EP4189051A1 - Use of an enzyme and surfactant for inhibiting microorganisms - Google Patents
Use of an enzyme and surfactant for inhibiting microorganismsInfo
- Publication number
- EP4189051A1 EP4189051A1 EP21751536.0A EP21751536A EP4189051A1 EP 4189051 A1 EP4189051 A1 EP 4189051A1 EP 21751536 A EP21751536 A EP 21751536A EP 4189051 A1 EP4189051 A1 EP 4189051A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- detergent composition
- use according
- virus
- hydrolytic enzyme
- enzyme
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
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- WQEPLUUGTLDZJY-UHFFFAOYSA-N n-Pentadecanoic acid Natural products CCCCCCCCCCCCCCC(O)=O WQEPLUUGTLDZJY-UHFFFAOYSA-N 0.000 description 1
- ZOCHHNOQQHDWHG-UHFFFAOYSA-N n-hexan-3-ol Natural products CCCC(O)CC ZOCHHNOQQHDWHG-UHFFFAOYSA-N 0.000 description 1
- 210000002850 nasal mucosa Anatomy 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- 235000012149 noodles Nutrition 0.000 description 1
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- QIQXTHQIDYTFRH-UHFFFAOYSA-N octadecanoic acid Chemical compound CCCCCCCCCCCCCCCCCC(O)=O QIQXTHQIDYTFRH-UHFFFAOYSA-N 0.000 description 1
- OQCDKBAXFALNLD-UHFFFAOYSA-N octadecanoic acid Natural products CCCCCCCC(C)CCCCCCCCC(O)=O OQCDKBAXFALNLD-UHFFFAOYSA-N 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 150000007530 organic bases Chemical class 0.000 description 1
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- 125000005342 perphosphate group Chemical group 0.000 description 1
- 235000020030 perry Nutrition 0.000 description 1
- JRKICGRDRMAZLK-UHFFFAOYSA-L persulfate group Chemical group S(=O)(=O)([O-])OOS(=O)(=O)[O-] JRKICGRDRMAZLK-UHFFFAOYSA-L 0.000 description 1
- 239000003208 petroleum Substances 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- HXITXNWTGFUOAU-UHFFFAOYSA-N phenylboronic acid Chemical class OB(O)C1=CC=CC=C1 HXITXNWTGFUOAU-UHFFFAOYSA-N 0.000 description 1
- UEZVMMHDMIWARA-UHFFFAOYSA-M phosphonate Chemical compound [O-]P(=O)=O UEZVMMHDMIWARA-UHFFFAOYSA-M 0.000 description 1
- 229920002006 poly(N-vinylimidazole) polymer Polymers 0.000 description 1
- 229920000196 poly(lauryl methacrylate) Polymers 0.000 description 1
- 229920005646 polycarboxylate Polymers 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 239000001205 polyphosphate Substances 0.000 description 1
- 235000011176 polyphosphates Nutrition 0.000 description 1
- 229920005996 polystyrene-poly(ethylene-butylene)-polystyrene Polymers 0.000 description 1
- 239000004300 potassium benzoate Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 239000004405 propyl p-hydroxybenzoate Substances 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 150000003219 pyrazolines Chemical class 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 230000000241 respiratory effect Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 238000009490 roller compaction Methods 0.000 description 1
- 229930007790 rose oxide Natural products 0.000 description 1
- 102200131574 rs11556620 Human genes 0.000 description 1
- 102220036452 rs137882485 Human genes 0.000 description 1
- 102200118280 rs33918343 Human genes 0.000 description 1
- 102200034374 rs6092 Human genes 0.000 description 1
- 102220005204 rs63750783 Human genes 0.000 description 1
- 102220289974 rs757282628 Human genes 0.000 description 1
- 102220123717 rs759057581 Human genes 0.000 description 1
- 102200025035 rs786203989 Human genes 0.000 description 1
- 102220099575 rs878853725 Human genes 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 238000011012 sanitization Methods 0.000 description 1
- 238000007127 saponification reaction Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 150000004671 saturated fatty acids Chemical class 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 229910001388 sodium aluminate Inorganic materials 0.000 description 1
- 239000000429 sodium aluminium silicate Substances 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- UIIMBOGNXHQVGW-UHFFFAOYSA-M sodium bicarbonate Substances [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- QSKQNALVHFTOQX-UHFFFAOYSA-M sodium nonanoyloxybenzenesulfonate Chemical compound [Na+].CCCCCCCCC(=O)OC1=CC=CC=C1S([O-])(=O)=O QSKQNALVHFTOQX-UHFFFAOYSA-M 0.000 description 1
- 229960001922 sodium perborate Drugs 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- WBPFVHVTNAEJCX-UHFFFAOYSA-M sodium;2-[[4-(dimethylamino)phenyl]-(4-dimethylazaniumylidenecyclohexa-2,5-dien-1-ylidene)methyl]-5-[ethyl-[(3-sulfonatophenyl)methyl]amino]benzenesulfonate Chemical compound [Na+].C=1C=C(C(=C2C=CC(C=C2)=[N+](C)C)C=2C=CC(=CC=2)N(C)C)C(S([O-])(=O)=O)=CC=1N(CC)CC1=CC=CC(S([O-])(=O)=O)=C1 WBPFVHVTNAEJCX-UHFFFAOYSA-M 0.000 description 1
- NETSNTQRMHVIEK-UHFFFAOYSA-M sodium;2-[n-butyl-4-[[4-[butyl(2-sulfonatoethyl)azaniumylidene]cyclohexa-2,5-dien-1-ylidene]-[4-(4-ethoxyanilino)phenyl]methyl]anilino]ethanesulfonate Chemical compound [Na+].C1=CC(N(CCS([O-])(=O)=O)CCCC)=CC=C1C(C=1C=CC(NC=2C=CC(OCC)=CC=2)=CC=1)=C1C=CC(=[N+](CCCC)CCS([O-])(=O)=O)C=C1 NETSNTQRMHVIEK-UHFFFAOYSA-M 0.000 description 1
- FLOMHNPVJPAASA-UHFFFAOYSA-M sodium;3-[[4-(dimethylamino)phenyl]-[4-[methyl-[(3-sulfonatophenyl)methyl]amino]phenyl]methylidene]-6-dimethylazaniumylidenecyclohexa-1,4-diene-1-sulfonate Chemical compound [Na+].C1=CC(N(C)C)=CC=C1C(\C=1C=CC(=CC=1)N(C)CC=1C=C(C=CC=1)S([O-])(=O)=O)=C\1C=C(S([O-])(=O)=O)C(=[N+](C)C)C=C/1 FLOMHNPVJPAASA-UHFFFAOYSA-M 0.000 description 1
- IXNUVCLIRYUKFB-UHFFFAOYSA-M sodium;3-[[4-[[4-(diethylamino)-2-methylphenyl]-[4-[ethyl-[(3-sulfonatophenyl)methyl]azaniumylidene]cyclohexa-2,5-dien-1-ylidene]methyl]-n-ethylanilino]methyl]benzenesulfonate Chemical compound [Na+].CC1=CC(N(CC)CC)=CC=C1C(C=1C=CC(=CC=1)N(CC)CC=1C=C(C=CC=1)S([O-])(=O)=O)=C(C=C1)C=CC1=[N+](CC)CC1=CC=CC(S([O-])(=O)=O)=C1 IXNUVCLIRYUKFB-UHFFFAOYSA-M 0.000 description 1
- IBDSNZLUHYKHQP-UHFFFAOYSA-N sodium;3-oxidodioxaborirane;tetrahydrate Chemical compound O.O.O.O.[Na+].[O-]B1OO1 IBDSNZLUHYKHQP-UHFFFAOYSA-N 0.000 description 1
- KQRZWHVIXVADGL-UHFFFAOYSA-M sodium;4-[[4-(dibenzylamino)phenyl]-(4-dibenzylazaniumylidenecyclohexa-2,5-dien-1-ylidene)methyl]benzene-1,3-disulfonate Chemical compound [Na+].[O-]S(=O)(=O)C1=CC(S(=O)(=O)[O-])=CC=C1C(C=1C=CC(=CC=1)N(CC=1C=CC=CC=1)CC=1C=CC=CC=1)=C(C=C1)C=CC1=[N+](CC=1C=CC=CC=1)CC1=CC=CC=C1 KQRZWHVIXVADGL-UHFFFAOYSA-M 0.000 description 1
- FTUYQIPAPWPHNC-UHFFFAOYSA-M sodium;4-[[4-[benzyl(ethyl)amino]phenyl]-[4-[benzyl(ethyl)azaniumylidene]cyclohexa-2,5-dien-1-ylidene]methyl]benzene-1,3-disulfonate Chemical compound [Na+].C=1C=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=CC=CC=2)C=2C(=CC(=CC=2)S([O-])(=O)=O)S([O-])(=O)=O)C=CC=1N(CC)CC1=CC=CC=C1 FTUYQIPAPWPHNC-UHFFFAOYSA-M 0.000 description 1
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 1
- 239000008247 solid mixture Substances 0.000 description 1
- LJFWQNJLLOFIJK-UHFFFAOYSA-N solvent violet 13 Chemical compound C1=CC(C)=CC=C1NC1=CC=C(O)C2=C1C(=O)C1=CC=CC=C1C2=O LJFWQNJLLOFIJK-UHFFFAOYSA-N 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 239000008117 stearic acid Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 150000005846 sugar alcohols Chemical class 0.000 description 1
- 230000001180 sulfating effect Effects 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-N sulfuric acid Substances OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- TUNFSRHWOTWDNC-HKGQFRNVSA-N tetradecanoic acid Chemical class CCCCCCCCCCCCC[14C](O)=O TUNFSRHWOTWDNC-HKGQFRNVSA-N 0.000 description 1
- 108010031354 thermitase Proteins 0.000 description 1
- 230000008719 thickening Effects 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- 150000003852 triazoles Chemical class 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- WCTAGTRAWPDFQO-UHFFFAOYSA-K trisodium;hydrogen carbonate;carbonate Chemical compound [Na+].[Na+].[Na+].OC([O-])=O.[O-]C([O-])=O WCTAGTRAWPDFQO-UHFFFAOYSA-K 0.000 description 1
- 241000712461 unidentified influenza virus Species 0.000 description 1
- AQLJVWUFPCUVLO-UHFFFAOYSA-N urea hydrogen peroxide Chemical compound OO.NC(N)=O AQLJVWUFPCUVLO-UHFFFAOYSA-N 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000001993 wax Substances 0.000 description 1
- 210000002268 wool Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/02—Anionic compounds
- C11D1/12—Sulfonic acids or sulfuric acid esters; Salts thereof
- C11D1/22—Sulfonic acids or sulfuric acid esters; Salts thereof derived from aromatic compounds
-
- 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
- C11D3/02—Inorganic compounds ; Elemental compounds
- C11D3/04—Water-soluble compounds
- C11D3/08—Silicates
-
- 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
- C11D3/02—Inorganic compounds ; Elemental compounds
- C11D3/04—Water-soluble compounds
- C11D3/10—Carbonates ; Bicarbonates
-
- 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
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
-
- 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
-
- C11D2111/12—
Definitions
- the present invention relates to the use of an enzyme and a surfactant in a detergent composition for inhibiting microorganisms.
- the present invention particularly relates to the use of an enzyme and a surfactant in detergent composition for antiviral activity.
- Sanitizing or disinfecting skin and inanimate surfaces is a very important aspect for ensuring healthy condition. Areas of focus for ensuring disinfection include personal uses like hand and body hygiene and hygiene of hard surfaces like doorknobs and soft surfaces such as clothing.
- Bacteria, virus and protozoa are the three common microorganisms known to cause diseases in human and other mammals. Cleaning skin and other animate and inanimate surfaces to reduce microbial populations is a first defense in removing such pathogens and minimizing the risk of infection. There are compositions available for disinfection against each of these types of organisms. While many antibacterial actives and compositions are available and widely used, killing of virus is more difficult and often requires harsher chemicals like chlorine or alcohol.
- Viruses are a category of pathogens of primary concern and viral infections are among the greatest causes of human morbidity. Virus infections of respiratory tract are generally spread from person to person by direct contact with virus-contaminated respiratory secretions. Typically, this contact is in the form of physical contact with a contaminated surface or via inhalation of airborne viral particles. Viruses can survive on environmental surfaces for hours after initial contamination, and infection is readily transmitted by finger-to-finger contact, and by contaminated environmental surface-to-finger contact, if the newly contaminated finger is then used to rub an eye or touch the nasal mucosa. Therefore, minimizing virus contamination of skin and environmental surfaces which includes inanimate and animate surfaces may prove to be effective in reducing the risk of transmitting the infection to the general population.
- Viruses propagate only within living cells.
- the principal obstacle encountered by a virus is gaining entry into the cell, which is protected by a cell membrane of thickness comparable to the size of the virus.
- a virus In order to penetrate a cell, a virus first must become attached to the cell surface. Therefore, in order to control a viral infection, it is important to rapidly kill a virus that contacts the skin, and ideally to provide a persistent antiviral activity on the skin, or inanimate surface, in order to control viral infections.
- Coronaviruses primarily infect the respiratory tract and gastrointestinal tract of mammals and birds. Coronaviruses are enveloped viruses with a positive-sense single-stranded RNA genome and with a nucleocapsid of helical symmetry. Coronavirus infection begins with attachment of the spike protein with its cognate cell receptor. It is desirable find new ways capable of deactivating viruses specifically coronaviruses.
- Virus control poses a more difficult problem than bacterial control. By sufficiently reducing bacterial populations, the risk of bacterial infection is reduced to acceptable levels.
- EP1065265 B1 discloses a germicidal detergent composition having a pH of 6.5 to 7.5 and which includes protease.
- WO 2010/069812 A2 discloses a process for disinfecting textiles and or hard surfaces by contacting with a virucidal treatment solution having at least one hydrolytic enzyme.
- detergent compositions which generally have pH in the range from 8 to 13 are known to impart stain removal benefits, they were not known to impart antimicrobial, particularly antibacterial and viral inactivation benefits.
- a further object is that the composition does not contain harsh chemicals which lead to undesirable affects that can be considered to be harmful to the consumer.
- the invention in a first aspect relates to the use of a combination of alkyl benzene sulphonate surfactant, hydrolytic enzyme, and an alkaline source in a solid detergent composition having a pH from 10 to 13 (as measured at 25°C and 10% aqueous concentration in deionised water) for inactivation of microorganisms on a textile article during a laundering process
- the hydrolytic enzyme is selected from the group consisting of protease, lipase, cellulase, amylase, mannanase or combinations thereof.
- the invention provides a method for inactivation of microorganisms from a textile article, the method comprising the steps of: i) contacting the surface to be laundered with an aqueous solution of a solid detergent composition of the first aspect; ii) allowing the surface to be laundered to remain in intimate contact with the aqueous solution for at least 30 minutes, still preferably at least 60 minutes; and, iii) optionally rinsing the surface with water.
- solid detergent composition includes granular, powder, tablets, or bar composition.
- the composition is a solid laundry detergent composition.
- alkyl benzene sulphonate surfactant in a detergent composition.
- Linear alkylbenzene sulfonate or LAS are linear alkylbenzenes that has been sulfonated to include an acidic sulfonate group attached to the benzene ring to form a parent acid, linear alkylbenzene sulfonic acid.
- the linear alkylbenzene sulfonic acid by neutralization using any of alkali metal hydroxides, alkaline earth hydroxides, ammonium hydroxides, alkylammonium hydroxides, alkanolamine or any chemical agent known by those skilled in the art forms water-soluble linear alkylbenzene sulfonates.
- the composition comprises alkyl benzene sulphonate, preferably a linear or branched, substituted or unsubstituted, Cs to C24 alkyl benzene sulphonate.
- the Cs to C24 alkyl benzene sulphonate can be a modified alkylbenzene sulphonate (MLAS) as described in more detail in WO 99/05243, WO 99/05242, WO 99/05244, WO 99/05082, WO 99/05084, WO 99/05241, WO 99/07656, WO 00/23549, and WO 00/23548.
- MLAS modified alkylbenzene sulphonate
- C 8 to C 2 alkyl benzene sulphonates are linear C10 to Cie alkylbenzene sulphonates.
- linear C10 to Ci3 alkylbenzene sulphonates that are obtainable, preferably obtained, by sulphonating commercially available linear alkyl benzenes (LAB);
- suitable LAB include low 2- phenyl LAB, such as those supplied by Sasol under the tradename Isochem® or those supplied by Petresa under the tradename Petrelab®, other suitable LAB include high 2- phenyl LAB, such as those supplied by Sasol under the tradename Hyblene®.
- the composition comprises alkyl benzene sulphonate, wherein the alkyl benzene sulphonate comprises at least 25 wt.% of the 2-phenyl isomer.
- a suitable alkyl benzene sulphonate having this feature is obtained by DETAL synthesis.
- suitable synthetic anionic detergent compounds are sodium and potassium salts, especially those obtained by sulphating alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl Cio to C20 benzene sulphonates, particularly sodium linear secondary alkyl C10 to C15 benzene sulphonates; are sodium Cn to C15 alkyl benzene sulphonates.
- the detergent composition according to the present invention comprises from 2 wt.% to 40 wt.% alkyl benzene sulphonate surfactant.
- the detergent composition comprises at least 6 wt.% alkyl benzene sulphonate surfactant based on the weight of the detergent composition, still preferably at least 7 wt.%, still preferably at least 8 wt.%, most preferably at least 10 wt.%, but typically not more than 35 wt.%, still preferably not more than 30 wt.%, more preferably not more than 25 wt.% and most preferably not more than 15 wt.% alkyl benzene sulphonate surfactant in the detergent composition.
- the use according to the first aspect of the present invention involves inactivating the microorganisms in a wash liquor prepared by addition of the solid detergent composition in water, wherein the alkyl benzene sulphonate surfactant is present at a concentration from 40 ppm to 2000 ppm.
- concentration is at least 50 ppm, still preferably at least 100 ppm, still preferably at least 200 ppm, most preferably at least 250 ppm, but typically not more than 1600ppm, still preferably not more than 1000 ppm, more preferably not more than 800 ppm and most preferably not more than 600 ppm in the wash liquor.
- a hydrolytic enzyme is a hydrolase enzyme which hydrolytically cleaves esters, ethers, peptides, glycosides, acid anhydrides or C-C bonds in a reversible reaction.
- the hydrolytic enzyme catalyzes the hydrolytic cleavage of substances.
- the hydrolytic enzyme is selected from the group consisting of protease, lipase, cellulase, amylase, mannanase or combinations thereof.
- Preferred further enzyme for use in the present invention includes but is not limited to the group consisting of glycosidase, hemicellulases, xylanase, pectinase, glucosidase, carrageenase, or combination thereof.
- the enzyme is a protease enzyme.
- the hydrolytic enzyme is present in the solid detergent composition of the invention in a preferred level of from 0.0001 to about 1%, more preferably from about 0.001 to about 0.5% and especially from about 0.005 to about 0.6% of active hydrolytic enzyme.
- the wash liquor prepared by diluting the solid detergent composition according to the present invention in water comprises from 0.0001 ppm to 30 ppm of pure hydrolytic enzyme, still preferably from 0.0001 ppm to 20 ppm of pure hydrolytic enzyme.
- the detergent composition comprises at least 0.0005 ppm, still preferably at least 0.001 ppm, still preferably at least 0.002 ppm, most preferably at least 0.005 ppm, still more preferably 0.4 ppm, but typically not more than 22 ppm, preferably not more than 20 ppm, still preferably not more than 15 ppm, most preferably not more than 10 ppm.
- the hydrolytic enzyme is a protease enzyme.
- the protease enzyme is an alkaline protease, preferably a serine protease.
- Suitable proteases include those of bacterial, fungal, plant, viral or animal origin, preferably of vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as subtilisin. A metalloproteases protease may for example be a thermolysin from e.g., family M4 or other metalloprotease such as those from M5, M7 or M8 families.
- Serine proteases are a subgroup of carbonyl hydrolases comprising a diverse class of enzymes having a wide range of specificities and biological functions.
- the term "subtilases” refers to a sub-group of serine protease according to Siezen et al. , 1991, Protein Engng. 4: 719-737 and Siezen et al., 1997, Protein Science 6: 501-523.
- Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate.
- the subtilases may be divided into 6 sub-divisions, i.e. , the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
- subtilases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US 7,262,042 and WO 2009/021867 , and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO 89/06279 and protease PD138 described in ( WO 93/18140 ).
- proteases may be those described in WO 92/175177, WO 01/16285, WO 02/026024, US8753861B2 and WO 02/016547.
- trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270, WO 94/25583 and WO 2005/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 2005/052161 and WO 2005/052146.
- a further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 95/23221, and variants thereof which are described in WO 92/21760, WO 95/23221, EP 1921147, and EP 1921148.
- metalloproteases are the neutral metalloprotease as described in WO 2007/044993 (Genencor Int.) such as those derived from Bacillus amyloliquefaciens.
- proteases are the variants described in: W092/19729, WO96/034946, WO98/20115 , WO98/20116 , WO99/011768 , WO01/44452 , W003/006602,
- subtilase variants may comprise the mutations: S3T, V41, S9R, A15T, K27R, *36D, V68A, N76D, N87S,R, *97E, A98S, S99G,D,A, S99AD, S101 G,M,R S103A, V104I,Y,N, S106A, G1 18V, R, H120D.N, N123S, S128L, P129Q, S130A, G160D, Y167A, R170S, A194P, G195E, V199M, V205I, L217D, N218D, M222S, A232V, K235L, Q236H, Q245R, N252K, T274A (using BPN' numbering).
- Suitable commercially available protease enzymes include those sold under the trade names AlcalaseTM, DuralaseTM, DurazymTM, RelaseTM, RelaseTM Ultra, SavinaseTM, SavinaseTM
- Lipase is an enzyme which catalyses hydrolysis of ester bonds of edible fats and oils, i.e. triglycerides, into free fatty acids, mono- and diglycerides and glycerol.
- the lipase may be selected from lipase enzymes in E.C. class 3.1, 3.2 or a combination thereof.
- the cleaning lipases selected is a Triacylglycerol lipases (E.C. 3.1.1.3).
- Suitable triacylglycerol lipases can be selected from variants of the Humicola lanuginosa (Thermomyces lanuginosus) lipase.
- Other suitable triacylglycerol lipases can be selected from variants of Pseudomonas lipases, e.g., from P. alcaligenes or P. pseudoalcaligenes (EP 218272), P. cepacia (EP 331 376), P. stutzeri (GB 1,372,034), P. fluorescens,
- Pseudomonas sp. strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis 25 (WO 96/12012), Bacillus lipases, e.g., from B. subtilis (Dartois et al. (1993),Biochemica et Biophysica Acta, 1131,253-360), B.stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422).
- EC 3.1.1.3 lipases include those described in WIPO publications WO 00/60063, WO 99/42566, WO 02/062973, WO 97/04078, WO 97/04079 and US 5,869,438.
- Preferred lipases are produced by Absidia reflexa, Absidia corymbefera, Rhizmucor miehei, Rhizopus deleman Aspergillus niger, Aspergillus tubigensis, Fusajum oxysporum, Fusarium heterosporum, Aspergillus oryzea, Penicilium camembertii, Aspergillus foetidus, Aspergillus niger, Thermomyces lanoginosus (synonym: Humicola lanuginosa) and Landerina penisapora, particularly Thermomyces lanoginosus.
- Certain preferred lipases are supplied by Novozymes and includes those under the tradenames of Lipolase®, Lipolase Ultra®, Lipoprime®, Lipoclean® and Lipex® (registered tradenames of Novozymes) and LIPASE P "AMANO®” available from Areario Pharmaceutical Co. Ltd., Nagoya, Japan, AMANO-CES®, commercially available from Toyo Jozo Co., Tagata, Japan; and further Chromobacter viscosum lipases from Amersham Pharmacia Biotech., Piscataway, New Jersey, U.S. A. and Diosynth Co., Netherlands, and other lipases such as Pseudomonas gladioli.
- lipase variants such as those described in EP407225 , WO92/05249 , WO94/01541 , W094/25578 , W095/14783 , WO95/30744 , W095/35381 , W095/22615 , W096/00292 , W097/04079 , W097/07202 , WO00/34450 , WO00/60063 , WO01/92502 , W007/87508 and WO09/109500 .
- Preferred commercial lipase products include LipolaseTM, LipexTM; LipolexTM and LipocleanTM (Novozymes A/S), LumafastTM (originally from Genencor) and LipomaxTM (originally from Gist-Brocades).
- LIPEX ® is particularly preferred, and LIPEX ® 100 TB is further particularly preferred.
- suitable lipases include the "first cycle lipases" described in WO 00/60063 and U.S. Patent 6,939,702 Bl, preferably a variant of SEQ ID No. 2, more preferably a variant of SEQ ID No. 2 having at least 90% homology to SEQ ID No. 2 comprising a substitution of an electrically neutral or negatively charged amino acid with R or K at any of positions 3, 224, 229, 231 and 233, with a most preferred variant comprising T23 IR and N233R mutations, such most preferred variant being sold under the tradename Lipex® (Novozymes).
- lipases can be used in combination (any mixture of lipases can be used). Suitable lipases can be purchased from Novozymes, Bagsvaerd, Denmark; Areario Pharmaceutical Co. Ltd., Nagoya, Japan; Toyo Jozo Co., Tagata, Japan; Amersham Pharmacia Biotech., Piscataway, New Jersey, U.S.A; Diosynth Co., Oss, Netherlands and/or made in accordance with the examples contained herein.
- Lipase with reduced potential for odour generation and a good relative performance are particularly preferred, as described in W02007/087243. These include lipoclean® (Novozyme).
- amylases include alpha-amylases and/or glucoamylases and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1,296,839.
- Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597 , WO 94/18314 , WO 97/43424 and SEQ ID NO: 4 of WO 99/019467 , such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 21 1, 243, 264, 304, 305, 391 , 408, and 444.
- amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
- Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.
- Other amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B.amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof.
- Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181, N190,
- amylases which are suitable are amylases having SEQ ID NO: 6 in WO99/019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
- Preferred variants of SEQ I D NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216 and K269.
- amylases are those having deletion in positions R181 and G182, or positions H183 and G184.
- Additional amylases which can be used are those having SEQ ID NO: 1 , SEQ ID NO: 3,
- Preferred variants of SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181,
- SEQ ID 2 of WO 96/023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181, 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184. Most preferred amylase variants of SEQ I D NO: 1, SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.
- amylases which can be used are amylases having SEQ ID NO: 2 of WO08/153815 , SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01/66712 .
- Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211 and 264.
- amylase variants such as those described in WO2011/098531 .
- amylases are DuramylTM, TermamylTM, FungamylTM, StainzymeTM, Stainzyme PlusTM, NatalaseTM, Liquozyme XTM and BANTM (from Novozymes AS), and RapidaseTM, PurastarTM/EffectenzTM, PoweraseTM, Preferenz S1000TM, Preferenz S100TM and Preferenz S110TM (from Genencor International Inc./DuPont).
- the lyase may be a pectate lyase derived from Bacillus, particularly B. licheniformis or B. agaradhaerens, or a variant derived of any of these, e.g. as described in US 6124127 , WO 99/27083 , WO 99/27084 , WO 02/006442 , WO 02/092741 , WO 03/095638 , Commercially available pectate lyases are XPectTM; PectawashTM and PectawayTM (Novozymes A/S).
- Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
- the mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens.
- Suitable mannanases are described in WO 1999/064619. A commercially available mannanase is MannawayTM (Novozymes A/S).
- 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, Thielavia terrestris, Myceliophthora thermophila, and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691 ,178, US 5,776,757, WO 89/09259, WO 96/029397, and WO 98/012307.
- cellulases include CelluzymeTM, CarezymeTM, CellucleanTM, EndolaseTM, RenozymeTM (Novozymes A/S), ClazinaseTM and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (Kao Corporation).
- the use according to the first aspect of the present invention is substantially free of hydrolytic enzyme selected from the group consisting of deoxyribonuclease, hexosaminidase or combination thereof.
- substantially free means that there is no intentionally added deoxyribonuclease and/or hexosaminidase hydrolytic enzyme in the composition, preferably their amount is 0 wt.%. It is highly preferred that all the hydrolytic enzyme is a detersive hydrolytic enzyme.
- present invention discloses the use of an alkaline source in a detergent composition for treating textile article for inactivation of microorganisms.
- alkaline source includes but is not limited to alkali metal or alkaline earth metal salts of carbonate, bicarbonate, silicate, metasilicates or combination thereof.
- the alkaline source is a carbonate.
- preferred carbonates are the alkaline earth and alkali metal carbonates, including sodium carbonate, bicarbonate and sesqui-carbonate or mixtures thereof.
- the carbonate and bicarbonate preferably have an amorphous structure.
- the carbonate and bicarbonates are coated with coating materials.
- the particles of carbonate and bicarbonate can have a mean particle size of 250 micrometers or greater, preferably 500 micrometers or greater.
- the carbonate salt of alkali metal and/or alkaline earth metal are present in the detergent composition of the present invention in an amount ranging from 10 wt.% to 35 wt.%.
- the term carbonates include bicarbonates and sesquicarbonates.
- the detergent composition according to the present invention comprises from 10 wt.% to 40 wt.% carbonate alkaline source.
- the detergent composition comprises at least 12 wt.% carbonate alkaline source based on the weight of the detergent composition, still preferably at least 15 wt.%, still preferably at least 18 wt.%, most preferably at least 20 wt.%, but typically not more than 35 wt.%, still preferably not more than 30 wt.%, more preferably not more than 25 wt.% carbonate alkaline source in the solid detergent composition.
- the alkalinity system may include other components, such as a silicate.
- a silicate is present in the detergent composition in an amount ranging from 1 wt.% to 10wt.%.
- Suitable silicates include the water-soluble sodium silicates with an S1O2: Na 2 0 ratio of from 1.0 to 2.8, with ratios of from 1.6 to 2.0 being preferred, and 2.0 ratio being most preferred.
- the silicates may be in the form of either the anhydrous salt or a hydrated salt.
- Sodium silicate with an S1O2: Na 2 0 ratio of 2.0 is the most preferred silicate.
- the silicates Preferably have an amorphous structure. Alkali metal persilicates or metasilicates are also suitable sources of silicate herein.
- Preferred crystalline layered silicates for use herein have the general formula NaMSix02x+l.yH20 wherein M is sodium or hydrogen, x is a number from 1.9 to 4 and y is a number from 0 to 20.
- Crystalline layered sodium silicates of this type are disclosed in EP-A- 0164514 and methods for their preparation are disclosed in DE-A-3417649 and DE-A- 3742043.
- x in the general formula above preferably has a value of 2, 3 or 4 and is preferably 2.
- the most preferred material is b-I ⁇ ShOs, available from Hoechst AG as NaSKS-6.
- the detergent composition according to the present invention comprises from 10 wt.% to 40 wt.% alkaline source.
- the detergent composition comprises at least 12 wt.% alkaline source based on the weight of the detergent composition, still preferably at least 15 wt.%, still preferably at least 18 wt.%, most preferably at least 20 wt.%, but typically not more than 35 wt.%, still preferably not more than 30 wt.%, more preferably not more than 25 wt.% alkaline source in the detergent composition.
- the use according to the first aspect of the present invention involves inactivating the microorganisms in a wash liquor prepared by addition of the solid detergent composition in water, wherein the alkaline source is present at a concentration from 120 ppm to 2500 ppm.
- concentration is at least 150 ppm, still preferably at least 200 ppm, still preferably at least 500 ppm, most preferably at least 600 ppm, but typically not more than 1800ppm, still preferably not more than 1600 ppm, more preferably not more than 1500 ppm and most preferably not more than 1000 ppm in the wash liquor.
- the alkaline source is selected from sodium carbonate, sodium silicate or a combination of sodium carbonate and sodium silicate.
- alkyl benzene sulphonate surfactant selected from the group consisting of protease, lipase, cellulase, amylase, mannanase or combinations thereof, and alkaline source according to the present invention can be employed in any suitable detergent composition having a pH from 10 to 13.
- the pH of the composition is from 10.2 to 13, still preferably from 10.5 to 13, still preferably from 10.2 to 12, more preferably from 10.2 to 11, still more preferably 10.2 to 11 and most preferably from 10.5 to about 11 , as measured at 25°C and 10% aqueous concentration in deionized water.
- the pH of the composition can be adjusted using pH modifying ingredients known in the art.
- the detergent composition must be suitable for use with a soft surface, preferably textile article.
- the detergent composition may be in any form such as solid, granular, powder, or in the form of a unit dose product where the solid detergent composition is at least partially enclosed in a water-soluble film.
- the solid detergent composition in particulate form may include agglomerate, a spray-dried powder, an extrudate, a flake, a needle, a noodle, a bead, or any combination thereof.
- the composition may be in compacted-particulate form, such as in the form of a tablet or bar.
- composition may be some other unit dose form, such as a pouch; typically being at least partially, preferably essentially completely, enclosed by a water-soluble film, such as polyvinyl alcohol.
- the composition is in free-flowing particulate form; by free- flowing particulate form, it is typically meant that the composition is in the form of separate discrete particles.
- the solid composition may be made by any suitable method including agglomeration, spray-drying, extrusion, mixing, dry-mixing, liquid spray-on, roller compaction, spheronisation, tabletting or any combination thereof.
- the solid detergent composition typically has a bulk density of from 450 g/l to 1 ,000 g/l, preferred low bulk density detergent compositions have a bulk density of from 550 g/l to 650 g/l and preferred high bulk density detergent compositions have a bulk density of from 750 g/l to 900 g/l.
- the composition is typically contacted with water to give a wash liquor having a pH of from 8 to 13, preferably from 8.5 to less than 11.
- compositions may be used only to deliver alkyl benzene sulphonate surfactant, hydrolytic enzyme and an alkaline source during the laundering process, or they may have additional functions such as cleaning.
- the first aspect of the present invention discloses a use of a combination of alkyl benzene sulphonate, hydrolytic enzyme selected from the group consisting of protease, lipase, cellulase, amylase, mannanase or combinations thereof and an alkaline source in a solid detergent composition having a pH of from 10 to 13 as measured at 25°C and 10% aqueous concentration in deionised water for inactivating microorganism on a textile surface during a laundering process.
- inactivation is understood in the context of the present invention to be an activity against at least one virus (antiviral efficacy) or bacteria species.
- a 1 to 3 log reduction is preferred, a log reduction of 3 to 5 is most preferred, whereas a log reduction of less than 1 is least preferred, for a particular contact time, generally ranging from 15 seconds to 5 minutes, more preferably the contact time ranges from 15 seconds to at least one hour.
- a highly preferred antimicrobial composition exhibits a 3 to 5 log reduction against a broad spectrum of microorganisms in a short contact time.
- Detersive surfactants utilized can be of the anionic, nonionic, zwitterionic, ampholytic or cationic type or can comprise compatible mixtures of these types. More preferably surfactants are selected from the group consisting of anionic, nonionic, cationic surfactants and mixtures thereof.
- Detergent surfactants useful herein are described in U.S. Patent 3,664,961, Norris, issued May 23, 1972, U.S. Patent 3,919,678, Laughlin et al., issued December 30, 1975 , U.S. Patent 4,222,905, Cockrell, issued September 16, 1980 , and in U.S. Patent 4,239,659, Murphy, issued December 16, 1980 . Anionic and nonionic surfactants are preferred.
- Fluorescent Agent These materials may be particularly useful in liquid laundry detergent compositions for hand wash.
- the composition preferably comprises a fluorescent agent (optical brightener).
- Preferred fluorescers are: sodium 2 (4-styryl-3-sulfophenyl)-2H-napthol[1 ,2-d]triazole, disodium 4,4'-bis ⁇ [(4-anilino-6-(N methyl-N-2 hydroxyethyl) amino 1 ,3,5-triazin-2- yl)]amino ⁇ stilbene-2-2' disulfonate, disodium 4,4'-bis ⁇ [(4-anilino-6-morpholino-1 ,3,5-triazin-2- yl)]amino ⁇ stilbene-2-2' disulfonate, and disodium 4,4'-bis(2-sulfostyryl)biphenyl.
- the shading dye chromophore is most preferably selected from mono-azo, bis-azo, anthraquinone, and azine.
- Such bleaching agents include hydrogen peroxide, or substances that can generate perhydroxyl radical, such as inorganic or organic peroxides.
- the peroxygen bleach compound or hydrogen peroxide must be activated.
- the solid detergent composition preferably includes a bleach.
- the bleach preferably has a peroxide source. Still preferably the bleach is present along with a bleach activator.
- Example 1 Evaluation of the virus inactivation using different detergent compositions.
- the virucidal efficacy test was set up with the three concentrations of test product solution as described above and a 60 minute contact time was given.
- the test temperature was maintained at 27°C and the interfering condition was Clean with low levels of organic soil.
- the virucidal efficacy of the test composition was tested for Adeno virus, Murine Norovirus, Poliovirus & bovine coronavirus and the final virucidal efficacy is expressed as log reduction.
- alkaline source is sodium carbonate.
- Example 2 Evaluation of the bacterial inactivation using different detergent compositions
- a detergent composition according to Table 3 was diluted using sterilized hard water according to the EN1276 standards described below to prepare an aqueous liquor with concentrations of 7.5 grams/litre. Table 3
- the aqueous liquor as described above was prepared from the detergent composition of Ex 3 and was tested for antibacterial efficacy in accordance to the European Standard method EN 1276 test.
- the antibacterial efficacy test was set up with a 7.5 grams/Litre concentration test product solution as described above and a 60 minutes contact time was provided. The test temperature was maintained at 27°C and the interfering condition was clean with low levels of organic soil. The antibacterial efficacy of the test composition was tested using Staphylococcus aureus (S. aureus), Enterococcus hirae (E. hirae) and the final antibacterial efficacy was expressed as log reduction. The test results are provided in Table 4.
Abstract
Description
Claims
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Family Cites Families (141)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US2220099A (en) | 1934-01-10 | 1940-11-05 | Gen Aniline & Flim Corp | Sulphonic acids |
US2477383A (en) | 1946-12-26 | 1949-07-26 | California Research Corp | Sulfonated detergent and its method of preparation |
GB1296839A (en) | 1969-05-29 | 1972-11-22 | ||
US3664961A (en) | 1970-03-31 | 1972-05-23 | Procter & Gamble | Enzyme detergent composition containing coagglomerated perborate bleaching agent |
GB1372034A (en) | 1970-12-31 | 1974-10-30 | Unilever Ltd | Detergent compositions |
US3919678A (en) | 1974-04-01 | 1975-11-11 | Telic Corp | Magnetic field generation apparatus |
US4222905A (en) | 1978-06-26 | 1980-09-16 | The Procter & Gamble Company | Laundry detergent compositions having enhanced particulate soil removal performance |
US4239659A (en) | 1978-12-15 | 1980-12-16 | The Procter & Gamble Company | Detergent compositions containing nonionic and cationic surfactants, the cationic surfactant having a long alkyl chain of from about 20 to about 30 carbon atoms |
DK187280A (en) | 1980-04-30 | 1981-10-31 | Novo Industri As | RUIT REDUCING AGENT FOR A COMPLETE LAUNDRY |
GR76189B (en) | 1981-07-13 | 1984-08-03 | Procter & Gamble | |
DE3413571A1 (en) | 1984-04-11 | 1985-10-24 | Hoechst Ag, 6230 Frankfurt | USE OF CRYSTALLINE LAYERED SODIUM SILICATES FOR WATER SOFTENING AND METHOD FOR WATER SOFTENING |
DE3417649A1 (en) | 1984-05-12 | 1985-11-14 | Hoechst Ag, 6230 Frankfurt | METHOD FOR PRODUCING CRYSTALLINE SODIUM SILICATES |
DE3684398D1 (en) | 1985-08-09 | 1992-04-23 | Gist Brocades Nv | LIPOLYTIC ENZYMES AND THEIR USE IN DETERGENTS. |
JPS6474992A (en) | 1987-09-16 | 1989-03-20 | Fuji Oil Co Ltd | Dna sequence, plasmid and production of lipase |
DE3742043A1 (en) | 1987-12-11 | 1989-06-22 | Hoechst Ag | METHOD FOR PRODUCING CRYSTALLINE SODIUM LAYER SILICATES |
WO1989006270A1 (en) | 1988-01-07 | 1989-07-13 | Novo-Nordisk A/S | Enzymatic detergent |
DK6488D0 (en) | 1988-01-07 | 1988-01-07 | Novo Industri As | ENZYMES |
GB8803036D0 (en) | 1988-02-10 | 1988-03-09 | Unilever Plc | Liquid detergents |
JP3079276B2 (en) | 1988-02-28 | 2000-08-21 | 天野製薬株式会社 | Recombinant DNA, Pseudomonas sp. Containing the same, and method for producing lipase using the same |
EP0406314B1 (en) | 1988-03-24 | 1993-12-01 | Novo Nordisk A/S | A cellulase preparation |
US5776757A (en) | 1988-03-24 | 1998-07-07 | Novo Nordisk A/S | Fungal cellulase composition containing alkaline CMC-endoglucanase and essentially no cellobiohydrolase and method of making thereof |
GB8821049D0 (en) * | 1988-09-08 | 1988-10-05 | Health Lab Service Board | Method & composition for treatment & prevention of viral infections |
CA2001927C (en) | 1988-11-03 | 1999-12-21 | Graham Thomas Brown | Aluminosilicates and detergent compositions |
GB8915658D0 (en) | 1989-07-07 | 1989-08-23 | Unilever Plc | Enzymes,their production and use |
EP0493398B1 (en) | 1989-08-25 | 1999-12-08 | Henkel Research Corporation | Alkaline proteolytic enzyme and method of production |
EP0528828B2 (en) | 1990-04-14 | 1997-12-03 | Genencor International GmbH | Alkaline bacillus lipases, coding dna sequences therefor and bacilli which produce these lipases |
US5869438A (en) | 1990-09-13 | 1999-02-09 | Novo Nordisk A/S | Lipase variants |
KR930702514A (en) | 1990-09-13 | 1993-09-09 | 안네 제케르 | Lipase variant |
US5292796A (en) | 1991-04-02 | 1994-03-08 | Minnesota Mining And Manufacturing Company | Urea-aldehyde condensates and melamine derivatives comprising fluorochemical oligomers |
EP0511456A1 (en) | 1991-04-30 | 1992-11-04 | The Procter & Gamble Company | Liquid detergents with aromatic borate ester to inhibit proteolytic enzyme |
PL170474B1 (en) | 1991-04-30 | 1996-12-31 | Procter & Gamble | Liquid detergent composition |
EP0583339B1 (en) | 1991-05-01 | 1998-07-08 | Novo Nordisk A/S | Stabilized enzymes and detergent compositions |
US5340735A (en) | 1991-05-29 | 1994-08-23 | Cognis, Inc. | Bacillus lentus alkaline protease variants with increased stability |
DK28792D0 (en) | 1992-03-04 | 1992-03-04 | Novo Nordisk As | NEW ENZYM |
DK88892D0 (en) | 1992-07-06 | 1992-07-06 | Novo Nordisk As | CONNECTION |
ES2334590T3 (en) | 1992-07-23 | 2010-03-12 | Novozymes A/S | ALFA-AMYLASE MUTANT, DETERGENT AND WASHING AGENT OF VAJILLA. |
CA2106609A1 (en) * | 1992-09-28 | 1994-03-29 | Irene Yeatman Aldridge | Proteases to inhibit and remove biofilm |
DE69415659T3 (en) | 1993-02-11 | 2010-05-12 | Genencor International, Inc., Palo Alto | OXIDATIVE STABLE ALPHA AMYLASE |
PL306812A1 (en) | 1993-04-27 | 1995-04-18 | Gist Brocades Nv | Novel lipase variants suitable for use in detergents |
DK52393D0 (en) | 1993-05-05 | 1993-05-05 | Novo Nordisk As | |
JP2859520B2 (en) | 1993-08-30 | 1999-02-17 | ノボ ノルディスク アクティーゼルスカブ | Lipase, microorganism producing the same, method for producing lipase, and detergent composition containing lipase |
WO1995010603A1 (en) | 1993-10-08 | 1995-04-20 | Novo Nordisk A/S | Amylase variants |
JPH07143883A (en) | 1993-11-24 | 1995-06-06 | Showa Denko Kk | Lipase gene and mutant lipase |
WO1995022615A1 (en) | 1994-02-22 | 1995-08-24 | Novo Nordisk A/S | A method of preparing a variant of a lipolytic enzyme |
DE69535736T2 (en) | 1994-02-24 | 2009-04-30 | Henkel Ag & Co. Kgaa | IMPROVED ENZYMES AND DETERGENTS CONTAINED THEREOF |
WO1995030744A2 (en) | 1994-05-04 | 1995-11-16 | Genencor International Inc. | Lipases with improved surfactant resistance |
WO1995035381A1 (en) | 1994-06-20 | 1995-12-28 | Unilever N.V. | Modified pseudomonas lipases and their use |
WO1996000292A1 (en) | 1994-06-23 | 1996-01-04 | Unilever N.V. | Modified pseudomonas lipases and their use |
BE1008998A3 (en) | 1994-10-14 | 1996-10-01 | Solvay | Lipase, microorganism producing the preparation process for the lipase and uses thereof. |
AR000862A1 (en) | 1995-02-03 | 1997-08-06 | Novozymes As | VARIANTS OF A MOTHER-AMYLASE, A METHOD TO PRODUCE THE SAME, A DNA STRUCTURE AND A VECTOR OF EXPRESSION, A CELL TRANSFORMED BY SUCH A DNA STRUCTURE AND VECTOR, A DETERGENT ADDITIVE, DETERGENT COMPOSITION, A COMPOSITION FOR AND A COMPOSITION FOR THE ELIMINATION OF |
JPH08228778A (en) | 1995-02-27 | 1996-09-10 | Showa Denko Kk | New lipase gene and production of lipase using the same |
CN1182451A (en) | 1995-03-17 | 1998-05-20 | 诺沃挪第克公司 | Novel endoglucanases |
KR100380006B1 (en) | 1995-05-05 | 2004-05-27 | 노보자임스 에이/에스 | Protease variants and compositions |
JP4307549B2 (en) | 1995-07-14 | 2009-08-05 | ノボザイムス アクティーゼルスカブ | Modified enzyme with lipolytic activity |
ATE267248T1 (en) | 1995-08-11 | 2004-06-15 | Novozymes As | NOVEL LIPOLYTIC ENZYMES |
US5763385A (en) | 1996-05-14 | 1998-06-09 | Genencor International, Inc. | Modified α-amylases having altered calcium binding properties |
CN100362100C (en) | 1996-09-17 | 2008-01-16 | 诺沃奇梅兹有限公司 | Cellulase variants |
KR100591553B1 (en) | 1996-11-04 | 2006-06-19 | 노보자임스 에이/에스 | Subtilase variants and composition |
JP4044143B2 (en) | 1996-11-04 | 2008-02-06 | ノボザイムス アクティーゼルスカブ | Subtilase variants and compositions |
WO1998050512A1 (en) * | 1997-05-06 | 1998-11-12 | The Procter & Gamble Company | Laundry and cleaning compositions containing hexosaminidase enzymes |
TR200000883T2 (en) | 1997-07-21 | 2000-07-21 | The Procter & Gamble Company | Improved alkylbenzenesulfonate surfactants |
PH11998001775B1 (en) | 1997-07-21 | 2004-02-11 | Procter & Gamble | Improved alkyl aryl sulfonate surfactants |
AU728580B2 (en) | 1997-07-21 | 2001-01-11 | Procter & Gamble Company, The | Improved processes for making alkylbenzenesulfonate surfactants and products thereof |
ZA986445B (en) | 1997-07-21 | 1999-01-21 | Procter & Gamble | Processes for making alkylbenzenesulfonate surfactants from alcohols and products thereof |
DE69814870T2 (en) | 1997-07-21 | 2004-05-06 | The Procter & Gamble Company, Cincinnati | DETERGENT COMPOSITIONS WITH CRYSTAL INHIBITANT SURFACES |
CA2297010C (en) | 1997-07-21 | 2003-04-15 | Kevin Lee Kott | Cleaning products comprising improved alkylarylsulfonate surfactants prepared via vinylidene olefins and processes for preparation thereof |
TR200000362T2 (en) | 1997-08-08 | 2000-07-21 | The Procter & Gamble Company | Processes developed for making surfactants by floating separation and products of these processes. |
CN1148444C (en) | 1997-08-29 | 2004-05-05 | 诺沃奇梅兹有限公司 | Protease variants and compositions |
ATE423192T1 (en) | 1997-10-13 | 2009-03-15 | Novozymes As | MUTANTS OF ALPHA-AMYLASE |
US6124127A (en) | 1997-11-24 | 2000-09-26 | Novo Nordisk A/S | Pectate lyase |
WO1999027083A1 (en) | 1997-11-24 | 1999-06-03 | Novo Nordisk A/S | PECTIN DEGRADING ENZYMES FROM $i(BACILLUS LICHENIFORMIS) |
BR9815007A (en) | 1997-11-24 | 2000-10-03 | Novo Nordisk As | Pectate lyase, isolated polynucleotide molecule encoding a polypeptide, expression vector, cultured cell into which an expression vector was introduced, isolated and fused polypeptides, enzyme preparation, processes for producing a polypeptide showing pectate lyase activity, for the cleaning of a hard surface, for the treatment of fabrics by machine, to improve the properties of cellulosic fibers, yarn, woven or nonwoven fabric, for the degradation or modification of plant material, for preparing animal food, and for processing wine or juice, isolated enzyme showing pectate lyase activity, and detergent composition |
AU3247699A (en) | 1998-02-17 | 1999-09-06 | Novo Nordisk A/S | Lipase variant |
AU755850B2 (en) | 1998-06-10 | 2002-12-19 | Novozymes A/S | Novel mannanases |
CZ20011308A3 (en) | 1998-10-20 | 2002-03-13 | The Procter & Gamble Company | Detergent compositions containing modified alkylbenzenesulfonates |
JP2002527605A (en) | 1998-10-20 | 2002-08-27 | ザ、プロクター、エンド、ギャンブル、カンパニー | Laundry detergent containing improved alkylbenzene sulfonate |
KR100748061B1 (en) | 1998-12-04 | 2007-08-09 | 노보자임스 에이/에스 | Cutinase variants |
WO2000060063A1 (en) | 1999-03-31 | 2000-10-12 | Novozymes A/S | Lipase variant |
EP1065265B1 (en) | 1999-06-30 | 2008-09-24 | Kao Corporation | Germicidal detergent composition |
EP2206786A1 (en) | 1999-08-31 | 2010-07-14 | Novozymes A/S | Novel proteases and variants thereof |
EP1244779B1 (en) | 1999-12-15 | 2014-05-07 | Novozymes A/S | Subtilase variants having an improved wash performance on egg stains |
CN101532001A (en) | 2000-03-08 | 2009-09-16 | 诺维信公司 | Variants with altered properties |
CN1426463A (en) | 2000-06-02 | 2003-06-25 | 诺维信公司 | Cutinase variants |
EP1305408B1 (en) | 2000-07-19 | 2009-01-21 | Novozymes A/S | Cell-wall degrading enzyme variants |
EP1370648A2 (en) | 2000-08-01 | 2003-12-17 | Novozymes A/S | Alpha-amylase mutants with altered properties |
CN1337553A (en) | 2000-08-05 | 2002-02-27 | 李海泉 | Underground sightseeing amusement park |
WO2002016547A2 (en) | 2000-08-21 | 2002-02-28 | Novozymes A/S | Subtilase enzymes |
CA2432329C (en) | 2001-02-07 | 2012-04-10 | Novozymes A/S | Lipase variants |
EP1389228B1 (en) | 2001-05-14 | 2009-03-11 | Novozymes A/S | Detergent compositions comprising bacillus subtilis pectate lyases |
DK200101090A (en) | 2001-07-12 | 2001-08-16 | Novozymes As | Subtilase variants |
DE10162728A1 (en) | 2001-12-20 | 2003-07-10 | Henkel Kgaa | New alkaline protease from Bacillus gibsonii (DSM 14393) and washing and cleaning agents containing this new alkaline protease |
MXPA04011011A (en) | 2002-05-14 | 2005-02-14 | Novozymes As | Pectate lyase variants. |
US20060228791A1 (en) | 2002-06-26 | 2006-10-12 | Novozymes A/S | Subtilases and subtilase variants having altered immunogenicity |
TWI319007B (en) | 2002-11-06 | 2010-01-01 | Novozymes As | Subtilase variants |
EP1625208A4 (en) | 2003-05-12 | 2006-10-18 | Genencor Int | Novel lipolytic enzyme lip2 |
EP1625202A4 (en) | 2003-05-12 | 2010-10-20 | Genencor Int | Novel lipolytic enzyme lip1 |
US7511005B2 (en) | 2003-05-12 | 2009-03-31 | Danisco Us Inc., Genencor Division | Lipolytic enzyme elip |
GB0314210D0 (en) | 2003-06-18 | 2003-07-23 | Unilever Plc | Laundry treatment compositions |
CN102994486A (en) | 2003-10-23 | 2013-03-27 | 诺维信公司 | Protease with improved stability in detergents |
EP1694847B1 (en) | 2003-11-19 | 2012-06-13 | Danisco US Inc. | Serine proteases, nucleic acids encoding serine enzymes and vectors and host cells incorporating same |
GB0420203D0 (en) | 2004-09-11 | 2004-10-13 | Unilever Plc | Laundry treatment compositions |
ES2326901T3 (en) | 2004-09-23 | 2009-10-21 | Unilever N.V. | COLADA TREATMENT COMPOSITIONS. |
GB0421145D0 (en) | 2004-09-23 | 2004-10-27 | Unilever Plc | Laundry treatment compositions |
DE102004052007B4 (en) | 2004-10-25 | 2007-12-06 | Müller Weingarten AG | Drive system of a forming press |
MX2007007494A (en) | 2004-12-23 | 2007-08-15 | Novozymes As | Alpha-amylase variants. |
EP2385112B1 (en) | 2005-07-08 | 2016-11-30 | Novozymes A/S | Subtilase variants |
AU2006299783B2 (en) | 2005-10-12 | 2012-06-14 | Danisco Us Inc. | Use and production of storage-stable neutral metalloprotease |
ES2628940T3 (en) | 2006-01-23 | 2017-08-04 | Novozymes A/S | Lipase variants |
EP1976967A2 (en) | 2006-01-23 | 2008-10-08 | The Procter and Gamble Company | Detergent compositions |
ZA200804295B (en) | 2006-08-10 | 2009-09-30 | Unilever Plc | Shading composition |
CA2673313A1 (en) * | 2006-12-18 | 2008-12-04 | Amcol International | Virus-interacting layered phyllosilicates and methods of use |
PL2192169T3 (en) | 2007-01-19 | 2012-10-31 | Procter & Gamble | Laundry care composition comprising a whitening agents for cellulosic substrates |
MX2009012393A (en) | 2007-05-18 | 2009-12-01 | Unilever Nv | Triphenodioxazine dyes. |
RU2009149406A (en) | 2007-05-30 | 2011-07-10 | ДАНИСКО ЮЭс, ИНК., ДЖЕНЕНКОР ДИВИЖН (US) | VARIANTS OF ALFA AMILASE WITH HIGHER LEVELS OF PRODUCTION IN THE PROCESSES OF FERMENTATION |
DE102007038031A1 (en) | 2007-08-10 | 2009-06-04 | Henkel Ag & Co. Kgaa | Agents containing proteases |
US8293174B2 (en) * | 2007-10-17 | 2012-10-23 | American Sterilizer Company | Prion deactivating composition and methods of using same |
WO2009109500A1 (en) | 2008-02-29 | 2009-09-11 | Novozymes A/S | Polypeptides having lipase activity and polynucleotides encoding same |
CN102015989B (en) | 2008-05-02 | 2012-07-04 | 荷兰联合利华有限公司 | Reduced spotting granules |
CN102037115B (en) | 2008-05-20 | 2012-10-03 | 荷兰联合利华有限公司 | Shading composition |
JP2012508031A (en) | 2008-11-11 | 2012-04-05 | ダニスコ・ユーエス・インク | Protease containing one or more combination mutations |
DE102008062772A1 (en) | 2008-12-18 | 2010-06-24 | Henkel Ag & Co. Kgaa | Disinfecting viruses on textiles and hard surfaces |
MY159509A (en) | 2009-03-05 | 2017-01-13 | Unilever Plc | Dye radical initiators |
CN102348769A (en) | 2009-03-12 | 2012-02-08 | 荷兰联合利华有限公司 | Dye-polymers formulations |
WO2010148624A1 (en) | 2009-06-26 | 2010-12-29 | Unilever Plc | Dye polymers |
JP5947213B2 (en) | 2009-09-25 | 2016-07-06 | ノボザイムス アクティーゼルスカブ | Use of protease variants |
RU2639534C2 (en) | 2009-09-25 | 2017-12-21 | Новозимс А/С | Application of protease versions |
CN113186178A (en) | 2010-02-10 | 2021-07-30 | 诺维信公司 | Variants and compositions comprising variants with high stability in the presence of chelating agents |
US20120101018A1 (en) | 2010-10-22 | 2012-04-26 | Gregory Scot Miracle | Bis-azo colorants for use as bluing agents |
WO2011011799A2 (en) | 2010-11-12 | 2011-01-27 | The Procter & Gamble Company | Thiophene azo dyes and laundry care compositions containing the same |
US20140206026A1 (en) | 2011-06-30 | 2014-07-24 | Novozymes A/S | Method for Screening Alpha-Amylases |
JP6204352B2 (en) | 2011-06-30 | 2017-09-27 | ノボザイムス アクティーゼルスカブ | α-Amylase mutant |
CN103007258A (en) * | 2011-09-22 | 2013-04-03 | 安淇生物控释技术(苏州)有限公司 | Medical composition containing fish serine protease and antibacterial compound, and uses thereof |
CA2867361C (en) | 2012-03-19 | 2017-07-25 | Milliken & Company | Carboxylate dyes |
EP2834340B1 (en) | 2012-04-03 | 2016-06-29 | The Procter and Gamble Company | Laundry detergent composition comprising water-soluble phthalocyanine compound |
WO2013170128A1 (en) * | 2012-05-11 | 2013-11-14 | Smith & Nephew, Inc. | Use of seaprose to remove bacterial biofilm |
CN108834403B (en) * | 2016-01-22 | 2022-03-11 | 诺瓦制药研究(澳大利亚)有限公司 | Disinfecting compositions |
WO2017207770A1 (en) * | 2016-06-03 | 2017-12-07 | Novozymes A/S | Cleaning compositions comprising enzymes |
CA3031866A1 (en) * | 2016-07-27 | 2018-02-01 | Smith & Nephew, Inc. | Use of thermolysin to reduce or eliminate bacterial biofilms from surfaces |
WO2018161899A1 (en) * | 2017-03-06 | 2018-09-13 | Novozymes A/S | Use of one or more enzymes in preventing, inhibiting or reducing microbe growth on a surface |
CN107267322A (en) * | 2017-07-09 | 2017-10-20 | 深圳市美益洁生物科技有限公司 | Degerming cleaning effervescent tablet of feeding bottle biology enzyme and its preparation method and application |
JP2019147778A (en) * | 2018-02-28 | 2019-09-05 | 国立大学法人秋田大学 | Antivirus agent |
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