EP2596087B1 - Combinations of rhamnolipids and enzymes for improved cleaning - Google Patents

Combinations of rhamnolipids and enzymes for improved cleaning Download PDF

Info

Publication number
EP2596087B1
EP2596087B1 EP11728878.7A EP11728878A EP2596087B1 EP 2596087 B1 EP2596087 B1 EP 2596087B1 EP 11728878 A EP11728878 A EP 11728878A EP 2596087 B1 EP2596087 B1 EP 2596087B1
Authority
EP
European Patent Office
Prior art keywords
rhamnolipid
rhamnolipids
composition according
mono
rha
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
Application number
EP11728878.7A
Other languages
German (de)
English (en)
French (fr)
Other versions
EP2596087A1 (en
Inventor
Alyn James Parry
Neil James Parry
Anne Cynthia Peilow
Paul Simon Stevenson
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Unilever PLC
Unilever NV
Original Assignee
Unilever PLC
Unilever NV
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Family has litigation
First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=43302709&utm_source=***_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=EP2596087(B1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Application filed by Unilever PLC, Unilever NV filed Critical Unilever PLC
Priority to EP11728878.7A priority Critical patent/EP2596087B1/en
Publication of EP2596087A1 publication Critical patent/EP2596087A1/en
Application granted granted Critical
Publication of EP2596087B1 publication Critical patent/EP2596087B1/en
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

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
    • C11D1/04—Carboxylic acids or salts thereof
    • C11D1/06—Ether- or thioether carboxylic acids
    • 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
    • C11D1/37—Mixtures of compounds all of which are anionic
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/0005—Other compounding ingredients characterised by their effect
    • C11D3/0036—Soil deposition preventing compositions; Antiredeposition agents
    • 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
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3715—Polyesters or polycarbonates
    • 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
    • C11D1/12—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
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/12—Soft surfaces, e.g. textile

Definitions

  • This invention relates to cleaning compositions comprising mono-rhamnolipids in combination with enzymes.
  • Rhamnolipids are a class of glycolipid. They are constructed of rhamnose combined with beta-hydroxy fatty acids. Rhamnose is a sugar. Fatty acids are ubiquitous in animals and plants. The carboxyl end of the fatty acid end is connected to the rhamnose. Rhamnolipids are compounds of only three common elements; carbon, hydrogen, and oxygen. They are a crystalline acid. Rhamnolipids may be produced by strains of the bacteria Pseudomonas aeruginosa. There are two major groups of rhamnolipids; mono-rhamnolipids and di-rhamnolipids.
  • Mono-rhamnolipids have a single rhamnose sugar ring.
  • a typical mono-rhamnolipid produced by P. aeruginosa is L-rhamnosyl- ⁇ -hydroxydecanoyl- ⁇ -hydroxydecanoate (RhaC 10 C 10 ). It may be referred to as Rha-C 10 -C 10 , with a formula of C 26 H 48 O 9 .
  • Mono-rhamnolipids have a single rhamnose sugar ring.
  • the IUPAC Name is 3-[3-[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxydecanoyloxy]decanoic acid.
  • Di-rhamnolipids have two rhamnose sugar rings.
  • a typical di-rhamnolipid is L-rhamnosyl-L-rhamnosyl- ⁇ -hydroxydecanoyl- ⁇ -hydroxydecanoate (Rha2C 10 C 10 ). It may be referred to as Rha-Rha-C 10 -C 10 , with a formula of C 32 H 58 O 13 .
  • the IUPAC name is 3-[3-[4,5-dihydroxy-6-methyl-3-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid.
  • Rhamnolipids produced by P. aeruginosa (unidentified as either mono- or di-rhamnolipids):
  • rhamnolipids are produced in various chemical formulas, each with a different HLB, it is known that rhamnolipids can be produced or mixed to have a range of foaming properties.
  • Rhamnolipids are an anionic surfactant with both hydrophilic end and a lipophilic end. When their concentration increases to a certain level it is known that the rhamnolipids join together inside a liquid in a micelle.
  • rhamnolipids with two shorter fatty acids are more active in reducing surface tension and as an emulsifier. Those rare rhamnolipids with a single fatty acid chain are not as effective.
  • Pseudomonas aeruginosa The bacterium Pseudomonas aeruginosa is found naturally in soils, in water, and on plants. Metabolically, P . aeruginosa is chemoheterotrophic, generally aerobic, utilizing a wide range of organic compounds for sources of carbon and nitrogen.
  • strains of P . aeruginosa can be isolated to produce rhamnolipids at higher concentrations and more efficiently. Strains can also be selected to produce less byproduct and to metabolize different feedstock or pollutants. This production is greatly affected by the environment in which the bacterium is grown.
  • US 5417879 A1 suggests a mixed micellar Glycolipid and lamellar surfactant composition, that can be either glycolipid, or not. Compositions are proposed for use at 0.5 to 50 g/l. Examples using Rhamnolipid did not use any enzyme. In column 12 lines 24 to 25, it is mentioned as possible to combine the biosurfactants with an undisclosed amount of enzyme. To arrive at a combination of enzyme with Rhamnolipid it is necessary to make several selections from this document.
  • US2006106120 describes a mixture of micro-organism, biosurfactant and a plastic degrading enzyme for the bioremediation of man-made materials.
  • the biosurfactant may be a rhamnolipid (para 62).
  • the enzyme may be a lipase (para 64). No preference is given for any components of the rhamnolipid. Neither rhamnolipids nor lipases are exemplified and rhamnolipids are not specifically claimed.
  • 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. 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 as described in EP924221 . These biosurfactants are not Rhamnolipids. The levels of biosurfactants generated were very low indeed and certainly would not have exceeded 0.5g/l.
  • the micro-organisms are said to be capable of producing and secreting useful laundry enzymes such as Oxidoreductases, Carbohydrases, Proteases, Lipases, Transferases and Glycosidases.
  • a detergent composition with a novel ratio of mono to di rhamnolipids in combination with lipase.
  • the amount of mono-rhamnolipid present is more than the amount of di-rhamnolipid present (if any).
  • at least 80 wt%, more preferably at least 90 wt% or even 100 wt% of the rhamnolipid in the composition is mono-Rhamnolipid.
  • the lipase is preferably derived from either fungal or bacterial sources.
  • bacterial sources we include expression from other microbes, such as yeast, of genes that have been cloned from bacteria.
  • the rhamnolipid is preferably present in an amount of from 0.5 to 40 wt%.
  • the lipase is preferably present in an amount of from 0.0001 to 5 wt%.
  • the detergent composition is preferably unbuilt. That is zeolite, phosphate or silicate builders are absent.
  • the detergent composition is preferably a liquid detergent composition and if citric acid builder is present, it is limited to a maximum level of 2 wt%.
  • the composition is especially useful as a laundry detergent and may be used with advantage for washing in water with a low water hardness of less than 15°F. A process whereby the laundry and the composition are washed in presoftened water is particularly advantageously used with the compositions of the invention.
  • compositions are used to remove fatty soils from laundry, especially from cotton cloths. Removal of soils from cotton is of increasing concern because many of the sophisticated soil removal and soil release technologies included in modern laundry detergents work best on polyester cloths. Accordingly, it is advantageous to combine the detergent system of the present invention with a polyester soil release polymer.
  • Using mono-rhamnolipids and lipase in a detergent composition according to the invention leads to enhanced cleaning benefits and possibly synergies with synthetic anionic surfactants, for example C12-14 alkyl benzene sulphonate synthetic anionic surfactant.
  • This surfactant is commonly employed in laundry detergent compositions and is typically used with a nonionic surfactant, such as the ethoxylated nonionic surfactant used in US5417879 .
  • a nonionic surfactant such as the ethoxylated nonionic surfactant used in US5417879 .
  • the rhamnolipids with mono to di rhamnolipid ratio claimed provide a suitable substitute for the nonionic surfactant component, especially when used to remove fatty soils and particularly when used to remove soils from cotton cloth.
  • the compositions are suited to low wash temperatures and fast wash times, which support energy and time savings.
  • a preferred fatty soil is beef fat.
  • Rhamnolipids formed by the degradation of oils and fats by Pseudomonas Aeg, show poor cleaning benefits when used at concentrations of components generated by the bacterial breakdown process.
  • mono and di rhamnolipid components of the expressed rhamnolipids are extracted and the mono-rhamnolipid is used with lipase superior cleaning results.
  • further enhancement in detergency may be achieved.
  • 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.
  • Suitable lipases for use in the compositions of the invention include those of bacterial, fungal or yeast origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces ), e.g. from H. lanuginosa (T. lanuginosus) as described in EP 258 068 and EP 305 216 or from H. insolens as described in WO 96/13580 , a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes ( EP 218 272 ), P. cepacia ( EP 331 376 ), P .
  • lipase variants such as those described in WO 92/05249 , WO 94/01541 , EP 407 225 , EP 260 105 , WO 95/35381 , WO 96/00292 , WO 95/30744 , WO 94/25578 , WO 95/14783 , WO 95/22615 , WO 97/04079 , WO 97/07202 , US2008004186 , US2006205628 , US5869438 , US6017866 , US2002110854 , US6939702 , US2009221034 , US200802425 , US2004053360 , US2005281912 , US2006075518 , US2005059130 , US20041542180 , US2003199069 , WO98106215 and WO08088489 .
  • lipases are described and referenced but not limited to those in Juardo et al J Surfact Deterg (2007) 10: 61-70 , Horchani et al J Molecular Catalysis: Enzymatic 56 (2009) 237-245 , Aloulou et al Biochimica et Biophysica acta 1771 (2007) 1446-1456 , Mogensen et al Biochemistry (2005) 44: 1719-1730 , Nicanuzia dos Prazeres et al Brazilian J of Microbiology (2006) 37: 505-509 , Fernandez-Lorente et al Biotechnology and Bioengineering, 97: vol2 242-250 , Gilbert (1993) Enzyme Microb. Technol.
  • Preferred commercially available lipase enzymes include LipolaseTM and Lipolase UltraTM, LipexTM, Novozym 525L (Novozymes A/S).
  • the composition may comprise a cutinase. classified in EC 3.1.1.74.
  • the cutinase used according to the invention may be of any origin.
  • cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.
  • Cutinases are enzymes that are able to degrade cutin.
  • the cutinase is derived from a strain of Aspergillus, in particular Aspergillus oryzae, a strain of Alternaria, in particular Alternaria brassiciola, a strain of Fusarium, in particular Fusarium solani, Fusarium solani pisi, Fusarium roseum culmorum, or Fusarium roseum sambucium, a strain of Helminthosporum, in particular Helminthosporum sativum, a strain of Humicola, in particular Humicola insolens, a strain of Pseudomonas, in particular Pseudomonas mendocina, or Pseudomonas putida, a strain of Rhizoctonia, in particular Rhizoctonia solani, a strain of Streptomyces, in particular Streptomyces scabies
  • the cutinase is derived from a strain of Humicola insolens, in particular the strain Humicola insolens DSM 1800.
  • Humicola insolens cutinase is described in WO 96/13580 .
  • the cutinase may be a variant, such as one of the variants disclosed in WO 00/34450 and WO 01/92502 , which are hereby incorporated by reference.
  • Preferred cutinase variants include variants listed in Example 2 of WO 01/92502 , which is hereby specifically incorporated by reference.
  • esterases are those described in US2002012959 , WO09085743 , WO09002480 , US2002137177 , US2003024009 , US2010151542 , US2003032161 , US2002007518 and US2007167344 . This also includes the Transferase enzyme class.
  • Preferred commercial cutinases include NOVOZYMTM 51032 (available from Novozymes A/S, Denmark).
  • the composition may also comprise 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 which 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 may be of any origin, e.g., of animal origin (such as, e.g., mammalian), e.g. from pancreas (e.g., bovine or porcine pancreas), or snake venom or bee venom.
  • animal origin such as, e.g., mammalian
  • pancreas e.g., bovine or porcine pancreas
  • snake venom or bee venom e.g., from snake venom or bee venom.
  • the phospholipase may be of microbial origin, e.g., from filamentous fungi, yeast or bacteria, such as the genus or species Aspergillus, e.g., A . niger, Dictyostelium, e.g., D. discoideum; Mucor, e.g. M. javanicus, M. mucedo, M.
  • subtilissimus Neurospora, e.g. N. crassa; Rhizomucor, e.g., R. pusillus; Rhizopus, e.g. R. arrhizus, R. japonicus, R. stolonifer, Sclerotinia, e.g., S . libertiana; Trichophyton, e.g. T . rubrum; Whetzelinia, e.g., W. sclerotiorum; 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; Streptomyces, e.g., S .
  • the phospholipase may be fungal, e.g., from the class Pyrenomycetes, such as the genus Fusarium, such as a strain of F. culmorum, F. heterosporum, F. solani, or a strain of F. oxysporum.
  • the phospholipase may also be from a filamentous fungus strain within the genus Aspergillus, such as a strain of Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger or Aspergillus oryzae.
  • Preferred phospholipases are derived from a strain of Humicola, especially Humicola lanuginosa.
  • the phospholipase may be a variant, such as one of the variants disclosed in WO 00/32758 , which are hereby incorporated by reference.
  • Preferred phospholipase variants include variants listed in Example 5 of WO 00/32758 , which is hereby specifically incorporated by reference.
  • the phospholipase is one described in WO 04/111216 , especially the variants listed in the table in Example 1.
  • the phospholipase is derived from a strain of Fusarium, especially Fusarium oxysporum.
  • the phospholipase may be the one concerned in WO 98/026057 displayed in SEQ ID NO: 2 derived from Fusarium oxysporum DSM 2672, or variants thereof.
  • the phospholipase is a phospholipase A 1 (EC. 3.1.1.32). In another preferred embodiment of the invention the phospholipase is a phospholipase A 2 (EC.3.1.1.4.).
  • Examples of commercial phospholipases include LECITASETM and LECITASETM ULTRA, YIELSMAX, or LIPOPAN F (available from Novozymes A/S, Denmark).
  • the composition may further comprise other enzymes enhancing the detergency of the composition such as softening agents, an amylase (e.g. Fungamyl(R) from Novo Nordisk A/S, Denmark), a lipase (e.g. Novocor(R) AD from Novo Nordisk A/S, Denmark), a cellulase (e.g. Celluzyme(R), Carezyme(R), and/or Celluclast(R), all from Novo Nordisk A/S, Denmark), a xylanase (e.g. Biofeed(R) PLUS or Shearzyme(TM) from Novo Nordisk A/S, Denmark), a beta-glucanase (e.g.
  • an amylase e.g. Fungamyl(R) from Novo Nordisk A/S, Denmark
  • a lipase e.g. Novocor(R) AD from Novo Nordisk A/S, Denmark
  • a cellulase e.g. Cellu
  • a pectinase e.g. Pectinex(TM) Ultra from Novo Nordisk A/S, Denmark
  • a peroxidase e.g. Guardzyme(TM) from Novo Nordisk A/S, Denmark
  • a laccase e.g. obtained from Myceliophthora or Polyporus
  • 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.
  • PBS phosphate buffered saline
  • 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 process of separating and characterising the mixture was carried out using an HPLC connected to an Ion Trap Electrospray ionisation Mass Spectrometer.
  • the mode of ionisation was in negative mode with a scanning range of 50-1200Da.
  • the column used to separate was a Phenomenex luna C18 250 x 4.6mm 5 ⁇ m column.
  • the mobile phase water (mobile phase A) and acetonitrile (mobile phase B) were used to separate via a gradient of 60:40 (A:B) changing to 30:70 (A:B) over 30 minutes.
  • the system was then held for 5 minutes before returning to the start conditions all at a flow rate of 0.5ml/min.
  • the injection volume was 10 ⁇ l.

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)
EP11728878.7A 2010-07-22 2011-07-04 Combinations of rhamnolipids and enzymes for improved cleaning Active EP2596087B1 (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
EP11728878.7A EP2596087B1 (en) 2010-07-22 2011-07-04 Combinations of rhamnolipids and enzymes for improved cleaning

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
EP10170403 2010-07-22
EP11728878.7A EP2596087B1 (en) 2010-07-22 2011-07-04 Combinations of rhamnolipids and enzymes for improved cleaning
PCT/EP2011/061214 WO2012010406A1 (en) 2010-07-22 2011-07-04 Combinations of rhamnolipids and enzymes for improved cleaning

Publications (2)

Publication Number Publication Date
EP2596087A1 EP2596087A1 (en) 2013-05-29
EP2596087B1 true EP2596087B1 (en) 2015-12-16

Family

ID=43302709

Family Applications (1)

Application Number Title Priority Date Filing Date
EP11728878.7A Active EP2596087B1 (en) 2010-07-22 2011-07-04 Combinations of rhamnolipids and enzymes for improved cleaning

Country Status (6)

Country Link
EP (1) EP2596087B1 (pt)
CN (2) CN107955721A (pt)
BR (1) BR112013000108B1 (pt)
ES (1) ES2561553T3 (pt)
WO (1) WO2012010406A1 (pt)
ZA (1) ZA201300377B (pt)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2022229069A1 (en) * 2021-04-29 2022-11-03 Unilever Ip Holdings B.V. Process to produce mono-rhamnolipids

Families Citing this family (27)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8957129B2 (en) 2012-05-07 2015-02-17 Rhodia Operations Aqueous coatings and paints incorporating one or more antimicrobial biosurfactants and methods for using same
DE102013205756A1 (de) 2013-04-02 2014-10-02 Evonik Industries Ag Mischungszusammensetzung enthaltend Rhamnolipide
DE102013205755A1 (de) * 2013-04-02 2014-10-02 Evonik Industries Ag Waschmittelformulierung für Textilien enthaltend Rhamnolipide mit einem überwiegenden Gehalt an di-Rhamnolipiden
WO2015091294A1 (en) * 2013-12-18 2015-06-25 Unilever Plc Mono-rhamnolipid based compositions.
CN105992814A (zh) * 2013-12-19 2016-10-05 荷兰联合利华有限公司 组合物
FR3026917B1 (fr) 2014-10-08 2018-03-02 Centre National De La Recherche Scientifique (Cnrs) Biosurfactants de pseudomonas pour lutter contre les legionelles
DE102014221889B4 (de) * 2014-10-28 2023-12-21 Henkel Ag & Co. Kgaa Waschmittel mit Mannosylerythritollipid, Verstärkung der Reinigungsleistung von Waschmitteln durch Mannosylerythritollipid, und Waschverfahren unter Einsatz von Mannosylerythritollipid
DE102014225789A1 (de) 2014-12-15 2016-06-16 Henkel Ag & Co. Kgaa Wasch- und Reinigungsmittel
CA2973183C (en) 2015-01-12 2023-10-03 Logos Technologies Llc Production of rhamnolipid compositions
EP3061442A1 (de) * 2015-02-27 2016-08-31 Evonik Degussa GmbH Zusammensetzung enthaltend Rhamnolipid und Siloxan
US10487294B2 (en) 2015-03-02 2019-11-26 Conopco, Inc. Compositions with reduced dye-transfer properties
US10259837B2 (en) 2015-03-02 2019-04-16 Conopco, Inc. Method of separating rhamnolipids from a fermentation broth
EP3070155A1 (de) 2015-03-18 2016-09-21 Evonik Degussa GmbH Zusammensetzung enthaltend peptidase und biotensid
AR105805A1 (es) * 2015-08-28 2017-11-08 Unilever Nv Composiciones de lavado mejoradas
CN106591013A (zh) * 2016-11-30 2017-04-26 大连百奥泰科技有限公司 一种生物洗涤剂组合物
CA3052437C (en) 2017-02-06 2024-02-20 Logos Technologies Llc Decolorization of concentrated rhamnolipid composition
DE102017214265A1 (de) 2017-08-16 2019-02-21 Henkel Ag & Co. Kgaa Rhamnolipidhaltige Wasch- und Reinigungsmittel
CN108085190A (zh) * 2017-12-25 2018-05-29 上海和黄白猫有限公司 具有抗污功能的羽绒服清洗剂
EP3749679A1 (en) 2018-02-09 2020-12-16 Evonik Operations GmbH Mixture composition comprising glucolipids
US11744269B2 (en) * 2020-01-06 2023-09-05 Vinay Bhalchandra PARANJPE Vegetable and fruit wash formulation and uses thereof
WO2022229052A1 (en) 2021-04-29 2022-11-03 Unilever Ip Holdings B.V. Process to produce mono-rhamnolipids
CN118339175A (zh) * 2021-12-02 2024-07-12 赢创运营有限公司 包含糖脂的组合物
DE102021214680A1 (de) 2021-12-20 2023-06-22 Henkel Ag & Co. Kgaa Neue Tensidkombination und Wasch- und Reinigungsmittel, welche diese enthalten
WO2023116569A1 (en) * 2021-12-21 2023-06-29 Novozymes A/S Composition comprising a lipase and a booster
EP4234664A1 (en) 2022-02-24 2023-08-30 Evonik Operations GmbH Composition comprising glucolipids and enzymes
EP4155371A1 (en) * 2022-08-29 2023-03-29 Evonik Operations GmbH Composition rich in mono-rhamnolipids
DE102022210879A1 (de) 2022-10-14 2024-04-25 Henkel Ag & Co. Kgaa Tensidmischungen

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0153634A2 (de) 1984-02-17 1985-09-04 Wintershall Aktiengesellschaft Verfahren zur biotechnischen Herstellung von Rhamnolipiden und Rhamnolipide mit nur einem beta-Hydroxidecancarbonsäurerest im Molekül
EP0499434A1 (en) 1991-02-12 1992-08-19 Unilever Plc Detergent compositions
DE19648439A1 (de) 1996-11-22 1998-05-28 Henkel Kgaa Verwendung von Mischungen aus Glycolipiden und Tensiden

Family Cites Families (60)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1542180A (en) 1924-04-28 1925-06-16 Clarence C Selden Art of and apparatus for the treatment of plant fiber or the like
GB1372034A (en) 1970-12-31 1974-10-30 Unilever Ltd Detergent compositions
DE3684398D1 (de) 1985-08-09 1992-04-23 Gist Brocades Nv Lipolytische enzyme und deren anwendung in reinigungsmitteln.
ES2058119T3 (es) 1986-08-29 1994-11-01 Novo Nordisk As Aditivo detergente enzimatico.
NZ221627A (en) 1986-09-09 1993-04-28 Genencor Inc Preparation of enzymes, modifications, catalytic triads to alter ratios or transesterification/hydrolysis ratios
EP0305216B1 (en) 1987-08-28 1995-08-02 Novo Nordisk A/S Recombinant Humicola lipase and process for the production of recombinant humicola lipases
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
JP3079276B2 (ja) 1988-02-28 2000-08-21 天野製薬株式会社 組換え体ｄｎａ、それを含むシュードモナス属菌及びそれを用いたリパーゼの製造法
GB8915658D0 (en) 1989-07-07 1989-08-23 Unilever Plc Enzymes,their production and use
DE4111321A1 (de) 1990-04-14 1991-10-17 Kali Chemie Ag Alkalische bacillus-lipasen, hierfuer codierende dna-sequenzen sowie bacilli, die diese lipasen produzieren
US5869438A (en) 1990-09-13 1999-02-09 Novo Nordisk A/S Lipase variants
BR9106839A (pt) 1990-09-13 1993-07-20 Novo Nordisk As Variante de lipase,construcao de dna,vetor de expressao de recombinante,celula,planta,processo para produzir uma variante de lipase,aditivo e composicao de detergente
GB9102945D0 (en) 1991-02-12 1991-03-27 Unilever Plc Detergent composition
DK88892D0 (da) 1992-07-06 1992-07-06 Novo Nordisk As Forbindelse
ATE287946T1 (de) 1993-04-27 2005-02-15 Genencor Int Neuartige lipasevarianten zur verwendung in reinigungsmitteln
JP2859520B2 (ja) 1993-08-30 1999-02-17 ノボ ノルディスク アクティーゼルスカブ リパーゼ及びそれを生産する微生物及びリパーゼ製造方法及びリパーゼ含有洗剤組成物
JPH07143883A (ja) 1993-11-24 1995-06-06 Showa Denko Kk リパーゼ遺伝子及び変異体リパーゼ
KR970701264A (ko) 1994-02-22 1997-03-17 안네 제케르 지질분해효소의 변이체 제조방법(a method of preparing a viriant of a lipolytic enzyme)
DE69528524T2 (de) 1994-05-04 2003-06-26 Genencor International, Inc. Lipasen mit verbesserten tensiostabilitaet
AU2884595A (en) 1994-06-20 1996-01-15 Unilever Plc Modified pseudomonas lipases and their use
AU2884695A (en) 1994-06-23 1996-01-19 Unilever Plc Modified pseudomonas lipases and their use
BE1008998A3 (fr) 1994-10-14 1996-10-01 Solvay Lipase, microorganisme la produisant, procede de preparation de cette lipase et utilisations de celle-ci.
JPH10507642A (ja) 1994-10-26 1998-07-28 ノボ ノルディスク アクティーゼルスカブ 脂肪分解活性を有する酵素
JPH08228778A (ja) 1995-02-27 1996-09-10 Showa Denko Kk 新規なリパーゼ遺伝子及びそれを用いたリパーゼの製造方法
CN1193346A (zh) 1995-07-14 1998-09-16 诺沃挪第克公司 一种具有脂解活性的修饰酶
US6495357B1 (en) 1995-07-14 2002-12-17 Novozyme A/S Lipolytic enzymes
CN1192780B (zh) 1995-08-11 2010-08-04 诺沃奇梅兹有限公司 新的脂解酶
US5767090A (en) 1996-01-17 1998-06-16 Arizona Board Of Regents, On Behalf Of The University Of Arizona Microbially produced rhamnolipids (biosurfactants) for the control of plant pathogenic zoosporic fungi
NZ334968A (en) 1996-09-30 2000-11-24 Genencor Int Esterases derived from Aspergillus
GB9621373D0 (en) 1996-10-14 1996-12-04 Scotia Holdings Plc Fatty acid treatment
CN1148442C (zh) 1996-12-09 2004-05-05 诺维信公司 利用来自具有磷脂酶a和/或b活性的丝状真菌的磷脂酶降低含有大量非水合磷的食用油中的含磷成分
IT1296987B1 (it) 1997-12-19 1999-08-03 Eniricerche S P A Ora Enitecno Biosurfattante lipopolisaccaridico
EP1047445B1 (en) 1998-01-23 2013-08-28 The Governing Council Of The University Of Toronto Modified enzymes and their use for peptide synthesis
US6284512B1 (en) 1998-01-23 2001-09-04 Genencor International, Inc. Chemically modified mutant enzymes and methods for producing them, and screening them for amidase and/or esterase activity
US7312062B2 (en) 1998-11-27 2007-12-25 Novozymes A/S Lipolytic enzyme variants
DK1131416T3 (da) 1998-11-27 2009-10-26 Novozymes As Lipolytiske enzymvarianter
JP4615723B2 (ja) 1998-12-04 2011-01-19 ノボザイムス アクティーゼルスカブ クチナーゼ変異体
JP4523178B2 (ja) 1999-03-31 2010-08-11 ノボザイムス アクティーゼルスカブ リパーゼ変異体
JP4851034B2 (ja) 1999-06-02 2012-01-11 ノボザイムス アクティーゼルスカブ 化学修飾された脂質分解酵素
US6254645B1 (en) 1999-08-20 2001-07-03 Genencor International, Inc. Enzymatic modification of the surface of a polyester fiber or article
ES2248328T3 (es) 2000-06-02 2006-03-16 Novozymes A/S Variantes de cutinasa.
US6511837B2 (en) 2000-06-26 2003-01-28 Novozymes A/S Lipolytic enzymes
EP1337652B1 (en) 2000-11-17 2009-04-22 Genencor International, Inc. Manipulation of the phenolic acid content and digestibility of plant cell walls by targeted expression of genes encoding cell wall degrading enzymes
ATE443759T1 (de) 2001-02-07 2009-10-15 Novozymes As Lipasevarianten
EP1506282A1 (en) 2002-05-23 2005-02-16 Unilever N.V. Article and process for cleaning fabrics
EP1595949B1 (en) 2002-10-23 2011-06-22 Tohoku Techno Arch Co., Ltd. Method of degrading plastic and process for producing useful substance using the same
DK1445302T3 (da) 2003-01-28 2006-10-09 Ecover N V Detergentsammensætninger
JP2006517989A (ja) 2003-02-18 2006-08-03 ノボザイムス アクティーゼルスカブ 洗剤組成物
WO2004111216A2 (en) 2003-06-19 2004-12-23 Novozymes A/S Phospholipase variants
US7754460B2 (en) 2003-12-03 2010-07-13 Danisco Us Inc. Enzyme for the production of long chain peracid
EP1799819B1 (en) 2004-09-30 2011-03-23 Novozymes Inc. Polypeptides having lipase activity and polynucleotides encoding same
US7300913B2 (en) 2004-10-15 2007-11-27 Naturell Clean, Inc. Systems and methods for cleaning materials
CN100419126C (zh) * 2005-06-16 2008-09-17 广州天至环保科技有限公司 一种应用于金属加工业前处理除油脱脂的生物除油剂及其处理金属表面油污的方法
PL2032698T3 (pl) 2006-06-23 2012-11-30 Danisco Us Inc Systematyczna ocena związków sekwencji i aktywności przy zastosowaniu bibliotek typu "ocena pozycji" do inżynierii wielorakich właściwości
US20080002425A1 (en) 2006-07-03 2008-01-03 Junhon Lin Lighting Device With Fluid Wave Projection
BRPI0720852A2 (pt) 2006-12-22 2014-03-11 Danisco Us Inc Genecor Division Desemulsificação auxiliada por enzima de extratos de lipídio aquosos
EP2121909A1 (en) 2007-02-27 2009-11-25 Danisco US Inc. Cleaning enzymes and fragrance production
WO2009002480A2 (en) 2007-06-26 2008-12-31 Danisco Us, Inc., Genencor Division Acyl transferase having altered substrate specificity
RU2495098C2 (ru) 2007-12-20 2013-10-10 ДАНИСКО ЮЖс ИНК. Способ ферментативного удаления биопленки, композиция и набор
MX337307B (es) 2008-02-29 2016-02-25 Novozymes As Variante de enzima lipolitica con estabilidad mejorada y polinucleotidos que codifican para la misma.

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0153634A2 (de) 1984-02-17 1985-09-04 Wintershall Aktiengesellschaft Verfahren zur biotechnischen Herstellung von Rhamnolipiden und Rhamnolipide mit nur einem beta-Hydroxidecancarbonsäurerest im Molekül
EP0499434A1 (en) 1991-02-12 1992-08-19 Unilever Plc Detergent compositions
DE19648439A1 (de) 1996-11-22 1998-05-28 Henkel Kgaa Verwendung von Mischungen aus Glycolipiden und Tensiden

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
CHEN ET AL.: "mixing behaviour of the biosurfactant rhamnolipid with a conventional anionic surfactant sodium dodecyl benzene sulfonate", LANGMUIR, vol. 26, no. 23, 2010, pages 17958 - 17968, XP055306933
CHEN ET AL.: "solution self assembly and adsorption at the air water interface", LANGMUIR, vol. 26, no. 23, 2010, pages 18281 - 18292, XP055132334
HELVACI ET AL.: "effect of electrolytes on the surface behaviour of rhamnolipids R1 an R2", COLLOIDS AND SURFACES B: BIOINTERFACES, vol. 35, 2004, pages 225 - 233, XP055306931
ÖZDEMIR ET AL.: "effect of PH on the surface and interfacial behaviour of rhamnolipds R1 and R2", COLLOIDS AND SURFACES A: PHYSICOCHEM. ENG. ASPECTS, vol. 234, 2004, pages 135 - 143, XP055190608

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2022229069A1 (en) * 2021-04-29 2022-11-03 Unilever Ip Holdings B.V. Process to produce mono-rhamnolipids

Also Published As

Publication number Publication date
ES2561553T3 (es) 2016-02-26
ZA201300377B (en) 2014-03-26
CN107955721A (zh) 2018-04-24
BR112013000108A2 (pt) 2017-06-13
CN103052704A (zh) 2013-04-17
EP2596087A1 (en) 2013-05-29
BR112013000108B1 (pt) 2021-05-11
WO2012010406A1 (en) 2012-01-26

Similar Documents

Publication Publication Date Title
EP2596087B1 (en) Combinations of rhamnolipids and enzymes for improved cleaning
EP2596088B1 (en) Detergent compositions comprising biosurfactant and enzyme
EP3341459B1 (en) Detergent compositions with lipase and biosurfactant
AU2007284126B2 (en) Bacteria cultures and compositions comprising bacteria cultures
EP2596089B1 (en) Detergent compositions comprising biosurfactant and lipase
EP2756063B1 (en) Detergent compositions comprising surfactant and enzyme
EP2675891A1 (en) Mitigation of odor in cleaning machines and cleaning processes
EP3158044A1 (en) Enzyme treatment composition
EP2744882A1 (en) Enzyme system

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

RIC1 Information provided on ipc code assigned before grant

Ipc: C11D 1/37 20060101ALI20140625BHEP

Ipc: C11D 1/06 20060101AFI20140625BHEP

Ipc: C11D 3/00 20060101ALI20140625BHEP

Ipc: C11D 3/386 20060101ALI20140625BHEP

INTG Intention to grant announced

Effective date: 20140708

17Q First examination report despatched

Effective date: 20150113

GRAP Despatch of communication of intention to grant a patent

Free format text: ORIGINAL CODE: EPIDOSNIGR1

INTG Intention to grant announced

Effective date: 20150709

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: 765569

Country of ref document: AT

Kind code of ref document: T

Effective date: 20160115

REG Reference to a national code

Ref country code: DE

Ref legal event code: R096

Ref document number: 602011022047

Country of ref document: DE

REG Reference to a national code

Ref country code: ES

Ref legal event code: FG2A

Ref document number: 2561553

Country of ref document: ES

Kind code of ref document: T3

Effective date: 20160226

REG Reference to a national code

Ref country code: NL

Ref legal event code: MP

Effective date: 20151216

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: 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: 20151216

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: 20160316

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: 20151216

REG Reference to a national code

Ref country code: AT

Ref legal event code: MK05

Ref document number: 765569

Country of ref document: AT

Kind code of ref document: T

Effective date: 20151216

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

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: 20151216

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: 20151216

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: 20151216

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: 20151216

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: 20160317

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: 20151216

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: 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: 20151216

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: 20151216

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: 20151216

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: 20151216

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: 20160416

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: 20160418

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: 20151216

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: 20151216

REG Reference to a national code

Ref country code: DE

Ref legal event code: R026

Ref document number: 602011022047

Country of ref document: DE

PLBI Opposition filed

Free format text: ORIGINAL CODE: 0009260

PLAX Notice of opposition and request to file observation + time limit sent

Free format text: ORIGINAL CODE: EPIDOSNOBS2

26 Opposition filed

Opponent name: HENKEL AG & CO. KGAA

Effective date: 20160915

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: 20151216

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: 20151216

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: 20151216

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

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: 20151216

REG Reference to a national code

Ref country code: CH

Ref legal event code: PL

PLBB Reply of patent proprietor to notice(s) of opposition received

Free format text: ORIGINAL CODE: EPIDOSNOBS3

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: 20151216

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: CH

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20160731

Ref country code: LI

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20160731

REG Reference to a national code

Ref country code: IE

Ref legal event code: MM4A

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: IE

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20160704

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 NON-PAYMENT OF DUE FEES

Effective date: 20160704

REG Reference to a national code

Ref country code: DE

Ref legal event code: R100

Ref document number: 602011022047

Country of ref document: DE

PLCK Communication despatched that opposition was rejected

Free format text: ORIGINAL CODE: EPIDOSNREJ1

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: 20151216

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

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 NON-PAYMENT OF DUE FEES

Effective date: 20160731

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: 20151216

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: 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: 20151216

PLBN Opposition rejected

Free format text: ORIGINAL CODE: 0009273

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: OPPOSITION REJECTED

27O Opposition rejected

Effective date: 20180417

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: 20151216

REG Reference to a national code

Ref country code: DE

Ref legal event code: R081

Ref document number: 602011022047

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