class 0.000 claims description 16
- 230000000249 desinfective Effects 0.000 claims description 15
- 229940088598 Enzyme Drugs 0.000 claims description 14
- 238000004140 cleaning Methods 0.000 claims description 14
- 230000002401 inhibitory effect Effects 0.000 claims description 14
- 230000000813 microbial Effects 0.000 claims description 14
- 102000003992 Peroxidases Human genes 0.000 claims description 12
- 108090000437 Peroxidases Proteins 0.000 claims description 12
- 125000004397 aminosulfonyl group Chemical group NS(=O)(=O)* 0.000 claims description 12
- 125000003917 carbamoyl group Chemical group [H]N([H])C(*)=O 0.000 claims description 12
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 12
- CPELXLSAUQHCOX-UHFFFAOYSA-M bromide Chemical compound [Br-] CPELXLSAUQHCOX-UHFFFAOYSA-M 0.000 claims description 10
- 235000013305 food Nutrition 0.000 claims description 10
- 241000223208 Curvularia Species 0.000 claims description 9
- NLKNQRATVPKPDG-UHFFFAOYSA-M Potassium iodide Chemical compound [K+].[I-] NLKNQRATVPKPDG-UHFFFAOYSA-M 0.000 claims description 9
- 229940072417 Peroxidase Drugs 0.000 claims description 8
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims description 8
- 239000002537 cosmetic Substances 0.000 claims description 8
- 229910052736 halogen Inorganic materials 0.000 claims description 8
- 150000002367 halogens Chemical class 0.000 claims description 8
- 244000005700 microbiome Species 0.000 claims description 8
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 claims description 8
- IOLCXVTUBQKXJR-UHFFFAOYSA-M Potassium bromide Chemical compound [K+].[Br-] IOLCXVTUBQKXJR-UHFFFAOYSA-M 0.000 claims description 7
- 238000004659 sterilization and disinfection Methods 0.000 claims description 7
- 241000371662 Curvularia verruculosa Species 0.000 claims description 6
- FVAUCKIRQBBSSJ-UHFFFAOYSA-M Sodium iodide Chemical compound [Na+].[I-] FVAUCKIRQBBSSJ-UHFFFAOYSA-M 0.000 claims description 6
- 238000000034 method Methods 0.000 claims description 6
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 6
- 241000894006 Bacteria Species 0.000 claims description 5
- 210000001508 Eye Anatomy 0.000 claims description 5
- 241000233866 Fungi Species 0.000 claims description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-M chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 claims description 5
- 238000005406 washing Methods 0.000 claims description 5
- YDRWXKNFHCZTJF-UHFFFAOYSA-N 2-(3,4-dimethoxyphenyl)-N-methylethanamine;hydroiodide Chemical compound [I-].C[NH2+]CCC1=CC=C(OC)C(OC)=C1 YDRWXKNFHCZTJF-UHFFFAOYSA-N 0.000 claims description 4
- SWLVFNYSXGMGBS-UHFFFAOYSA-N Ammonium bromide Chemical compound [NH4+].[Br-] SWLVFNYSXGMGBS-UHFFFAOYSA-N 0.000 claims description 4
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonium chloride Substances [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 claims description 4
- BFNBIHQBYMNNAN-UHFFFAOYSA-N Ammonium sulfate Chemical group N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 4
- JHJLBTNAGRQEKS-UHFFFAOYSA-M Sodium bromide Chemical compound [Na+].[Br-] JHJLBTNAGRQEKS-UHFFFAOYSA-M 0.000 claims description 4
- 125000003545 alkoxy group Chemical group 0.000 claims description 4
- 125000000217 alkyl group Chemical group 0.000 claims description 4
- 125000003277 amino group Chemical group 0.000 claims description 4
- 229940077484 ammonium bromide Drugs 0.000 claims description 4
- 235000019270 ammonium chloride Nutrition 0.000 claims description 4
- 229960001040 ammonium chloride Drugs 0.000 claims description 4
- 229940107816 ammonium iodide Drugs 0.000 claims description 4
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 4
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 4
- 125000004432 carbon atoms Chemical group C* 0.000 claims description 4
- 239000002781 deodorant agent Substances 0.000 claims description 4
- 229910052739 hydrogen Inorganic materials 0.000 claims description 4
- 239000001257 hydrogen Substances 0.000 claims description 4
- QDHHCQZDFGDHMP-UHFFFAOYSA-N monochloramine Chemical compound ClN QDHHCQZDFGDHMP-UHFFFAOYSA-N 0.000 claims description 4
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 claims description 4
- 241000195493 Cryptophyta Species 0.000 claims description 3
- 210000000214 Mouth Anatomy 0.000 claims description 3
- 230000001166 anti-perspirant Effects 0.000 claims description 3
- 239000003213 antiperspirant Substances 0.000 claims description 3
- 238000001816 cooling Methods 0.000 claims description 3
- 235000013365 dairy product Nutrition 0.000 claims description 3
- 239000002674 ointment Substances 0.000 claims description 3
- 239000000126 substance Substances 0.000 claims description 3
- 229910052720 vanadium Inorganic materials 0.000 claims description 3
- LEONUFNNVUYDNQ-UHFFFAOYSA-N vanadium(0) Chemical compound [V] LEONUFNNVUYDNQ-UHFFFAOYSA-N 0.000 claims description 3
- 125000004214 1-pyrrolidinyl group Chemical group [H]C1([H])N(*)C([H])([H])C([H])([H])C1([H])[H] 0.000 claims description 2
- 241001465180 Botrytis Species 0.000 claims description 2
- 241000589516 Pseudomonas Species 0.000 claims description 2
- 229940083599 Sodium Iodide Drugs 0.000 claims description 2
- 241000187747 Streptomyces Species 0.000 claims description 2
- 241000266300 Ulocladium Species 0.000 claims description 2
- 125000004103 aminoalkyl group Chemical group 0.000 claims description 2
- 239000006071 cream Substances 0.000 claims description 2
- 125000002485 formyl group Chemical group [H]C(*)=O 0.000 claims description 2
- 239000008187 granular material Substances 0.000 claims description 2
- 125000004435 hydrogen atoms Chemical class [H]* 0.000 claims description 2
- 239000007788 liquid Substances 0.000 claims description 2
- 239000006210 lotion Substances 0.000 claims description 2
- SCKXCAADGDQQCS-UHFFFAOYSA-N performic acid Chemical compound OOC=O SCKXCAADGDQQCS-UHFFFAOYSA-N 0.000 claims description 2
- 239000001103 potassium chloride Substances 0.000 claims description 2
- 235000011164 potassium chloride Nutrition 0.000 claims description 2
- OZAIFHULBGXAKX-UHFFFAOYSA-N precursor Substances N#CC(C)(C)N=NC(C)(C)C#N OZAIFHULBGXAKX-UHFFFAOYSA-N 0.000 claims description 2
- 238000002791 soaking Methods 0.000 claims description 2
- 229940075581 sodium bromide Drugs 0.000 claims description 2
- 235000009518 sodium iodide Nutrition 0.000 claims description 2
- 125000000547 substituted alkyl group Chemical group 0.000 claims description 2
- QAOWNCQODCNURD-UHFFFAOYSA-L sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 claims description 2
- 125000002887 hydroxy group Chemical group [H]O* 0.000 claims 2
- 241001465183 Drechslera Species 0.000 claims 1
- 230000002195 synergetic Effects 0.000 abstract description 6
- 210000004027 cells Anatomy 0.000 description 31
- 230000000844 anti-bacterial Effects 0.000 description 29
- 241000196324 Embryophyta Species 0.000 description 8
- 241000191963 Staphylococcus epidermidis Species 0.000 description 8
- HZAXFHJVJLSVMW-UHFFFAOYSA-N ethanolamine Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 7
- 108020005203 Oxidases Proteins 0.000 description 6
- 229940037645 Staphylococcus epidermidis Drugs 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 6
- 239000003795 chemical substances by application Substances 0.000 description 6
- KWYUFKZDYYNOTN-UHFFFAOYSA-M potassium hydroxide Inorganic materials [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 6
- 230000002538 fungal Effects 0.000 description 5
- 230000001590 oxidative Effects 0.000 description 5
- 238000004321 preservation Methods 0.000 description 5
- 108010035722 EC 1.11.1.10 Proteins 0.000 description 4
- 210000004400 Mucous Membrane Anatomy 0.000 description 4
- 210000003491 Skin Anatomy 0.000 description 4
- 210000000515 Tooth Anatomy 0.000 description 4
- 239000004599 antimicrobial Substances 0.000 description 4
- 230000001580 bacterial Effects 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 200000000019 wound Diseases 0.000 description 4
- SXGZJKUKBWWHRA-UHFFFAOYSA-N 2-(N-morpholino)ethanesulfonic acid Chemical compound [O-]S(=O)(=O)CC[NH+]1CCOCC1 SXGZJKUKBWWHRA-UHFFFAOYSA-N 0.000 description 3
- 108010036012 Iodide Peroxidase Proteins 0.000 description 3
- 102000011845 Iodide Peroxidase Human genes 0.000 description 3
- 239000007987 MES buffer Substances 0.000 description 3
- 238000004164 analytical calibration Methods 0.000 description 3
- 235000013361 beverage Nutrition 0.000 description 3
- 238000011088 calibration curve Methods 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 230000000875 corresponding Effects 0.000 description 3
- 235000012041 food component Nutrition 0.000 description 3
- 239000005417 food ingredient Substances 0.000 description 3
- 230000001965 increased Effects 0.000 description 3
- XMBWDFGMSWQBCA-UHFFFAOYSA-M iodide Chemical compound [I-] XMBWDFGMSWQBCA-UHFFFAOYSA-M 0.000 description 3
- 239000003973 paint Substances 0.000 description 3
- 229940057428 LACTOPEROXIDASE Drugs 0.000 description 2
- 108010023244 Lactoperoxidase Proteins 0.000 description 2
- 102000028880 Lactoperoxidase Human genes 0.000 description 2
- 108090000235 Myeloperoxidases Proteins 0.000 description 2
- 102000003896 Myeloperoxidases Human genes 0.000 description 2
- 101700052286 PRXV Proteins 0.000 description 2
- 229940055023 Pseudomonas aeruginosa Drugs 0.000 description 2
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 2
- 210000003296 Saliva Anatomy 0.000 description 2
- 230000003385 bacteriostatic Effects 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M buffer Substances [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
- 230000000855 fungicidal Effects 0.000 description 2
- 230000001408 fungistatic Effects 0.000 description 2
- 125000004356 hydroxy functional group Chemical group O* 0.000 description 2
- 239000008235 industrial water Substances 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 150000002978 peroxides Chemical class 0.000 description 2
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 2
- 229910052700 potassium Inorganic materials 0.000 description 2
- 239000011591 potassium Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 230000003253 viricidal Effects 0.000 description 2
- 239000000080 wetting agent Substances 0.000 description 2
- 206010000496 Acne Diseases 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 229940025131 Amylases Drugs 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 241000866604 Burkholderia pyrrocinia Species 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 210000003298 Dental Enamel Anatomy 0.000 description 1
- 108010015776 EC 1.1.3.4 Proteins 0.000 description 1
- 108010073997 EC 1.11.1.18 Proteins 0.000 description 1
- 239000004129 EU approved improving agent Substances 0.000 description 1
- 210000003979 Eosinophils Anatomy 0.000 description 1
- 229940116332 GLUCOSE OXIDASE Drugs 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 108050006227 Haem peroxidases Proteins 0.000 description 1
- 241000186984 Kitasatospora aureofaciens Species 0.000 description 1
- 108010029541 Laccase Proteins 0.000 description 1
- 240000008415 Lactuca sativa Species 0.000 description 1
- 241000222118 Leptoxyphium fumago Species 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 240000002129 Malva sylvestris Species 0.000 description 1
- 235000006770 Malva sylvestris Nutrition 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 210000004379 Membranes Anatomy 0.000 description 1
- 230000036740 Metabolism Effects 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 235000010703 Modiola caroliniana Nutrition 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 108091005771 Peptidases Proteins 0.000 description 1
- 102000035443 Peptidases Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 229920001131 Pulp (paper) Polymers 0.000 description 1
- PKIKBRRQNSHDAV-UHFFFAOYSA-N S(=O)(=O)([O-])[O-].[I-].[NH4+].[NH4+].[NH4+] Chemical compound S(=O)(=O)([O-])[O-].[I-].[NH4+].[NH4+].[NH4+] PKIKBRRQNSHDAV-UHFFFAOYSA-N 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 206010040872 Skin infection Diseases 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 101700006119 XYL1 Proteins 0.000 description 1
- 101700047052 XYLA Proteins 0.000 description 1
- 101700051122 XYLD Proteins 0.000 description 1
- 101700065756 XYN4 Proteins 0.000 description 1
- 101700001256 Xyn Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 125000003158 alcohol group Chemical group 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 150000003868 ammonium compounds Chemical class 0.000 description 1
- 239000002280 amphoteric surfactant Substances 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 230000003110 anti-inflammatory Effects 0.000 description 1
- 239000003899 bactericide agent Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 108010089934 carbohydrase Proteins 0.000 description 1
- 239000011111 cardboard Substances 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 229910010293 ceramic material Inorganic materials 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 239000003086 colorant Substances 0.000 description 1
- 239000004567 concrete Substances 0.000 description 1
- 108010005400 cutinase Proteins 0.000 description 1
- 239000000551 dentifrice Substances 0.000 description 1
- 239000000645 desinfectant Substances 0.000 description 1
- GFEYTWVSRDLPLE-UHFFFAOYSA-L dihydrogenvanadate Chemical compound O[V](O)([O-])=O GFEYTWVSRDLPLE-UHFFFAOYSA-L 0.000 description 1
- 201000009910 diseases by infectious agent Diseases 0.000 description 1
- 230000002708 enhancing Effects 0.000 description 1
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- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 108010090622 glycerol oxidase Proteins 0.000 description 1
- 239000001963 growth media Substances 0.000 description 1
- 150000002431 hydrogen Chemical class 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- PMRPLIMEJYCXCT-UHFFFAOYSA-N hydrogen peroxide;lead Chemical compound [Pb].OO PMRPLIMEJYCXCT-UHFFFAOYSA-N 0.000 description 1
- 230000000415 inactivating Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 229910052740 iodine Inorganic materials 0.000 description 1
- 239000011630 iodine Substances 0.000 description 1
- 230000001665 lethal Effects 0.000 description 1
- 108090001060 lipase Proteins 0.000 description 1
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- PMZURENOXWZQFD-UHFFFAOYSA-L na2so4 Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
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- PNIJRIIGBGFYHF-UHFFFAOYSA-N perborate(2-) Chemical compound O[B-]1(O)OO[B-](O)(O)OO1 PNIJRIIGBGFYHF-UHFFFAOYSA-N 0.000 description 1
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- 159000000001 potassium salts Chemical class 0.000 description 1
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- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
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- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- MWNQXXOSWHCCOZ-UHFFFAOYSA-L sodium;oxido carbonate Chemical compound [Na+].[O-]OC([O-])=O MWNQXXOSWHCCOZ-UHFFFAOYSA-L 0.000 description 1
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Abstract
An enzymatic antimicrobial composition comprising a haloperoxidase, a hydrogen peroxide source, a halide source, and an ammonium source, in particular an ammonium salt or an aminoalcohol, in which there is a hitherto unknown synergistic effect between the halide and the ammonium source.
Description
ANTIMICROBIAL COMPOSITION CONTAINING ONE. HAL0PER0XIDA5A, ONE SOURCE OF HYDROGEN PEROXIDE, ONE
SOURCE OF HALURO AND A SOURCE OF .AMONIO
Field of the Invention
The present invention relates to a very effective enzymatic composition, capable of killing or inhibiting microbial cells or microorganisms, more specifically microbial cells or microorganisms present in clothes for washing, on hard surfaces, in water systems, on the skin, teeth or mucous membranes; and to preserve food products, cosmetics, paints, coatings, etc.
Background of the Invention
Various enzymatic antimicrobial compositions are already known in the art. For example, WO 94/04127 discloses stabilized dentifrice compositions which are capable of producing effective anti-microbial concentrations of hypothiocyanite ions. The compositions contain an oxidoreductase capable of producing hydrogen peroxide Ref.032548 and a peroxidase enzyme capable of oxidizing thiocyanate ions, which are normally present in saliva, to antimicrobial hypothiocyanite ions. Suitable peroxidases include lactoperoxidase, myeloperoxidase, peroxidase and chloroperoxidase of saliva. EP-A-0 500 387 discloses enzymatic antimicrobial compositions comprising a haloperoxidase, for example, myeloperoxidase, eosinophil oxidase, lactoperoxidase and chloroperoxidase, which bind electively to, and inhibit the growth of target or target microorganisms. in the presence of peroxide and halide. WO 95/27046 describes an antimicrobial composition comprising a vanadium chloroperoxidase, halide ions, and hydrogen peroxide or a hydrogen peroxide generating agent. WO 96/38548 describes an antimicrobial composition comprising a haloperoxidase, a halide ion, a peroxide generating agent and an amino acid type. The object of the present invention is to provide a composition for killing or inhibiting microbial cells, i.e., for disinfection or preservation, which is easy to use and an effective alternative for compositions and methods of disinfection and preservation.
Brief Description of the Invention
Surprisingly, it has been found that the combined action of a haloperoxidase, a source of hydrogen peroxide, a source of halide and a source of ammonium, leads to a synergistic antimicrobial effect hitherto unknown. Accordingly, based on these findings, the present invention provides, in a first aspect, an enzymatic antimicrobial composition comprising a haloperoxidase, a source of hydrogen peroxide, a halide source and an ammonium source wherein the composition leads to an antimicrobial effect hitherto unknown. The composition of the invention is useful as the antimicrobial ingredient wherever such an ingredient is necessary, for example, for the preservation of foods, beverages, cosmetics, deodorants, contact lens products, food ingredients or enzyme compositions; as a disinfectant for use, for example, on the skin of a human or animal, the hair, the oral cavity, the mucous membranes, the wounds, the hit parts or in the eye; to kill microbial cells in clothes to wash; and for incorporation into cleaning compositions or disinfectants for cleaning a hard surface, for water treatment, or for disinfection. Accordingly, in the further aspects, the present invention provides a method of inhibiting the microorganisms present in laundry, wherein the laundry is treated with a soaking, washing or rinsing liquor comprising this composition; a method of inhibiting microbial growth on a hard surface, wherein the surface is contacted with this composition; a method of inhibition of microbial cells present in industrial water lines; and a method of killing the microbial cells present on the skin of a human or animal, the mucous membranes, the teeth, the wounds, the hit parts or in the eyes or for the inhibition of the growth thereof, where the cells that are going to be exterminated or inhibited on the skin, the mucous membrane, the teeth, the wounds or the hit parts are / are in contact with this composition.
Brief Description of the Drawings
The present invention is further illustrated by reference to the accompanying drawings, in which: Figure 1 shows a calibration curve for the growth of Pseudomonas aeruginosa ATCC 10146 in TSB at 25 ° C; see Example 1. Figure 2 shows a graph of the response surface for antibacterial activity against Staphylococcus epidermidis; when sodium chloride and / or ammonium are added to the reaction medium; see Example 1. Figure 3 shows the bactericidal activity of Curvularia haloperoxidase combined with ammonium iodide sulfate (: Kl and (NH4) 2S04; Kl); see example 2. Figure 4 shows the bactericidal activity of the haloperoxidase Curvularia combined with the bromide and ammonium sulfate; (: KBr and (NH4) 2S04;; KBr); see Example 2. Figure 5 shows the bactericidal activity of the Curvularia haloperoxidase (rCvP) combined with chloride and ethanolamine; see Example 4.
Detailed description of the invention
In the context of the present invention the term "antimicrobial" is proposed to mean that there is a bactericidal effect and / or a bacteriostatic effect and / or a fungicidal effect and / or a fungistatic effect and / or a virucidal effect, in where. The term "bactericide" is going to be understood as capable of killing bacterial cells. The term "bacteriostatic" is going to be understood as capable of inhibiting bacterial growth, ie inhibiting the growth of bacterial cells. The term "fungicide" is going to be understood as capable of exterminating fungal cells. The term "fungistatic" is going to be understood as capable of inhibiting fungal growth, ie inhibiting the growth of fungal cells. The term "virucidal" is going to be understood as capable of inactivating viruses. The term "microbial cells" denotes bacterial or fungal cells, and the term "microorganism" denotes a fungus (including yeast) or a bacterium.
In the context of the present invention the term "which inhibits the growth of microbial cells" is understood to mean that the cells are in the non-growth state, i.e., that they are not capable of propagating. The term "hard surface" as used herein, refers to any surface which is essentially non-permeable for microorganisms. Examples of hard surfaces are surfaces made of metal, for example, stainless steel, plastics, rubber, cardboard, glass, wood, paper, textiles, concrete, rock, marble, plaster and ceramic materials which can be optimally coated , for example, with paint, enamel and the like. The hard surface can also be a process equipment, for example, a cooling tower, an osmotic membrane, a water treatment plant, a dairy, a food processing plant, a chemical or pharmaceutical process plant. Accordingly, the composition according to the present invention is useful in a conventional on-site cleaning system (C-I-P).
Haloperoxidases
In the context of the present invention the term "haloperoxidase" is proposed to mean an enzyme selected from the group consisting of peroxidase chloride (EC 1.11.1.10), peroxidase bromide, and iodide peroxidase (EC 1.11.1.8). A chloride peroxidase is an enzyme capable of oxidizing chloride, bromide and iodine ions with the consumption of H202. A peroxidase bromide is an enzyme capable of oxidizing bromide and iodide ions with the consumption of H2O2. An iodide peroxidase is an enzyme capable of oxidizing iodide ions with the consumption of H202. According to the invention, vanadium haloperoxidases are preferred. Vanadium peroxidases are different from other haloperoxidases because the prosthetic group in these enzymes has structural characteristics similar to vanadate (vanadium V), while the other haloperoxidases are hemeperoxidases. The vanadium haloperoxidases described in WO 95/27046 are preferred. Haloperoxidases form a class of enzymes which are capable of oxidizing halides (X = Cl-, Br-, or I-) in the presence of hydrogen peroxide to the corresponding hypohalide acid (HOX) according to:
H20 + X- + H + - > H20 + HOX
If an appropriate nucleophilic compound is present, a reaction with HOX will occur, which has an antimicrobial effect. Haloperoxidases have been isolated from several organisms: mammals, marine animals, plants, algae, lichen, fungi and bacteria (for reference see Biochimica et Biophysica Acta 1161, 1993, pp. 249-256). It is generally accepted that haloperoxidases are the enzymes responsible for the formation of halogenated compounds, although other enzymes may be involved. Haloperoxidases have been isolated from many different fungi, in particular from the fungal group of dematiaceous hyphomyteces, such as Caldariomyces, for example, C. fumago, Alternarla, Curvularia, for example, C. verruculosa and C. inaeqúalis, Dreschslera, Ulocladium and Botrytis. (See US Patent No. 4,937,192). According to the present invention, a haloperoxidase obtainable from Curvularia, in particular C. verruculose, is preferred, such as C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70. Curvularia haloperoxidase and recombinant production thereof is described in WO 97/04102. Haloperoxidase has also been isolated from bacteria such as Pseudomonas, for example, P. pyrrocinia (for reference see The Journal of Biological Chemistry 263, 1998, pp. 13725-13732) and Streptomyces, eg, S. aureofaciens (for reference see Structural Biology 1, 1994, pp. 532-537). Peroxidase bromide has been isolated from algae (see US Patent No. 4,937,192). In use, the concentration of the haloperoxidase can be varied to achieve the desired antimicrobial effect in the desired time frame. However, according to the invention, the haloperoxidase will normally be added at a concentration of 0.01-100 mg of enzyme protein per liter, preferably at a concentration of 0.05-50 mg of enzyme protein per liter, more preferably at a concentration of 0.5-10 mg of enzyme protein per liter.
Sources of Hydrogen Peroxide
According to the invention, the hydrogen peroxide necessary for the reaction with the haloperoxidase can be achieved in many different ways: it can be hydrogen peroxide or a precursor of hydrogen peroxide, such as, for example, percarbonate or perborate, or a peroxycarboxylic acid or a salt thereof, or the same may be a system of enzymes that generate hydrogen peroxide, such as, for example, an oxidase and its substrate. Useful oxidases can be, for example, a glucose oxidase, a glycerol oxidase or an amino acid oxidase. An example of an amino acid oxidase is given in WO 94/25574. It can be advantageous to use the hydrogen peroxide generated enzymatically, since this source leads to a relatively low concentration of hydrogen peroxide under the biologically relevant conditions. Low concentrations of hydrogen peroxide lead to an increase in the rate of the reaction catalyzed by the haloperoxidase. According to the invention, the source of hydrogen peroxide necessary for the reaction with the haloperoxidase can be added in a concentration corresponding to a concentration of hydrogen peroxide in the range from 0.01-1000 mM, preferably in the range from 0.1-100. mM.
Haluro sources
According to the invention, the halide source necessary for the reaction with the haloperoxidase can be achieved in many different ways, for example, by adding a halide salt: it can be sodium chloride, potassium chloride, sodium bromide, bromide of potassium, sodium iodide, or potassium iodide. The concentration of the halide source will typically correspond to a concentration of 0.01-1000 mM, preferably in the range of 0.05-500 mM.
Ammonium sources
When an ammonium source is added to the antimicrobial composition (haloperoxidase, hydrogen peroxide, halide), halide amines are formed which lead to a 100% bactericidal activity of the enzyme system.
It has thus been observed that there is a synergistic effect between the halide and the ammonium source present in the composition (see Examples 1, 2 and 4). The ammonium source used can be the compounds of the formula: Rl / HNr \ R2
wherein the substituent groups R1 and R2, which may be identical or different, independently represent any of the following radicals: hydrogen, halide, sulfate, phenyl, a straight or branched chain alkyl having from 1 to 14 carbon atoms, or a straight or branched substituted alkyl group having from 1 to 14 carbon atoms wherein the substituent group is located on C3-C18 and represents any of the following radicals: hydroxy, halogen, formyl, carboxy, and esters and salts thereof, carbamoyl, sulfo, and the esters and salts thereof, sulfamoyl, nitro, amino, phenyl, C1-C5 alkoxy, carbonyl-C? -C5-alkyl, aryl-C? -C5-alkyl; such carbamoyl, sulfamoyl, and amino groups can also be substituted or unsubstituted once or twice with a substituent group R3; and such phenyl may also be substituted or unsubstituted with one or more substituent groups R3; and such C1-C14 alkyl groups, C1-C5 alkoxy, C-C5-alkylcarbonyl, and aryl-Ci-C5alkyl can be saturated or unsaturated, branched or unbranched, and can also be substituted or not substituted with one or more substituent groups R3; such a substituent group R3 represents any of the following radicals: halogen, hydroxy, formyl, carboxy and esters and the salts thereof, carbamoyl, sulfo and esters and salts thereof, sulfamoyl, nitro, amino, phenyl, aminoalkyl, piperidino, piperazinyl, pyrrolidin-1-yl, Ci-Cs-alkyl, Ci-Cs-alkoxy; such carbamoyl, sulfamoyl, and amino groups can also be unsubstituted or substituted once or twice with hydroxy, Ci-Cs-alkyl, Ci-Cs-alkoxy; and such phenyl may be further substituted with one or more of the following radicals: halogen, hydroxy, amino, formyl, carboxy and esters and salts thereof, carbamoyl, sulfo and esters and salts thereof, and sulfamoyl; and such C? -C5-alkyl, and C? -C5-alkoxy groups may also be saturated or unsaturated, branched or unbranched, and may be further substituted once or twice with any of the following radicals: halogen, hydroxy, amino, formyl, carboxy and esters and salts thereof, carbamoyl, sulfo and esters and salts thereof, and sulfamoyl in which the general formula of the substituent groups R1-R2 can together form a group -B-, in the which B represents any of the following groups: (-CHR3-N == N-), (-CH = CH-) no (-CH = N-) n in such groups n represents an integer from 1 to 3, R3 it is a substituent group as defined. (It is to be understood that if the formula mentioned above comprises two or more substituent groups R3, these substituent groups R3 may be the same or different). When used herein, the ammonium compounds may be in their cationic form. In a preferred embodiment R 1 is hydrogen. In another preferred embodiment R1 is hydrogen and R2 is an alcohol (aminoalcohol), for example, ethanolamine. In a further preferred embodiment the ammonium source is an ammonium salt, ie any ammonium salt known in the art: for example, diammonium sulfate, ammonium chloride, ammonium bromide, or ammonium iodide. According to the invention, the ammonium source necessary for the reaction with the haloperoxidase can be added in a corresponding concentration with an ammonium concentration in the range from 0.01-1000 mM, preferably in the range from 0.05-500 mM.
The composition
The composition comprising the haloperoxidase, the source of hydrogen peroxide, the halide source, and the ammonium source can be formulated as a solid or a liquid. When formulated as a solid all components can be mixed together, for example, as a powder, a granulate or a gelled product. When compositions different from those of the dry form are used and even in this case, it is preferred to use a two part formulation system having the hydrogen peroxide separated from the other components. The composition of the invention may further comprise auxiliary agents such as wetting agents, thickening agents, buffers, stabilizers, perfume, colorants, fillers and the like.
Useful wetting agents are surfactants, i.e., nonionic, anionic, amphoteric or zwitterionic surfactants. The composition of the invention can be a concentrated product or a ready-to-use product. In use, 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 present microorganisms. The optimum pH is usually a compromise between the optimum stability and the optimal activity of the haloperoxidase in question. However, the invention can be advantageously carried out at a relatively high pH, since it is contemplated that the bacteriocidal activities are optimal at high pH values. The composition of the invention can also be formulated as a two-part system wherein one part is the haloperoxidase and the ammonium source; the other part is the source of hydrogen peroxide; and the halide source can then come from the tap water or be naturally present in another way.
Applications
The composition of the invention can be incorporated into a detergent or cleaning composition comprising more types of enzymes useful in detergent or cleaning compositions, preferably at least one additional enzyme selected from the group consisting of proteases, carbohydrases, amylases, cutinases, peroxidases, oxidases, laccases, cellulases, xylanases, and lipases. When used for the preservation of foods, beverages, cosmetics such as lotions, creams, gels, ointments, soaps, shampoos, conditioners, antiperspirants, deodorants, mouthwashes, products for contact lenses, enzyme formulations, or food ingredients, the composition used in the method of the present invention can be incorporated for example in foods, beverages, cosmetics, contact lens products, food ingredients or anti-inflammatory products in an amount effective to kill or inhibit the growth of microbial cells. Accordingly, the composition used in the method of the invention can be useful as a disinfectant, for example, in the treatment of acne, infections in the eyes or mouth, skin infections; in antiperspirants or deodorants; in the salts for the bath of the feet; for cleaning and disinfecting contact lenses, hard surfaces, teeth (oral care), wounds, battered parts and the like. It is generally contemplated that the composition of the present invention is useful for cleaning, disinfecting or inhibiting microbial growth on any hard surface. Examples of the surfaces, which can be advantageously contacted with the composition of the invention, are surfaces of the process equipment used for example in dairies, chemical or pharmaceutical process plants, water sanitation systems, processing plants of paper pulp, water treatment plants, and cooling towers. The composition of the invention must be used in an amount, which is effective for cleaning, disinfecting or inhibiting microbial growth on the surface in question. Furthermore, it is contemplated that the composition of the invention may be advantageously used in a cleaning system in place (C.I.P.) for the cleaning of process equipment of any kind. The method of the invention can be used additionally to clean surfaces and kitchen utensils in food processing plants and in any area in which foods such as hospitals, private hospitals, restaurants, especially fast food restaurants are prepared or served, Prepared and similar grocery stores. They can also be used as an antimicrobial in food products and could be especially useful as a surface antimicrobial in cheeses., fruits and vegetables and food on salad bars. They can also be used as a preservation agent or a disinfection agent in water-based paints. The 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 present invention is further illustrated in the following examples which are not proposed in any way to limit the scope of the invention as claimed.
EXAMPLE 1
Antibacterial activity of haloperoxidase against P. aeruginosa and S. epidermidis.
The antibacterial activity of the recombinant peroxidase of Curvularia verruculosa (rCvP), produced as described in WO 97/04102, available from Novo Nordisk A / S, DK-2880 Bagsvaerd, Denmark, has been tested with the following improving agents: sodium and diammonium sulfate. The antibacterial activity of a haloperoxidase was tested in a buffer of MES (2- [N-morpholino] ethanesulfonic acid) (pH 6.0) against Pseudomonas aeruginosa ATCC 10146 and Staphylococcus epidermidis DSM 20 042 with sodium chloride as an electron donor, and hydrogen peroxide was added as an electron acceptor in the presence of NH4 +. The cells (approximately 106 cfu / ml) were incubated with the enzyme for 15 minutes at 40 ° C. The bactericidal activity was determined by incubation in Malthus. The detection times measured by the Malthus instrument were converted to cfu / ml by a calibration curve.
Malthus measurements were used either direct or indirect when total surviving cells are listed (Malthus Flexi M2060, Malthus Instrument Limited). For direct measurements, cell metabolism was determined by conductance measurements in the growth substrate. For indirect measurements, 3 ml of the growth medium was transferred to the external chamber of the indirect Malthus cells, and 0.5 ml of sterile KOH (0.1 M) were transferred to the internal chamber. The suspensions of the cells were transferred after treatment of the enzymes to the external chamber of the Malthus cell. When the cells are growing in the outer chamber, they produce C02 which dissolves in the KOH in the internal chamber and through this the KOH conductance is changed. The amount of C02 formed by the breathing cells that survive the treatment of the enzymes are used to estimate the number of cells available. When the conductance change is measurable by
Malthus, a detection time (dt) will be recorded. The dt's were converted to colony counts by the use of a calibration curve that relates cfu / ml to dt (Fig. 1).
The antibacterial activity of a haloperoxidase (1 mg / l) with NaCl was observed at pH 6 at NaCl concentrations above 20 mM, the antibacterial activity increased with increasing NaCl concentrations but a plateau was reached at approximately 100 mM (depending on pH, temperature, test strains, etc.). Hydrogen peroxide was added to a final concentration of 0.5 mM. The use of 200 mM NaCl as an electron donor led to a reduction in living cells (both strains) from 106 cfu / ml to approximately 103 cfu / ml. A significant synergistic effect was observed between NaCl and (NH4) 2S04. The combination of NaCl and (NH4) 2S04 led to a 100% lethal activity against both strains (Figure 2) at a concentration of approximately 3 mM NH +.
EXAMPLE 2
Antibacterial activity of the recombinant haloperoxidase of Curcularia verruculosa using different enhancing agents • The antibacterial activity of a haloperoxidase (1 mg / ml) was tested in MES buffer (2- [N-morpholino] ethanesulfonic acid) (pH 6.0) against Staphylococcus epidermidis DSM 20 042 with potassium iodide and potassium bromide as an electron donor, and hydrogen peroxide (at a final concentration of 0.5 mM) was added as an electron acceptor in the presence of NH4 +. The cells (approximately 10 6 cfu / ml) were incubated with the enzyme for 15 min at 40 ° C. The bactericidal activity was determined by incubation in Malthus (see Example 1). An antibacterial activity of 100% of the haloperoxidase combined with iodide was determined at an iodide concentration of approximately 0.2 M. If ammonium is added, a 100% antibacterial activity was already determined at a concentration of approximately 0.05-0.1 mM iodide ( Figure 3). A high concentration of bromide (> 10 mM) was necessary for a 100% bactericidal activity, but the combination of the bromide and ammonium ions led to a 100% bactericidal activity at a bromide concentration above 2.5 mM ( Figure 4).
EXAMPLE 3
Antibacterial activity of the recombinant haloperoxidase of Curcularia verruculosa using ammonium halides as electron donors
The antibacterial activity of a haloperoxidase (1 mg / l) was tested in MES buffer (2- [N-morpholino] ethanesulfonic acid) (pH 6.0) against Staphylococcus epidermidis DSM 20 042 with ammonium iodide, ammonium chloride or bromide. ammonium as electron donors, and hydrogen peroxide was added as the electron acceptor giving the final concentration of 0.5 mM. The cells (approximately 10 6 cfu / ml) were incubated with enzyme for 15 minutes at 40 ° C. The bactericidal activity was determined by incubation in Malthus (see Example 1). The concentration of the ammonium halides which is necessary for the antibacterial activity is below the concentration of the potassium or sodium halides necessary for the same activity (Table 1).
Table 1: Bactericidal activity against S. epidermidis. The electron donor is added either as a sodium or potassium salt or an ammonium salt.
Concentration of the halide Concentration log in the number of the cells (log cfu / ml) - 0 0 INH4: 0.25 6.2 0.5 6.2
Kl: 0.25 5.1 0.5 6.1
C1NH4: 25 6.2 50 6.2
NaCl: 25 0.5 50 0.8
BrNH4: 4 3.7 8 6.2
KBr: 4 2.8 8 5.4 It can be seen from Table 1 that if the salt is an ammonium halide salt such as ammonium iodide, ammonium chloride, or ammonium bromide, a bactericidal activity of 100% is possible. . Thus, the source of halide and the ammonium source may be the same, but normally the optimum concentrations of halide and ammonium will be at different levels.
EXAMPLE 4
Antibacterial synergistic activity of the recombinant haloperoxidase of Curcularia verruculosa (rCvP) using ethanolamine in combination with halides
The antibacterial activity of the haloperoxidase of Curvularia verruculosa (1 mg / l) is tested in HEPES buffer (Sigma H3375) (pH 7.0) against Staphylococcus epidermidis DSM 20 042 with chloride (80 mM) as the electron donor combined with ethanolamine (2.5 mM), and hydrogen peroxide was added as the electron acceptor giving the final concentration of 0.5 mM. The synergistic effects were found using a 2 'factorial design. The cells (approximately 10 6 cfu / ml) were incubated with enzyme for 15 minutes at 40 ° C. The bactericidal activity was determined by incubation in Malthus (see Example 1). The addition of ethanolamine significantly increased the activity of the enzyme system (see Figure 5). Therefore, 100% killing against Staphylococcus epidermidis was achieved when ethanolamine was added, while a cell reduction of about 3 log units was observed when ethanolamine was not added.
It is noted that in relation to this date, the best method known by the applicant to carry out the aforementioned invention, is the conventional one for the manufacture of the objects to which it relates.
Having described the invention as above, property is claimed as contained in the following
Claims (32)
1. An enzymatic antimicrobial composition, characterized in that it comprises a haloperoxidase, a source of hydrogen peroxide, a halide source, and an ammonium source of the formula: wherein the substituent groups R1 and R2, which may be identical or different, independently represent any of the following radicals: hydrogen, halide, sulfate, phenyl, a straight or branched chain alkyl having from 1 to 14 carbon atoms, or a straight or branched substituted alkyl group having from 1 to 14 carbon atoms wherein the substituent group is located on C3-C18 and represents any of the following radicals: hydroxy, halogen, formyl, carboxy, and esters and salts thereof, carbamoyl, sulfo, and the esters and salts thereof, sulfamoyl, nitro, amino, phenyl, alkoxy with C1-C5, carbonyl-C? -C5-alkyl, aryl-Ca-Cs-alkyl; such carbamoyl, sulfamoyl, and amino groups can also be substituted or unsubstituted once or twice with a substituent group R3; and such phenyl may also be substituted or unsubstituted with one or more substituent groups R3; and such alkyl groups with Ci-, C1-C5 alkoxy, carbonyl-Ci-Cs-alkyl, and aryl-Ci-C5-alkyl can be saturated or unsaturated, branched or unbranched, and can be further substituted or unsubstituted with one or more substituent groups R3; such a substituent group R3 represents any of the following radicals: halogen, hydroxy, formyl, carboxy and esters and the salts thereof, carbamoyl, sulfo and esters and salts thereof, sulfamoyl, nitro, amino, phenyl, aminoalkyl, piperidino, piperazinyl, pyrrolidin-1-yl, Ci-Cs-alkyl, Ci-Cs-alkoxy; such carbamoyl, sulfamoyl, and amino groups can also be unsubstituted or substituted once or twice with hydroxy, Ci-Cs-alkyl, Ci-Cs-alkoxy; and such phenyl may be further substituted with one or more of the following radicals: halogen, hydroxy, amino, formyl, carboxy and esters and salts thereof, carbamoyl, sulfo and esters and salts thereof, and sulfamoyl; and such C? -C5-alkyl, and C? -C5-alkoxy groups may also be saturated or unsaturated, branched or unbranched, and may be further substituted once or twice with any of the following radicals: halogen, hydroxy, amino, formyl, carboxy and esters and salts thereof, carbamoyl, sulfo and esters and salts thereof, and sulfamoyl; or in such a general formula the substituent groups Rl-R2 can jointly form a group -B-, in which B represents any of the following groups: (-CHR3-N = N-), (-CH = CH-) no (-CH = N-) n in such groups n represents a. whole number from 1 to 3, R3 is a substituent group as defined.
2. The composition according to claim 1, characterized in that the haloperoxidase is obtainable from fungi, bacteria, or algae.
3. The composition according to claim 2, characterized in that the haloperoxidase is obtainable from a fungus selected from the group consisting of Caldariomyces, Alternarla, Curvularia, Drechslera, Ulocladium and Botrytis.
4. The composition according to claim 3, characterized in that the haloperoxidase is obtainable from the Curvularia.
5. The composition according to claim 4, characterized in that the haloperoxidase is obtainable from the verrucous Curvularia.
6. The composition according to claim 5, characterized in that the haloperoxidase is obtainable from the Currularia verruculose CBS 147.63, or the haloperoxidase is reactive immunologically cross-linked with the haloperoxidase obtainable from the Curvularia verruculosa CBS 147.63.
7. The composition according to claim 2, characterized in that the haloperoxidase is obtainable from a bacterium selected from the group consisting of Pseudomonas and Streptomyces.
8. The composition according to claim 1, characterized in that the haloperoxidase is a vanadium peroxidase.
9. The composition according to claim 1, characterized in that the haloperoxidase is a peroxidase chloride or a peroxidase bromide.
10. The composition according to claim 1, characterized in that the source of hydrogen peroxide is hydrogen peroxide, or a precursor of hydrogen peroxide, or an enzyme system that generates hydrogen peroxide, or a peroxycarboxylic acid or a salt of the same.
11. The composition according to claim 1, characterized in that the halide source is a halide salt.
12. The composition according to claim 11, characterized in that the halide source is sodium chloride, potassium chloride, sodium bromide, potassium bromide, sodium iodide, or potassium iodide.
13. The composition according to claim 1, characterized in that the source of ammonium is an ammonium salt.
14. The composition according to claim 13, characterized in that the source of ammonium is diammonium sulfate, ammonium chloride, ammonium bromide, or ammonium iodide.
15. The composition according to claim 1, characterized in that the ammonium source is an amino alcohol.
16. The composition according to claim 1, characterized in that the composition is a. aqueous composition.
17. The composition according to claim 16, characterized in that the concentration of the haloperoxidase is in the range from 0.01-100 mg of enzyme protein per liter.
18. The composition according to claim 16, characterized in that the concentration of the source of hydrogen peroxide corresponds to 0.01 1000 mM.
19. The composition according to claim 16, characterized in that the concentration of the halide source corresponds to 0.01-1000 mM.
20. The composition according to claim 16, characterized in that the concentration of the ammonium source corresponds to 0.01-1000 mM.
21. The composition according to claim 1, characterized in that the composition is a granulate.
22. A method of inhibiting the microorganisms present in laundry, characterized in that the laundry is treated with a soaking, washing or rinsing liquor comprising an effective amount of the composition according to claim 1.
23. The method according to claim 22, characterized in that the laundry is treated in a washing machine.
24. A method of preserving a cosmetic product, characterized in that an effective amount of the composition according to claim 1 is incorporated in the cosmetic product.
25. The method according to claim 24, characterized in that the cosmetic product is a composition for washing the mouth, a cosmetic liquid or a gel or a paste, a lotion for the eyes, an antiperspirant, a deodorant, a dew solution nasal, an ointment for the eyes, an ointment or cream, a salt for the bath of the feet.
26. The use of the composition according to claim 1, for cleaning or disinfecting contact lenses.
27. A method of cleaning, disinfecting or inhibiting microbial growth on a hard surface, wherein the surface is contacted with the composition according to claim 1.
28. The method according to claim 27, characterized in that the hard surface is a process equipment such as an element of a cooling tower, a water treatment plant, a dairy, a food processing plant, a processing plant chemical or pharmaceutical.
29. The method according to claim 27, characterized in that the hard surface is a sanitary surface of the water.
30. The method according to claim 29, characterized in that the hard surface is a surface of equipment for processing the pulp of the paper.
31. The use of the composition in accordance with. Claim 1 in a cleaning system in place.
32. The use of the composition according to claim 1 for the disinfection of water systems.
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
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DK0940/97 | 1997-08-14 |
Publications (1)
Publication Number | Publication Date |
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MXPA00001369A true MXPA00001369A (en) | 2001-03-05 |
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