WO2012010406A1 - Combinaisons de rhamnolipides et d'enzymes pour nettoyage amélioré - Google Patents
Combinaisons de rhamnolipides et d'enzymes pour nettoyage amélioré Download PDFInfo
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- WO2012010406A1 WO2012010406A1 PCT/EP2011/061214 EP2011061214W WO2012010406A1 WO 2012010406 A1 WO2012010406 A1 WO 2012010406A1 EP 2011061214 W EP2011061214 W EP 2011061214W WO 2012010406 A1 WO2012010406 A1 WO 2012010406A1
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- rhamnolipids
- rhamnolipid
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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
- C11D1/37—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
- 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
- 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
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- 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 (RhaCi 0 Ci 0 ). It may be referred to as Rha-Ci 0 -Ci 0 , with a formula of C26H48O9.
- Mono-rhamnolipids have a single rhamnose sugar ring.
- the lUPAC 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 (Rha2Ci 0 Ci 0 ). It may be referred to as Rha- Rha-C-io-C-io, with a formula of C 3 2H5 8 0i 3 .
- the lUPAC name is 3-[3-[4,5-dihydroxy-6-methyl-3- (3 ,4 , 5-tri hyd roxy-6-m ethyloxan-2-yl)oxyoxan-2-yl]oxyd ecanoyloxy]d ecanoic acid .
- rhamnolipid 2 is a mono-rhamnolipid and "rhamnolipid 1 " is a di-rhamnolipid. This leads to some ambiguity in the usage or "RL1 " and “RL2” in the literature. Throughout this patent specification, we use the terms mono- and di-rhamnolipid in order to avoid this possible confusion. However, if abbreviations are used R1 is mono-rhamnolipid and R2 is di-rhamnolipid. For more information on the confusion of terminology in the prior art see the introduction to US 4814272.
- Rha-Rha-C 8 -Cio Rha-Rha-C 8 -Ci 2: i , Rha-Rha-Ci 0 -C 8 , Rha-Rha-Ci 0 -Ci 0 , Rha-Rha-Cio-Ci 2: i , Rha-
- Rhamnolipids produced by P. aeruginosa (unidentified as either mono- or di-rhamnolipids):
- Rha-Cio-C ⁇ 8 Rha-C"io-C"io> Rha-Ci2-Cio
- Rhamnolipids produced by Burkholdera pseudomallei (di-rhamnolipids only):
- 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.
- the bacterium Pseudomonas aeruginosa is found naturally in soils, in water, and on plants.
- P. aeruginosa is chemoheterotrophic, generally aerobic, utilizing a wide range of organic compounds for sources of carbon and nitrogen.
- ATCC American Type Culture Collection
- strains of P. aeruginosa can be isolated to produce
- 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 (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.
- 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, Carbohyd rases, 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.
- the compositions are used to remove fatty soils from laundry, especially from cotton cloths.
- 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. For environmental reasons it is desirable to eliminate this nonionic surfactant from the composition.
- 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.
- biosurfactants are generated by the action of bacteria on renewable feedstocks and are increasingly becoming more and more viable options as sustainable replacements of current synthetic surfactants.
- 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.
- the mono and di rhamnolipid components of the expressed rhamnolipids are extracted and the mono-rhamnolipid is used with lipase superior cleaning results.
- by producing blends and mixing with synthetic anionic surfactants 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, US20021 10854, US6939702, US2009221034, US200802425, US2004053360, US2005281912, US2006075518, US2005059130, US20041542180, US2003199069,
- 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
- 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
- Rhizoctonia in particular Rhizoctonia solani
- Rhizoctonia solani a strain of Rhizoctonia
- Streptomyces in particular Streptomyces scabies, or a strain of Ulocladium, in particular
- 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
- 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. Several types of phospholipase activity can be distinguished, including phospholipases A-i and A 2 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 release diacyl glycerol or phosphatidic acid respectively.
- phospholipase includes enzymes with phospholipase activity, e.g., phospholipase A (A-i 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-i 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.
- 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.
- filamentous fungi e.g., yeast or bacteria
- Aspergillus e.g., A. niger
- Dictyostelium e.g., D. discoideum
- Mucor e.g. M. javanicus, M. mucedo, M. subtil
- 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.
- Serratia e.g., S. liquefasciens, S. marcescens
- Shigella e.g., S. flexneri
- 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 04/1 1 1216, 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-i (EC.
- 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. Cell
- 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 mis 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
- Fungal enzyme is "Lipolase”, derived from Humicola languginosa as described in EP 0 258 068 and available from NovoZymes A S.
- RBR425 Rhamnolipid: a biosurfactant of bacterial origin. Commercially available from Jeneil as RBR425 (25%AM). The composition of this material was analysed and is given in Table 3 below.
- 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 ⁇ .
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Abstract
Priority Applications (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| ES11728878.7T ES2561553T3 (es) | 2010-07-22 | 2011-07-04 | Combinaciones de ramnolípidos y enzimas para una limpieza mejorada |
| CN2011800357973A CN103052704A (zh) | 2010-07-22 | 2011-07-04 | 用于提高清洁的鼠李糖脂和酶的组合物 |
| EP11728878.7A EP2596087B1 (fr) | 2010-07-22 | 2011-07-04 | Combinaisons de rhamnolipides et d'enzymes pour nettoyage amélioré |
| BR112013000108-9A BR112013000108B1 (pt) | 2010-07-22 | 2011-07-04 | composição detergente, seus usos, e processo para a limpeza de um substrato |
| ZA2013/00377A ZA201300377B (en) | 2010-07-22 | 2013-01-15 | Combinations of rhamnolipids and enzymes for improved cleaning |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP10170403 | 2010-07-22 | ||
| EP10170403.9 | 2010-07-22 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO2012010406A1 true WO2012010406A1 (fr) | 2012-01-26 |
Family
ID=43302709
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/EP2011/061214 Ceased WO2012010406A1 (fr) | 2010-07-22 | 2011-07-04 | Combinaisons de rhamnolipides et d'enzymes pour nettoyage amélioré |
Country Status (6)
| Country | Link |
|---|---|
| EP (1) | EP2596087B1 (fr) |
| CN (2) | CN107955721A (fr) |
| BR (1) | BR112013000108B1 (fr) |
| ES (1) | ES2561553T3 (fr) |
| WO (1) | WO2012010406A1 (fr) |
| ZA (1) | ZA201300377B (fr) |
Cited By (25)
| Publication number | Priority date | Publication date | Assignee | Title |
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| WO2014027249A3 (fr) * | 2012-05-07 | 2014-07-17 | Rhodia Operations | Revêtements et peintures aqueux incorporant un ou plusieurs biosurfactants antimicrobiens et leurs procédés d'utilisation |
| EP2786743A1 (fr) * | 2013-04-02 | 2014-10-08 | Evonik Industries AG | Composition de mélange contenant des rhamnolipides |
| EP2787065A1 (fr) * | 2013-04-02 | 2014-10-08 | Evonik Industries AG | Composition détergente pour textiles contenant des rhamnolipides ayant une teneur majoritaire en di-rhamnolipides |
| WO2015091294A1 (fr) * | 2013-12-18 | 2015-06-25 | Unilever Plc | Compositions à base d'un monorhamnolipide |
| WO2015091457A1 (fr) * | 2013-12-19 | 2015-06-25 | Unilever Plc | Composition |
| WO2016055591A1 (fr) | 2014-10-08 | 2016-04-14 | Centre National De La Recherche Scientifique (Cnrs) | Biosurfactants de pseudomonas pour lutter contre les legionelles |
| WO2016066464A1 (fr) * | 2014-10-28 | 2016-05-06 | Henkel Ag & Co. Kgaa | Détergents à base de mannosylérythritollipide |
| DE102014225789A1 (de) | 2014-12-15 | 2016-06-16 | Henkel Ag & Co. Kgaa | Wasch- und Reinigungsmittel |
| WO2016139032A1 (fr) * | 2015-03-02 | 2016-09-09 | Unilever Plc | Compositions aux propriétés réduites en termes de chromo-transfert |
| EP3070155A1 (fr) | 2015-03-18 | 2016-09-21 | Evonik Degussa GmbH | Composition comprenant des peptidases et biotenseurs |
| WO2017036901A1 (fr) * | 2015-08-28 | 2017-03-09 | Unilever Plc | Compositions de lavage améliorées |
| US9884883B2 (en) | 2015-01-12 | 2018-02-06 | Logos Technologies, Llc | Production of rhamnolipid compositions |
| DE102017214265A1 (de) | 2017-08-16 | 2019-02-21 | Henkel Ag & Co. Kgaa | Rhamnolipidhaltige Wasch- und Reinigungsmittel |
| US10259837B2 (en) | 2015-03-02 | 2019-04-16 | Conopco, Inc. | Method of separating rhamnolipids from a fermentation broth |
| WO2019154970A1 (fr) * | 2018-02-09 | 2019-08-15 | Evonik Degussa Gmbh | Composition de mélange comprenant des glucolipides |
| US10829507B2 (en) | 2017-02-06 | 2020-11-10 | Stepan Company | Decolorization of concentrated rhamnolipid composition |
| US20210204571A1 (en) * | 2020-01-06 | 2021-07-08 | Vinay Bhalchandra PARANJPE | Vegetable and Fruit Wash Formulation and Uses Thereof |
| EP4155371A1 (fr) * | 2022-08-29 | 2023-03-29 | Evonik Operations GmbH | Composition riche en mono-rhamnolipides |
| WO2023099346A1 (fr) * | 2021-12-02 | 2023-06-08 | Evonik Operations Gmbh | Composition comprenant des glucolipides |
| EP4198112A1 (fr) | 2021-12-20 | 2023-06-21 | Henkel AG & Co. KGaA | Combinaison tensioactive et produits de lavage et de nettoyage contenant cette combinaison |
| WO2023116569A1 (fr) * | 2021-12-21 | 2023-06-29 | Novozymes A/S | Composition comprenant une lipase et un renforçateur |
| EP4234664A1 (fr) | 2022-02-24 | 2023-08-30 | Evonik Operations GmbH | Composition comprenant des glucolipides et des enzymes |
| EP4353806A1 (fr) | 2022-10-14 | 2024-04-17 | Henkel AG & Co. KGaA | Mélanges de tensioactifs |
| DE102023205205A1 (de) | 2023-06-05 | 2024-12-05 | Henkel Ag & Co. Kgaa | Neue Tensidkombination und Wasch- und Reinigungsmittel, welche diese enthalten |
| DE102023205206A1 (de) | 2023-06-05 | 2024-12-05 | Henkel Ag & Co. Kgaa | Neue Tensidkombination und Wasch- und Reinigungsmittel, welche diese enthalten |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| EP3061442A1 (fr) * | 2015-02-27 | 2016-08-31 | Evonik Degussa GmbH | Composition contenant du rhamnolipide et du siloxane |
| 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 |
| 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 |
| BR112023022205A2 (pt) | 2021-04-29 | 2023-12-19 | Unilever Ip Holdings B V | Processo para converter dirramnolipídeo em monorramnolipídeo |
| CN117280041A (zh) | 2021-04-29 | 2023-12-22 | 联合利华知识产权控股有限公司 | 产生单鼠李糖脂的方法 |
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| 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 |
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2011
- 2011-07-04 WO PCT/EP2011/061214 patent/WO2012010406A1/fr not_active Ceased
- 2011-07-04 CN CN201711278691.1A patent/CN107955721A/zh active Pending
- 2011-07-04 CN CN2011800357973A patent/CN103052704A/zh active Pending
- 2011-07-04 EP EP11728878.7A patent/EP2596087B1/fr active Active
- 2011-07-04 BR BR112013000108-9A patent/BR112013000108B1/pt active IP Right Grant
- 2011-07-04 ES ES11728878.7T patent/ES2561553T3/es active Active
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Also Published As
| Publication number | Publication date |
|---|---|
| BR112013000108B1 (pt) | 2021-05-11 |
| ZA201300377B (en) | 2014-03-26 |
| EP2596087B1 (fr) | 2015-12-16 |
| ES2561553T3 (es) | 2016-02-26 |
| CN103052704A (zh) | 2013-04-17 |
| BR112013000108A2 (pt) | 2017-06-13 |
| CN107955721A (zh) | 2018-04-24 |
| EP2596087A1 (fr) | 2013-05-29 |
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