EP2596089B1 - Detergent compositions comprising biosurfactant and lipase - Google Patents
Detergent compositions comprising biosurfactant and lipase Download PDFInfo
- Publication number
- EP2596089B1 EP2596089B1 EP11729626.9A EP11729626A EP2596089B1 EP 2596089 B1 EP2596089 B1 EP 2596089B1 EP 11729626 A EP11729626 A EP 11729626A EP 2596089 B1 EP2596089 B1 EP 2596089B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- biosurfactant
- enzyme
- lipase
- cleaning
- bacterial
- 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.)
- Active
Links
- 239000003876 biosurfactant Substances 0.000 title claims description 52
- 102000004882 Lipase Human genes 0.000 title claims description 48
- 108090001060 Lipase Proteins 0.000 title claims description 48
- 239000000203 mixture Substances 0.000 title claims description 35
- 239000004367 Lipase Substances 0.000 title description 39
- 235000019421 lipase Nutrition 0.000 title description 39
- 239000003599 detergent Substances 0.000 title description 10
- 102000004190 Enzymes Human genes 0.000 claims description 53
- 108090000790 Enzymes Proteins 0.000 claims description 53
- 230000001580 bacterial effect Effects 0.000 claims description 28
- 238000004140 cleaning Methods 0.000 claims description 24
- 239000004094 surface-active agent Substances 0.000 claims description 23
- 150000002016 disaccharides Chemical group 0.000 claims description 8
- FCBUKWWQSZQDDI-UHFFFAOYSA-N rhamnolipid Chemical group CCCCCCCC(CC(O)=O)OC(=O)CC(CCCCCCC)OC1OC(C)C(O)C(O)C1OC1C(O)C(O)C(O)C(C)O1 FCBUKWWQSZQDDI-UHFFFAOYSA-N 0.000 claims description 8
- 239000000758 substrate Substances 0.000 claims description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 8
- 239000002253 acid Chemical group 0.000 claims description 7
- 238000000034 method Methods 0.000 claims description 6
- HVCOBJNICQPDBP-UHFFFAOYSA-N 3-[3-[3,5-dihydroxy-6-methyl-4-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid;hydrate Chemical compound O.OC1C(OC(CC(=O)OC(CCCCCCC)CC(O)=O)CCCCCCC)OC(C)C(O)C1OC1C(O)C(O)C(O)C(C)O1 HVCOBJNICQPDBP-UHFFFAOYSA-N 0.000 claims description 5
- 229930186217 Glycolipid Natural products 0.000 claims description 5
- 125000002252 acyl group Chemical group 0.000 claims description 2
- 238000005406 washing Methods 0.000 claims description 2
- SHZGCJCMOBCMKK-JFNONXLTSA-N L-rhamnopyranose Chemical group C[C@@H]1OC(O)[C@H](O)[C@H](O)[C@H]1O SHZGCJCMOBCMKK-JFNONXLTSA-N 0.000 claims 1
- 229940088598 enzyme Drugs 0.000 description 51
- 108010064785 Phospholipases Proteins 0.000 description 19
- 102000015439 Phospholipases Human genes 0.000 description 19
- 230000000694 effects Effects 0.000 description 16
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 description 15
- 230000002538 fungal effect Effects 0.000 description 13
- 241000894006 Bacteria Species 0.000 description 11
- 108091005804 Peptidases Proteins 0.000 description 8
- 239000004365 Protease Substances 0.000 description 8
- 102000013142 Amylases Human genes 0.000 description 7
- 108010065511 Amylases Proteins 0.000 description 7
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 7
- 235000019418 amylase Nutrition 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 244000005700 microbiome Species 0.000 description 7
- 239000002689 soil Substances 0.000 description 7
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 6
- 239000004382 Amylase Substances 0.000 description 5
- 239000004744 fabric Substances 0.000 description 5
- 238000009472 formulation Methods 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 241000233866 Fungi Species 0.000 description 4
- 108020002496 Lysophospholipase Proteins 0.000 description 4
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 4
- 238000012512 characterization method Methods 0.000 description 4
- 239000004615 ingredient Substances 0.000 description 4
- 230000000813 microbial effect Effects 0.000 description 4
- ZTOKUMPYMPKCFX-CZNUEWPDSA-N (E)-17-[(2R,3R,4S,5S,6R)-6-(acetyloxymethyl)-3-[(2S,3R,4S,5S,6R)-6-(acetyloxymethyl)-3,4,5-trihydroxyoxan-2-yl]oxy-4,5-dihydroxyoxan-2-yl]oxyoctadec-9-enoic acid Chemical compound OC(=O)CCCCCCC/C=C/CCCCCCC(C)O[C@@H]1O[C@H](COC(C)=O)[C@@H](O)[C@H](O)[C@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](COC(C)=O)O1 ZTOKUMPYMPKCFX-CZNUEWPDSA-N 0.000 description 3
- 241000193830 Bacillus <bacterium> Species 0.000 description 3
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- PPMPLIBYTIWXPG-MSJADDGSSA-N L-rhamnosyl-3-hydroxydecanoyl-3-hydroxydecanoic acid Chemical compound CCCCCCCC(CC(O)=O)OC(=O)CC(CCCCCCC)O[C@@H]1O[C@@H](C)[C@H](O)[C@@H](O)[C@H]1O PPMPLIBYTIWXPG-MSJADDGSSA-N 0.000 description 3
- 235000015278 beef Nutrition 0.000 description 3
- 239000007844 bleaching agent Substances 0.000 description 3
- 150000003904 phospholipids Chemical class 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 238000012552 review Methods 0.000 description 3
- 235000014469 Bacillus subtilis Nutrition 0.000 description 2
- 229920000742 Cotton Polymers 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 102220644676 Galectin-related protein_D96L_mutation Human genes 0.000 description 2
- 102100037611 Lysophospholipase Human genes 0.000 description 2
- 102000011720 Lysophospholipase Human genes 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108090000553 Phospholipase D Proteins 0.000 description 2
- 102000011420 Phospholipase D Human genes 0.000 description 2
- 241000168225 Pseudomonas alcaligenes Species 0.000 description 2
- 241000589540 Pseudomonas fluorescens Species 0.000 description 2
- 241000589774 Pseudomonas sp. Species 0.000 description 2
- 241000589614 Pseudomonas stutzeri Species 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- 241000223258 Thermomyces lanuginosus Species 0.000 description 2
- 102000014384 Type C Phospholipases Human genes 0.000 description 2
- 108010079194 Type C Phospholipases Proteins 0.000 description 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 2
- 229940025131 amylases Drugs 0.000 description 2
- -1 cellobiose lipid Chemical class 0.000 description 2
- 230000000593 degrading effect Effects 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 238000004851 dishwashing Methods 0.000 description 2
- 150000002149 estolides Chemical class 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 125000001924 fatty-acyl group Chemical group 0.000 description 2
- 238000005187 foaming Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 108010020132 microbial serine proteinases Proteins 0.000 description 2
- 239000002304 perfume Substances 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 239000008107 starch Substances 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- UJEADPSEBDCWPS-SGJODSJKSA-N (2R,3R)-1-[(3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]butane-1,2,3,4-tetrol Chemical class C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)C([C@H](O)[C@H](O)CO)O UJEADPSEBDCWPS-SGJODSJKSA-N 0.000 description 1
- PORPENFLTBBHSG-MGBGTMOVSA-N 1,2-dihexadecanoyl-sn-glycerol-3-phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(O)=O)OC(=O)CCCCCCCCCCCCCCC PORPENFLTBBHSG-MGBGTMOVSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- 244000099147 Ananas comosus Species 0.000 description 1
- 238000009020 BCA Protein Assay Kit Methods 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 241000194107 Bacillus megaterium Species 0.000 description 1
- 241000194103 Bacillus pumilus Species 0.000 description 1
- 108700003860 Bacterial Genes Proteins 0.000 description 1
- 108010077805 Bacterial Proteins Proteins 0.000 description 1
- 102100032487 Beta-mannosidase Human genes 0.000 description 1
- 241000589513 Burkholderia cepacia Species 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- 102000016938 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 108010059892 Cellulase Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 241000588923 Citrobacter Species 0.000 description 1
- 241000588919 Citrobacter freundii Species 0.000 description 1
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 1
- 241000607473 Edwardsiella <enterobacteria> Species 0.000 description 1
- 241000607471 Edwardsiella tarda Species 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000588914 Enterobacter Species 0.000 description 1
- 241000588697 Enterobacter cloacae Species 0.000 description 1
- 101000925662 Enterobacteria phage PRD1 Endolysin Proteins 0.000 description 1
- 241000588698 Erwinia Species 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 1
- 241000223198 Humicola Species 0.000 description 1
- 101710091977 Hydrophobin Proteins 0.000 description 1
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
- 108010028688 Isoamylase Proteins 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- 241000588915 Klebsiella aerogenes Species 0.000 description 1
- PNNNRSAQSRJVSB-UHFFFAOYSA-N L-rhamnose Natural products CC(O)C(O)C(O)C(O)C=O PNNNRSAQSRJVSB-UHFFFAOYSA-N 0.000 description 1
- 241000588912 Pantoea agglomerans Species 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 102100035200 Phospholipase A and acyltransferase 4 Human genes 0.000 description 1
- 102000004861 Phosphoric Diester Hydrolases Human genes 0.000 description 1
- 108090001050 Phosphoric Diester Hydrolases Proteins 0.000 description 1
- 244000110797 Polygonum persicaria Species 0.000 description 1
- 241000588769 Proteus <enterobacteria> Species 0.000 description 1
- 241000588768 Providencia Species 0.000 description 1
- 241000588778 Providencia stuartii Species 0.000 description 1
- 241001514713 Pseudohyphozyma bogoriensis Species 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 241000589630 Pseudomonas pseudoalcaligenes Species 0.000 description 1
- 101000968491 Pseudomonas sp. (strain 109) Triacylglycerol lipase Proteins 0.000 description 1
- 241000577556 Pseudomonas wisconsinensis Species 0.000 description 1
- 241000893045 Pseudozyma Species 0.000 description 1
- 241000187562 Rhodococcus sp. Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 241000607720 Serratia Species 0.000 description 1
- 241000607715 Serratia marcescens Species 0.000 description 1
- 241000607768 Shigella Species 0.000 description 1
- 241000607762 Shigella flexneri Species 0.000 description 1
- 241001278026 Starmerella bombicola Species 0.000 description 1
- 244000301083 Ustilago maydis Species 0.000 description 1
- 235000015919 Ustilago maydis Nutrition 0.000 description 1
- 241000235015 Yarrowia lipolytica Species 0.000 description 1
- 241001149679 [Candida] apicola Species 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 108090000637 alpha-Amylases Proteins 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 108010055059 beta-Mannosidase Proteins 0.000 description 1
- 239000007956 bioemulsifier Substances 0.000 description 1
- 238000004061 bleaching Methods 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 150000001773 cellobioses Chemical class 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 235000010980 cellulose Nutrition 0.000 description 1
- 150000005829 chemical entities Chemical class 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000003086 colorant Substances 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 230000037029 cross reaction Effects 0.000 description 1
- 108010005400 cutinase Proteins 0.000 description 1
- 150000001982 diacylglycerols Chemical class 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 239000002158 endotoxin Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 150000002430 hydrocarbons Chemical class 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000003752 hydrotrope Substances 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 108010032581 isopullulanase Proteins 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 230000002366 lipolytic effect Effects 0.000 description 1
- 229920006008 lipopolysaccharide Polymers 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 101150115538 nero gene Proteins 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 239000003605 opacifier Substances 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000000518 rheometry Methods 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 150000003625 trehaloses Chemical class 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 238000004065 wastewater treatment Methods 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
- 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
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/02—Anionic compounds
- C11D1/04—Carboxylic acids or salts thereof
- C11D1/06—Ether- or thioether carboxylic acids
Definitions
- This invention relates to detergent compositions comprising biosurfactant and lipase.
- Enzymes have been used in detergent formulations as a cleaning aid for many years. They may be derived from bacterial of other sources. The most commonly employed enzymes are proteases, amylases, mannanases, lipases and cellulases. They are often derived from fungal or yeast cultures.
- Lipases are used in surfactant containing detergent formulations to aid the cleaning of oily soils from fabrics. Despite their isolation and characterisation some decades ago, these enzymes have been difficult to formulate in conventional surfactant formulations because there is a competition between the enzyme and the surfactant for the target substrate oil. Surfactants will win this competition for the surface and will out-compete or displace enzymes from the oily surface and therefore reduce the enzyme performance on those soils. Thus, the practical impact of lipases in detergent cleaning products is limited, especially when compared to the impact of other cleaning enzymes, such as proteases and amylases.
- JP5168489A describes a method of making a biosurfactant using a lipase enzyme.
- the biosurfactant that is present in combination with the lipase does not have any acid moieties.
- the presence of a disaccharide moiety is optional.
- US2006106120 describes a mixture of microorganism, biosurfactant and a plastic degrading enzyme for the bioremediation of man-made materials.
- the biosurfactant may be derived from bacterial or other sources; the preferred enzyme used in the examples is a cutinase of bacterial origin. It may be co expressed with amylase and hydrophobin. The compositions are not used for cleaning.
- CN101126052 describes a biosurfactant containing cleaning composition that also contains a protease.
- the origin of the protease is a pineapple plant.
- US5417879 (Unilever) describes synergistic dual surfactant laundry composition containing sophorolipid (from yeast), cellobiose lipid (from fungus) or rhamnolipid (from bacteria) glycolipid biosurfactant. Examples using these biosurfactants did not comprise any enzyme. In column 12 lines 24 to 25, it is mentioned as possible to combine the biosurfactants with an undisclosed amount of enzyme of undisclosed origin.
- US2004171512A (Igarashi Keisuke ; Hirata Yoshihiko ; Furuta Taro ) discloses low-foaming detergent compositions comprising a biosurfactant (sophorolipid from yeast) which can replace a conventional low foaming block polymer nonionic surfactant.
- the biosurfactant may be used with an undisclosed type of enzyme selected from amylase, protease, cellulose, lipase, pullulanase, isopullulanase, isoamylase, catalase, peroxidase, or the like.
- the enzyme can be added by selecting appropriately in light of its substrate specificity.
- protease may be selected for a protein stain
- amylase may be selected for a starch stain.
- sophorolipids for dishwashing (hard surface cleaning) in combination with Savinase 6.0T a protease from Novo Nordisk and Duramyl 60T a starch lytic enzyme (amylase) from Novo Nordisk.
- Duramyl is produced from Bacillus Licheniformis and Savinase is produced from Bacillus Clausi / lentus, both bacterial sources. These are not taught to be generically preferred sources in this document.
- US2009188055A discloses compositions comprising sulfonated estolides and other derivatives of fatty acids.
- Table 20 provides prophetic examples of these surfactants in combination with other surfactants, including rhamnolipids. Enzymes are not included in these examples. Elsewhere in the document, it is said that the cleaning performance on greasy soils is synergistically improved with the estolides by using lipases.
- Suitable lipase enzymes include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1,372,034 .
- Suitable lipases include those that show a positive immunological cross-reaction with the antibody of the lipase, produced by the microorganism Pseudomonas fluorescens IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P "Amano,” hereafter referred to as "Amano-P". Further suitable lipases are lipases such as M1 Lipase.RTM and Lipomax.RTM (Gist-Brocades). Highly preferred lipases are the D96L lipolytic enzyme variant of the native lipase derived from Humicola lanuginosa (a fungus) as described in U.S.
- the Humicola lanuginosa strain DSM 4106 is used.
- This enzyme is incorporated into the composition in accordance with the present technology at a level of from 50 LU to 8500 LU per litre wash solution.
- the variant D96L is present at a level of from 100 LU to 7500 LU per litre of wash solution. More preferably at a level of from 150 LU to 5000 LU per litre of wash solution.
- US2006080785A (Nero ) describes carpet cleaning by applying a cleaning composition having biosurfactants and enzymes to the carpet; and bonnet cleaning the material.
- the enzymes are derived from Sea Kelp.
- US2004072713A discloses an article for use in an enzymatic fabric cleaning process, said article containing one or more types of harmless micro-organisms capable of excreting enzymes useful in said fabric cleaning process.
- the microorganism may be a bacterium, although fungal microorganisms are also exemplified.
- the examples all express bleaching enzymes.
- biosurfactants for example lipopolysaccharides.
- No wash liquor or concentrate comprising a mixture of biosurfactants derived from bacteria together with enzymes derived from bacteria is actually disclosed in this document. We are confident that the concentration of biosurfactant would have been much less than 0.5 g/L.
- a cleaning composition comprising an effective amount of surfactant system and an enzyme system characterised in that the surfactant system comprises at least 1 wt% (based on the cleaning composition) of a biosurfactant, which is a glycolipid surfactant comprising at least 20 mol% of glycolipid having both disaccharide and acid moieties and at least one lipase enzyme of bacterial origin.
- a biosurfactant which is a glycolipid surfactant comprising at least 20 mol% of glycolipid having both disaccharide and acid moieties and at least one lipase enzyme of bacterial origin.
- Lipases are a key enzyme for insertion into detergent compositions, especially laundry detergents, but also compositions designed to clean hard surfaces such as dishwashing compositions, that clean everyday dirt and stains effectively at reduced surfactant levels to enable concentration of the formulation.
- biosurfactant (fungal, bacterial and yeast) in combination with two types of lipase enzyme (fungal and bacterial).
- the bacterial enzymes consistently outperformed the fungal ones with the biosurfactants.
- the best result comes from a combination of bacterially derived enzyme with bacterially derived biosurfactant comprising at least 80mol% of biosurfactant having disaccharide and acid moieties (di-Rhamnolipid).
- a process for cleaning a substrate comprising the steps of immersing the substrate in water adding a composition according to any preceding claim to the water to form a wash liquor and washing the substrate characterised in that the wash cycle time is less than 60 minutes, preferably less than 30 minutes and the water temperature is less than 35 °C at all times.
- Suitable lipases include those of bacterial origin. Chemically modified or protein engineered mutants are included. Examples of useful bacterial lipases include lipases from P . alcaligenes or P. pseudoalcaligenes ( EP 218 272 ), 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 ( WO 96/12012 ), a Bacillus lipase, 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 ).
- useful bacterial lipases include
- Bacterial genes encoding bacterial lipase enzymes can be transferred to preferred expression production hosts, which are not limited to bacterial and includes for example other microbial hosts.
- preferred expression production hosts which are not limited to bacterial and includes for example other microbial hosts.
- bacterial lipase includes lipase produced from such expression hosts but originating from bacteria.
- the enzyme may be a phospholipase classified as EC 3.1.1.4 and/or EC 3.1.1.32.
- phospholipase is an enzyme, which has activity towards phospholipids.
- Phospholipids such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol.
- Phospholipases are enzymes that participate in the hydrolysis of phospholipids.
- phospholipases A 1 and A 2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid
- lysophospholipase or phospholipase B
- Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
- phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (A 1 or A 2 ), phospholipase B activity, phospholipase C activity or phospholipase D activity.
- phospholipase A used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase A 1 and/or Phospholipase A 2 activity.
- the phospholipase activity may be provided by enzymes having other activities as well, such as, e.g., a lipase with phospholipase activity.
- the phospholipase activity may, e.g., be from a lipase with phospholipase side activity.
- the phospholipase enzyme activity is provided by an enzyme having essentially only phospholipase activity and wherein the phospholipase enzyme activity is not a side activity.
- the phospholipase is of bacterial origin Bacillus, e.g., B. megaterium, B. subtilis; Citrobacter, e.g., C . freundii; Enterobacter, e.g., E . aerogenes, E. cloacae Edwardsiella, E. tarda; Erwinia, e.g., E . herbicola; Escherichia, e.g., E . coli; Klebsiella, e.g., K. pneumoniae; Proteus, e.g., P. vulgaris; Providencia, e.g., P. stuartii; Salmonella, e.g. S . typhimurium; Serratia, e.g., S . liquefasciens, S. marcescens; Shigella, e.g., S . flexneri;
- composition may further comprise Enzymes that are not of bacterial origin. Particularly protease, amylase and cellulase, although non-bacterial lipases could also be included.
- Biosurfactant in this patent specification does not include surfactants derived from plant material such as Alkyl polyglucosides (APG).
- Rhamnolipids typically from Pseudomonas sp.
- Information about other bacterially derived biosurfactants is available from " Mapping of Patents in Bioemulsifiers and biosurfactants - review, published in the Journal of Scientific and Industrial Research Vol 65, 2006, P91 .
- bacterially produced biosurfactants we include those where a bacterial gene is cloned and subsequently expressed from another organism as a manufacturing technique. For example, Rhamnolipids have been produced from E. coli in this way.
- Biosurfactants from non-bacterial microbial sources include those derived from fungi and yeasts, e.g. sophorolipids from Candida sp and Torulopsis sp. Candida apicola, Candida bombicola, Candida lipolytica, Candida bogoriensis. See: Environmental applications for biosurfactants - Environmental Pollution, Volume 133, 2005, Pages 183-198 Catherine N. Mulligan . See also, Towards commercial production of microbial surfactants - Trends in Biotechnology, Volume 24, 2006, Pages 509-515 : Soumen Mukherjee, Palashpriya Das, Ramkrishna Sen.
- Mannosylerythritol Lipids are typically from Pseudozyma (formerly Candida) Antarctica. Cellobiose lipids are typically from Ustilago maydis. Trehalose Lipids typically from Rhodococcus sp.
- the detergent composition may comprise other ingredients commonly found in laundry liquids. Especially polyester substantive soil release polymers, hydrotropes, opacifiers, colorants, perfumes, other enzymes, other surfactants, microcapsules of ingredients such as perfume or care additives, softeners, polymers for anti redeposition of soil, bleach, bleach activators and bleach catalysts, antioxidants, pH control agents and buffers, thickeners, external structurants for rheology modification, visual cues, either with or without functional ingredients embedded therein and other ingredients known to those skilled in the art.
- the composition is preferably a liquid and is advantageously packaged in either a multidose bottle or in a unit dose soluble pouch
- Wash solutions were prepared by dispersing lipase at a concentration of 4mg protein per litre together with detergent surfactant at the required concentration in phosphate buffered saline (PBS) adjusted to pH 8 and 12° FH water hardness. 10 mls of the wash solution were mixed in 25 ml plastic vials at 37°C with agitation at 200 rpm in an orbital incubator for 30 minutes. Swatches (approximately 1 cm 2 ) of cotton cloth stained with Sudan Red coloured Beef fat were then added and the vials returned to the shaking incubator. Swatches were removed at timed intervals, rinsed in cold water and dried at 37°C. The residual colour was monitored using a Macbeth Colour Eye, and compared with untreated stained cloths. Results are shown in Table 1 for 30 minutes and Table 2 for 4 hours.
- Bacterial enzyme is "Lipomax", a bacterially derived Lipase variant M21 L of the lipase of Pseudomonas alcaligenes as described in WO 94/25578 to Gist-Brocades (M.M.M.J. Cox, H.B.M. Lenting, L.J.S.M. Mulleners and J.M. van der Laan).
- Fungal enzyme is "Lipolase”, derived from Humicola languginosa as described in EP 0 258 068 and available from NovoZymes A/S.
- the bacterial lipase enzyme consistently outperforms the fungal lipase enzyme across all stain types. For the Sophorolipids at higher concentration and long wash times the presence of the fungal lipase enzyme provides no benefit over using the surfactant without a lipase.
- the enzymes were all dosed at the same level by determining the amount of active enzyme protein in each of the samples by use of a standard BCA protein Assay kit (ex Pierce) following the manufacturer's protocol.
- Example 2 The same experimentation was carried out as in Example 1 except the rhamnolipid material was separated into its mono-rhamnolipid and di-rhamnolipid components.
- the di rhamnolipid having two rhamnose sugars on the acyl group.
- R1 for the mono rhamnolipid
- R2 for the di-rhamnolipid material.
- the cleaning results for 1 hour and 4 hours are given in Tables 3 and 4.
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
- Enzymes And Modification Thereof (AREA)
Description
- This invention relates to detergent compositions comprising biosurfactant and lipase.
- A general description of biosurfactants is published by Rahman in Biotechnology 7 (2): 360-370, 2008 ISSN 1682-296X "Production, Characterisation and application of Biosurfactants - review".
- Enzymes have been used in detergent formulations as a cleaning aid for many years. They may be derived from bacterial of other sources. The most commonly employed enzymes are proteases, amylases, mannanases, lipases and cellulases. They are often derived from fungal or yeast cultures.
- Lipases are used in surfactant containing detergent formulations to aid the cleaning of oily soils from fabrics. Despite their isolation and characterisation some decades ago, these enzymes have been difficult to formulate in conventional surfactant formulations because there is a competition between the enzyme and the surfactant for the target substrate oil. Surfactants will win this competition for the surface and will out-compete or displace enzymes from the oily surface and therefore reduce the enzyme performance on those soils. Thus, the practical impact of lipases in detergent cleaning products is limited, especially when compared to the impact of other cleaning enzymes, such as proteases and amylases.
- The move to more sustainable chemistries reinforces a desire to reduce the surfactant level in the wash. As a bio alternative, enzymes represent a weight efficient choice to maintain performance on oily soil removal as surfactant levels are lowered. The use of biosurfactants has been proposed in many prior art documents.
- The following documents relate to combinations of biosurfactants and enzymes produced from bacteria.
-
JP5168489A - "Lipase and biosurfactant production for utilisation in bioremediation of vegetable oils and hydrocarbon". Martins VG et al (2008) Quimica Nova No 31 vol 8, 1942-1947.
- "Isolation and characterisation of a lipid degrading bacterium and its application to lipid containing wastewater treatment". Matsumiya Y. et al (2007) Journal of Bioscience and Bioengineering No 103, Vol 4, 325-330.
-
US2006106120 describes a mixture of microorganism, biosurfactant and a plastic degrading enzyme for the bioremediation of man-made materials. The biosurfactant may be derived from bacterial or other sources; the preferred enzyme used in the examples is a cutinase of bacterial origin. It may be co expressed with amylase and hydrophobin. The compositions are not used for cleaning. - The following documents relate to combinations of biosurfactants and enzymes not specifically produced from bacteria, for cleaning.
-
CN101126052 describes a biosurfactant containing cleaning composition that also contains a protease. The origin of the protease is a pineapple plant. -
US5417879 (Unilever) describes synergistic dual surfactant laundry composition containing sophorolipid (from yeast), cellobiose lipid (from fungus) or rhamnolipid (from bacteria) glycolipid biosurfactant. Examples using these biosurfactants did not comprise any enzyme. In column 12 lines 24 to 25, it is mentioned as possible to combine the biosurfactants with an undisclosed amount of enzyme of undisclosed origin. -
US2004171512A (Igarashi Keisuke ; Hirata Yoshihiko ; Furuta Taro ) discloses low-foaming detergent compositions comprising a biosurfactant (sophorolipid from yeast) which can replace a conventional low foaming block polymer nonionic surfactant. According to the general disclosure, the biosurfactant may be used with an undisclosed type of enzyme selected from amylase, protease, cellulose, lipase, pullulanase, isopullulanase, isoamylase, catalase, peroxidase, or the like. The enzyme can be added by selecting appropriately in light of its substrate specificity. For example, protease may be selected for a protein stain, and amylase may be selected for a starch stain. Examples use the sophorolipids for dishwashing (hard surface cleaning) in combination with Savinase 6.0T a protease from Novo Nordisk and Duramyl 60T a starch lytic enzyme (amylase) from Novo Nordisk. Duramyl is produced from Bacillus Licheniformis and Savinase is produced from Bacillus Clausi/lentus, both bacterial sources. These are not taught to be generically preferred sources in this document. -
US2009188055A (Stepan Co) discloses compositions comprising sulfonated estolides and other derivatives of fatty acids. Table 20 provides prophetic examples of these surfactants in combination with other surfactants, including rhamnolipids. Enzymes are not included in these examples. Elsewhere in the document, it is said that the cleaning performance on greasy soils is synergistically improved with the estolides by using lipases. Suitable lipase enzymes include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent1,372,034 U.S. 6,017,871 issued Jan. 25, 2000 (P&G). Preferably, the Humicola lanuginosa strain DSM 4106 is used. This enzyme is incorporated into the composition in accordance with the present technology at a level of from 50 LU to 8500 LU per litre wash solution. Preferably, the variant D96L is present at a level of from 100 LU to 7500 LU per litre of wash solution. More preferably at a level of from 150 LU to 5000 LU per litre of wash solution. -
US2006080785A (Nero ) describes carpet cleaning by applying a cleaning composition having biosurfactants and enzymes to the carpet; and bonnet cleaning the material. The enzymes are derived from Sea Kelp. - One document suggests combinations of biosurfactants and enzymes derived from bacteria for cleaning.
-
US2004072713A (Unilever ) discloses an article for use in an enzymatic fabric cleaning process, said article containing one or more types of harmless micro-organisms capable of excreting enzymes useful in said fabric cleaning process. In one embodiment, the microorganism may be a bacterium, although fungal microorganisms are also exemplified. The examples all express bleaching enzymes. Although not used in the examples the document speculates that it is especially useful if, in addition to enzymes, the micro-organisms are also capable of producing other chemical entities that contribute to the cleaning process, e.g. biosurfactants, for example lipopolysaccharides. No wash liquor or concentrate comprising a mixture of biosurfactants derived from bacteria together with enzymes derived from bacteria is actually disclosed in this document. We are confident that the concentration of biosurfactant would have been much less than 0.5 g/L. - According to the present invention there is a cleaning composition comprising an effective amount of surfactant system and an enzyme system characterised in that the surfactant system comprises at least 1 wt% (based on the cleaning composition) of a biosurfactant, which is a glycolipid surfactant comprising at least 20 mol% of glycolipid having both disaccharide and acid moieties and at least one lipase enzyme of bacterial origin.
- Surprising synergistic benefits on cleaning on stains and soils have been found when lipases, derived from bacteria, are combined with biological surfactants (biosurfactants) having both disaccharide and acid moieties.
- The combination may be used in any biological formulation. Lipases are a key enzyme for insertion into detergent compositions, especially laundry detergents, but also compositions designed to clean hard surfaces such as dishwashing compositions, that clean everyday dirt and stains effectively at reduced surfactant levels to enable concentration of the formulation.
- We tested three types of biosurfactant: (fungal, bacterial and yeast) in combination with two types of lipase enzyme (fungal and bacterial). The bacterial enzymes consistently outperformed the fungal ones with the biosurfactants. The best result comes from a combination of bacterially derived enzyme with bacterially derived biosurfactant comprising at least 80mol% of biosurfactant having disaccharide and acid moieties (di-Rhamnolipid).
- According to a second aspect of the present invention there is a process for cleaning a substrate comprising the steps of immersing the substrate in water adding a composition according to any preceding claim to the water to form a wash liquor and washing the substrate characterised in that the wash cycle time is less than 60 minutes, preferably less than 30 minutes and the water temperature is less than 35 °C at all times.
- Suitable lipases include those of bacterial origin. Chemically modified or protein engineered mutants are included. Examples of useful bacterial lipases include lipases from P. alcaligenes or P. pseudoalcaligenes (
EP 218 272 EP 331 376 GB 1,372,034 WO 95/06720 WO 96/27002 WO 96/12012 JP 64/744992 WO 91/16422 - Bacterial genes encoding bacterial lipase enzymes can be transferred to preferred expression production hosts, which are not limited to bacterial and includes for example other microbial hosts. The term bacterial lipase includes lipase produced from such expression hosts but originating from bacteria.
- The enzyme may be a phospholipase classified as EC 3.1.1.4 and/or EC 3.1.1.32. As used herein, the term phospholipase is an enzyme, which has activity towards phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol. Phospholipases are enzymes that participate in the hydrolysis of phospholipids. Several types of phospholipase activity can be distinguished, including phospholipases A1 and A2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid; and lysophospholipase (or phospholipase B) which can hydrolyze the remaining fatty acyl group in lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterases) release diacyl glycerol or phosphatidic acid respectively.
- The term phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (A1 or A2), phospholipase B activity, phospholipase C activity or phospholipase D activity. The term "phospholipase A" used herein in connection with an enzyme of the invention is intended to cover an enzyme with Phospholipase A1 and/or Phospholipase A2 activity. The phospholipase activity may be provided by enzymes having other activities as well, such as, e.g., a lipase with phospholipase activity. The phospholipase activity may, e.g., be from a lipase with phospholipase side activity. In other embodiments of the invention the phospholipase enzyme activity is provided by an enzyme having essentially only phospholipase activity and wherein the phospholipase enzyme activity is not a side activity.
- Preferably, the phospholipase is of bacterial origin Bacillus, e.g., B. megaterium, B. subtilis; Citrobacter, e.g., C. freundii; Enterobacter, e.g., E. aerogenes, E. cloacae Edwardsiella, E. tarda; Erwinia, e.g., E. herbicola; Escherichia, e.g., E. coli; Klebsiella, e.g., K. pneumoniae; Proteus, e.g., P. vulgaris; Providencia, e.g., P. stuartii; Salmonella, e.g. S. typhimurium; Serratia, e.g., S. liquefasciens, S. marcescens; Shigella, e.g., S. flexneri;
- The composition may further comprise Enzymes that are not of bacterial origin. Particularly protease, amylase and cellulase, although non-bacterial lipases could also be included.
- These are derived from microbial sources including bacteria, yeasts and fungi. The term Biosurfactant in this patent specification does not include surfactants derived from plant material such as Alkyl polyglucosides (APG).
- These are, for example, the Rhamnolipids typically from Pseudomonas sp. Information about other bacterially derived biosurfactants is available from "Mapping of Patents in Bioemulsifiers and biosurfactants - review, published in the Journal of Scientific and Industrial Research Vol 65, 2006, P91. Within the definition of bacterially produced biosurfactants, we include those where a bacterial gene is cloned and subsequently expressed from another organism as a manufacturing technique. For example, Rhamnolipids have been produced from E. coli in this way.
- Biosurfactants from non-bacterial microbial sources include those derived from fungi and yeasts, e.g. sophorolipids from Candida sp and Torulopsis sp. Candida apicola, Candida bombicola, Candida lipolytica, Candida bogoriensis. See: Environmental applications for biosurfactants - Environmental Pollution, Volume 133, 2005, Pages 183-198 Catherine N. Mulligan. See also, Towards commercial production of microbial surfactants - Trends in Biotechnology, Volume 24, 2006, Pages 509-515 : Soumen Mukherjee, Palashpriya Das, Ramkrishna Sen.
- Mannosylerythritol Lipids are typically from Pseudozyma (formerly Candida) Antarctica. Cellobiose lipids are typically from Ustilago maydis. Trehalose Lipids typically from Rhodococcus sp.
- Further information is given in Production, Characterisation and Applications of Biosurfactants Review - Biotechnology - Volume 7, 2008, page 370: Pattanathu, Rahman and Gakpe.
- The detergent composition may comprise other ingredients commonly found in laundry liquids. Especially polyester substantive soil release polymers, hydrotropes, opacifiers, colorants, perfumes, other enzymes, other surfactants, microcapsules of ingredients such as perfume or care additives, softeners, polymers for anti redeposition of soil, bleach, bleach activators and bleach catalysts, antioxidants, pH control agents and buffers, thickeners, external structurants for rheology modification, visual cues, either with or without functional ingredients embedded therein and other ingredients known to those skilled in the art. The composition is preferably a liquid and is advantageously packaged in either a multidose bottle or in a unit dose soluble pouch
- The invention will now be further described with reference to the following nonlimiting examples.
- In this example, various Enzyme / biosurfactant compositions were tested to determine their ability to remove a coloured beef stain from cotton cloth.
- Wash solutions were prepared by dispersing lipase at a concentration of 4mg protein per litre together with detergent surfactant at the required concentration in phosphate buffered saline (PBS) adjusted to pH 8 and 12° FH water hardness. 10 mls of the wash solution were mixed in 25 ml plastic vials at 37°C with agitation at 200 rpm in an orbital incubator for 30 minutes. Swatches (approximately 1 cm2) of cotton cloth stained with Sudan Red coloured Beef fat were then added and the vials returned to the shaking incubator. Swatches were removed at timed intervals, rinsed in cold water and dried at 37°C. The residual colour was monitored using a Macbeth Colour Eye, and compared with untreated stained cloths. Results are shown in Table 1 for 30 minutes and Table 2 for 4 hours.
- Bacterial enzyme is "Lipomax", a bacterially derived Lipase variant M21 L of the lipase of Pseudomonas alcaligenes as described in
WO 94/25578 - Fungal enzyme is "Lipolase", derived from Humicola languginosa as described in
EP 0 258 068 and available from NovoZymes A/S. - Details of the surfactants were as follows:
- SL = Sophorolipid: a biosurfactant of fungal origin comprising disaccharide moieties and at least 20% acid moieties.
- AC = Accell: a biosurfactant derived from a yeast.
- RL = Rhamnolipid: a biosurfactant of bacterial origin comprising acid moieties and wherein R2 comprises disaccharide moieties. RL is approximately 70 mol% di Rhamnolipid and 30 mol% mono Rhamnolipid. Only the di Rhamnolipid has the required disaccharide moiety.
- The bacterial lipase enzyme consistently outperforms the fungal lipase enzyme across all stain types. For the Sophorolipids at higher concentration and long wash times the presence of the fungal lipase enzyme provides no benefit over using the surfactant without a lipase.
- The enzymes were all dosed at the same level by determining the amount of active enzyme protein in each of the samples by use of a standard BCA protein Assay kit (ex Pierce) following the manufacturer's protocol.
- In this example, various enzyme/Biosurfactant compositions were examined to determine their ability to remove a coloured beef stain.
- The same experimentation was carried out as in Example 1 except the rhamnolipid material was separated into its mono-rhamnolipid and di-rhamnolipid components. The di rhamnolipid having two rhamnose sugars on the acyl group. We use the notation R1 for the mono rhamnolipid and R2 for the di-rhamnolipid material. The cleaning results for 1 hour and 4 hours are given in Tables 3 and 4.
Table 3 - 1 hour Biosurfactant No Enzyme Bacterial lipase Fungal lipase 05g/l SL 6.34 10.28 9.72 0.5 g/l RL 1.15 8.88 1.04 0.5 g/l R1 9.85 11.31 12.25 0.5 g/l R2 0.80 8.87 1.05 Table 4-4 hours Biosurfactant No Enzyme Bacterial lipase Fungal lipase 0.5 g/l SL 10.25 12.54 11.17 0.5 g/l RL 1.18 10.68 1.89 0.5 g/l R1 14.52 12.43 14.19 0.5 g/l R2 1.14 11.42 2.85
Biosurfactant | No Enzyme | Bacterial lipase | Fungal enzyme |
0.25g/l SL | 2.83 | 8.42 | 4.29 |
0.25g/l AC | 0.96 | 2.39 | 1.25 |
0.25 g/l RL | 3.35 | 5.40 | 3.29 |
0.5 g/l SL | 8.98 | 11.20 | 8.44 |
0.5 g/l AC | 1.05 | 1.95 | 1.00 |
0.5 g/l RL | 1.28 | 10.00 | 0.82 |
Biosurfactant | No Enzyme | Bacterial lipase | Fungal enzyme |
0.25g/l SL | 5.52 | 12.98 | 8.61 |
0.25g/l AC | 3.67 | 9.15 | 3.19 |
0.25 g/l RL | 3.12 | 8.01 | 3.36 |
0.5 g/l SL | 12.23 | 13.59 | 11.29 |
0.5 g/l AC | 2.22 | 8.40 | 3.52 |
0.5 g/l RL | 1.38 | 12.01 | 2.34 |
Claims (6)
- A cleaning composition comprising an effective amount of surfactant system and an enzyme system characterised in that the surfactant system comprises at least 1 wt% (based on the cleaning composition) of a biosurfactant, which is a glycolipid surfactant, comprising at least 20 mol% of glycolipid having both disaccharide and acid moieties and at least one lipase enzyme of bacterial origin.
- A composition according to claim 1 in which the biosurfactant is selected from Rhamnolipids, Sophorolipids and mixtures thereof
- A composition according to claim 1 in which the biosurfactant is of bacterial origin.
- A composition according to any preceding claim in which the biosurfactant is a rhamnolipid.
- A composition according to claim 4 in which the rhamnolipid comprises two or more rhamnose units on the acyl chain and is at least 60% di-rhamnolipid.
- A process for cleaning a substrate comprising the steps of immersing the substrate in water adding a composition according to any preceding claim to the water to form a wash liquor and washing the substrate characterised in that the wash cycle time is less than 60 minutes, preferably less than 30 minutes and the water temperature is less than 35 °C at all times.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP11729626.9A EP2596089B1 (en) | 2010-07-22 | 2011-07-04 | Detergent compositions comprising biosurfactant and lipase |
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP10170404 | 2010-07-22 | ||
PCT/EP2011/061216 WO2012010407A1 (en) | 2010-07-22 | 2011-07-04 | Detergent compositions comprising biosurfactant and lipase |
EP11729626.9A EP2596089B1 (en) | 2010-07-22 | 2011-07-04 | Detergent compositions comprising biosurfactant and lipase |
Publications (2)
Publication Number | Publication Date |
---|---|
EP2596089A1 EP2596089A1 (en) | 2013-05-29 |
EP2596089B1 true EP2596089B1 (en) | 2014-12-17 |
Family
ID=43304742
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP11729626.9A Active EP2596089B1 (en) | 2010-07-22 | 2011-07-04 | Detergent compositions comprising biosurfactant and lipase |
Country Status (6)
Country | Link |
---|---|
EP (1) | EP2596089B1 (en) |
CN (1) | CN103052703A (en) |
BR (1) | BR112013000114B1 (en) |
ES (1) | ES2532537T3 (en) |
WO (1) | WO2012010407A1 (en) |
ZA (1) | ZA201300376B (en) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US10017710B2 (en) | 2015-03-27 | 2018-07-10 | Croda International Plc | Method of separating mannosylerythritol lipids |
Families Citing this family (19)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN103146496B (en) * | 2013-03-11 | 2015-02-25 | 广州舒国生物科技有限公司 | Preparation method of microbial detergent |
US10674726B2 (en) * | 2013-12-19 | 2020-06-09 | Conopco, Inc. | Composition |
DE102014221889B4 (en) | 2014-10-28 | 2023-12-21 | Henkel Ag & Co. Kgaa | Detergents with mannosylerythritol lipid, enhancing the cleaning performance of detergents through mannosylerythritol lipid, and washing processes using mannosylerythritol lipid |
DE102014225789A1 (en) | 2014-12-15 | 2016-06-16 | Henkel Ag & Co. Kgaa | Detergents and cleaners |
CN104876405A (en) * | 2015-04-21 | 2015-09-02 | 南开大学 | Method for cleaning aged oil sludge |
AR105805A1 (en) * | 2015-08-28 | 2017-11-08 | Unilever Nv | IMPROVED WASH COMPOSITIONS |
US10576519B2 (en) | 2015-09-10 | 2020-03-03 | Locus Oil Ip Company, Llc | Enhanced microbial production of biosurfactants and other products, and uses thereof |
DE102016216539A1 (en) | 2016-09-01 | 2018-03-01 | Henkel Ag & Co. Kgaa | Detergent with saponin |
PE20190848A1 (en) | 2016-09-08 | 2019-06-18 | Locus Ip Co Llc | DISTRIBUTED SYSTEMS FOR THE EFFICIENT PRODUCTION AND USE OF COMPOSITIONS BASED ON MICRO-ORGANISMS |
MX2019006780A (en) | 2016-12-11 | 2019-12-02 | Locus Oil Ip Company Llc | Microbial products and their use in bioremediation and to remove paraffin and other contaminating substances from oil and gas production and processing equipment. |
JP7261174B2 (en) * | 2017-04-09 | 2023-04-19 | ローカス アイピー カンパニー、エルエルシー | Materials and methods for maintaining industrial, machinery and restaurant equipment |
EP3621586A4 (en) | 2017-05-07 | 2020-12-23 | Locus IP Company, LLC | Cosmetic compositions for skin health and methods of using same |
DE102017214265A1 (en) | 2017-08-16 | 2019-02-21 | Henkel Ag & Co. Kgaa | Rhamnolipid-containing detergents and cleaners |
WO2020058024A1 (en) * | 2018-09-17 | 2020-03-26 | Unilever Plc | Detergent composition |
EP3686265A1 (en) | 2019-01-23 | 2020-07-29 | BlueSun Consumer Brands, S.L. | Detergent composition with sophorolipids |
DE102021214680A1 (en) | 2021-12-20 | 2023-06-22 | Henkel Ag & Co. Kgaa | New combination of surfactants and detergents and cleaning agents containing them |
EP4234664A1 (en) | 2022-02-24 | 2023-08-30 | Evonik Operations GmbH | Composition comprising glucolipids and enzymes |
EP4234671A1 (en) * | 2022-02-24 | 2023-08-30 | Evonik Operations GmbH | Compositions containing biosurfactants and a lipase from stachybotrys chlorohalonata |
DE102022210879A1 (en) | 2022-10-14 | 2024-04-25 | Henkel Ag & Co. Kgaa | Surfactant mixtures |
Family Cites Families (20)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB1372034A (en) | 1970-12-31 | 1974-10-30 | Unilever Ltd | Detergent compositions |
DE3684398D1 (en) | 1985-08-09 | 1992-04-23 | Gist Brocades Nv | LIPOLYTIC ENZYMES AND THEIR USE IN DETERGENTS. |
EP0258068B1 (en) | 1986-08-29 | 1994-08-31 | Novo Nordisk A/S | Enzymatic detergent additive |
JPS6474992A (en) | 1987-09-16 | 1989-03-20 | Fuji Oil Co Ltd | Dna sequence, plasmid and production of lipase |
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 |
JP3112937B2 (en) | 1990-04-14 | 2000-11-27 | カリ―ヒエミー アクチエンゲゼルシヤフト | Alkaline Bacillus lipase, DNA sequence encoding the same and Bacillus producing this lipase |
GB9102945D0 (en) * | 1991-02-12 | 1991-03-27 | Unilever Plc | Detergent composition |
JP3125809B2 (en) * | 1991-12-26 | 2001-01-22 | 不二製油株式会社 | Glycolipid production method |
PL306812A1 (en) | 1993-04-27 | 1995-04-18 | Gist Brocades Nv | Novel lipase variants suitable for use in detergents |
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 |
ATE361355T1 (en) | 1993-10-14 | 2007-05-15 | Procter & Gamble | CLEANING AGENTS CONTAINING PROTEASE |
BE1008998A3 (en) | 1994-10-14 | 1996-10-01 | Solvay | Lipase, microorganism producing the preparation process for the lipase and uses thereof. |
JPH08228778A (en) | 1995-02-27 | 1996-09-10 | Showa Denko Kk | New lipase gene and production of lipase using the same |
JP2003013093A (en) | 2001-06-27 | 2003-01-15 | Saraya Kk | Low foaming detergent composition |
CA2485079A1 (en) | 2002-05-23 | 2003-12-04 | Unilever Plc | Article and process for cleaning fabrics |
WO2004038016A1 (en) | 2002-10-23 | 2004-05-06 | Tohoku Techno Arch Co., Ltd | Method of degrading plastic and process for producing useful substance using the same |
DK2258836T3 (en) * | 2004-09-10 | 2016-07-25 | Novozymes North America Inc | Methods for the prevention, elimination, reduction or destruction of biofilms |
US7300913B2 (en) | 2004-10-15 | 2007-11-27 | Naturell Clean, Inc. | Systems and methods for cleaning materials |
CN101126052A (en) | 2007-08-16 | 2008-02-20 | 王锦容 | Environmental protection remover |
US7666828B2 (en) | 2008-01-22 | 2010-02-23 | Stepan Company | Sulfonated estolides and other derivatives of fatty acids, methods of making them, and compositions and processes employing them |
-
2011
- 2011-07-04 ES ES11729626.9T patent/ES2532537T3/en active Active
- 2011-07-04 EP EP11729626.9A patent/EP2596089B1/en active Active
- 2011-07-04 BR BR112013000114-3A patent/BR112013000114B1/en active IP Right Grant
- 2011-07-04 WO PCT/EP2011/061216 patent/WO2012010407A1/en active Application Filing
- 2011-07-04 CN CN2011800357954A patent/CN103052703A/en active Pending
-
2013
- 2013-01-15 ZA ZA2013/00376A patent/ZA201300376B/en unknown
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US10017710B2 (en) | 2015-03-27 | 2018-07-10 | Croda International Plc | Method of separating mannosylerythritol lipids |
Also Published As
Publication number | Publication date |
---|---|
WO2012010407A1 (en) | 2012-01-26 |
ZA201300376B (en) | 2014-03-26 |
EP2596089A1 (en) | 2013-05-29 |
BR112013000114B1 (en) | 2020-12-29 |
CN103052703A (en) | 2013-04-17 |
BR112013000114A2 (en) | 2017-05-30 |
ES2532537T3 (en) | 2015-03-27 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
EP2596089B1 (en) | Detergent compositions comprising biosurfactant and lipase | |
EP2596088B1 (en) | Detergent compositions comprising biosurfactant and enzyme | |
EP0218272B1 (en) | Novel lipolytic enzymes and their use in detergent compositions | |
US20190233767A1 (en) | Surfactants that improve the cleaning of lipid-based stains treated with lipases | |
EP2596087B1 (en) | Combinations of rhamnolipids and enzymes for improved cleaning | |
US7183248B2 (en) | Enzymatic cleaner having high pH stability | |
JP5486810B2 (en) | Surface active bleach and dynamic pH | |
US5827718A (en) | Lipase, microorganisms producing the lipase, method of producing the lipase and use of the lipase | |
JP5448169B2 (en) | Cleaning enzyme and odor control | |
DK164709B (en) | Enzymic detergent composition and enzymic detergent additive | |
CN101622343A (en) | Cleaning enzymes and fragrance production | |
EP2756063B1 (en) | Detergent compositions comprising surfactant and enzyme | |
WO1996016153A1 (en) | Detergent compositions containing specific lipolytic enzymes | |
CA2010986A1 (en) | Unique microbial lipases with activity at high temperatures and phs suitable for use in detergents | |
WO2006131503A2 (en) | Detergents with enzymatic builder and bleach systems | |
EP0399681B1 (en) | Method of laundering fabrics | |
US5935271A (en) | Laundry detergent compositions containing lipolytic enzyme and amines | |
EP2935549B1 (en) | Method for removing fat and/or oil stains | |
Grbavčić et al. | Development of an environmentally acceptable detergent formulation for fatty soils based on the lipase from the indigenous extremophile Pseudomonas aeruginosa strain | |
WO2024027829A1 (en) | Hard surface cleaning composition and cleaning method |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PUAI | Public reference made under article 153(3) epc to a published international application that has entered the european phase |
Free format text: ORIGINAL CODE: 0009012 |
|
17P | Request for examination filed |
Effective date: 20130116 |
|
AK | Designated contracting states |
Kind code of ref document: A1 Designated state(s): AL AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO PL PT RO RS SE SI SK SM TR |
|
DAX | Request for extension of the european patent (deleted) | ||
GRAP | Despatch of communication of intention to grant a patent |
Free format text: ORIGINAL CODE: EPIDOSNIGR1 |
|
INTG | Intention to grant announced |
Effective date: 20140708 |
|
GRAS | Grant fee paid |
Free format text: ORIGINAL CODE: EPIDOSNIGR3 |
|
GRAA | (expected) grant |
Free format text: ORIGINAL CODE: 0009210 |
|
AK | Designated contracting states |
Kind code of ref document: B1 Designated state(s): AL AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO PL PT RO RS SE SI SK SM TR |
|
REG | Reference to a national code |
Ref country code: GB Ref legal event code: FG4D |
|
REG | Reference to a national code |
Ref country code: CH Ref legal event code: EP |
|
REG | Reference to a national code |
Ref country code: IE Ref legal event code: FG4D |
|
REG | Reference to a national code |
Ref country code: AT Ref legal event code: REF Ref document number: 701934 Country of ref document: AT Kind code of ref document: T Effective date: 20150115 |
|
REG | Reference to a national code |
Ref country code: DE Ref legal event code: R096 Ref document number: 602011012333 Country of ref document: DE Effective date: 20150212 |
|
REG | Reference to a national code |
Ref country code: ES Ref legal event code: FG2A Ref document number: 2532537 Country of ref document: ES Kind code of ref document: T3 Effective date: 20150327 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: LT Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: FI Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: NO Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20150317 |
|
REG | Reference to a national code |
Ref country code: LT Ref legal event code: MG4D |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: GR Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20150318 Ref country code: LV Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: RS Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: HR Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: SE Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
REG | Reference to a national code |
Ref country code: AT Ref legal event code: MK05 Ref document number: 701934 Country of ref document: AT Kind code of ref document: T Effective date: 20141217 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: NL Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: RO Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: CZ Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: EE Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: SK Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: PL Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: IS Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20150417 Ref country code: AT Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
REG | Reference to a national code |
Ref country code: DE Ref legal event code: R097 Ref document number: 602011012333 Country of ref document: DE |
|
PLBE | No opposition filed within time limit |
Free format text: ORIGINAL CODE: 0009261 |
|
STAA | Information on the status of an ep patent application or granted ep patent |
Free format text: STATUS: NO OPPOSITION FILED WITHIN TIME LIMIT |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: DK Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
26N | No opposition filed |
Effective date: 20150918 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: MC Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: SI Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
REG | Reference to a national code |
Ref country code: CH Ref legal event code: PL |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: LU Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20150704 |
|
REG | Reference to a national code |
Ref country code: IE Ref legal event code: MM4A |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: LI Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20150731 Ref country code: CH Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20150731 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: BE Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
REG | Reference to a national code |
Ref country code: FR Ref legal event code: PLFP Year of fee payment: 6 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: IE Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20150704 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: MT Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: HU Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT; INVALID AB INITIO Effective date: 20110704 Ref country code: SM Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 Ref country code: BG Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: CY Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
REG | Reference to a national code |
Ref country code: FR Ref legal event code: PLFP Year of fee payment: 7 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: MK Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
REG | Reference to a national code |
Ref country code: FR Ref legal event code: PLFP Year of fee payment: 8 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: PT Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: AL Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT Effective date: 20141217 |
|
REG | Reference to a national code |
Ref country code: DE Ref legal event code: R081 Ref document number: 602011012333 Country of ref document: DE Owner name: UNILEVER GLOBAL IP LIMITED, WIRRAL, GB Free format text: FORMER OWNER: UNILEVER N.V., ROTTERDAM, NL |
|
REG | Reference to a national code |
Ref country code: ES Ref legal event code: PC2A Owner name: UNILEVER IP HOLDINGS B.V. Effective date: 20211228 |
|
REG | Reference to a national code |
Ref country code: GB Ref legal event code: 732E Free format text: REGISTERED BETWEEN 20220127 AND 20220202 |
|
P01 | Opt-out of the competence of the unified patent court (upc) registered |
Effective date: 20230428 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: TR Payment date: 20230626 Year of fee payment: 13 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: IT Payment date: 20230719 Year of fee payment: 13 Ref country code: GB Payment date: 20230720 Year of fee payment: 13 Ref country code: ES Payment date: 20230926 Year of fee payment: 13 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: FR Payment date: 20230725 Year of fee payment: 13 Ref country code: DE Payment date: 20230719 Year of fee payment: 13 |