WO2014095617A1 - Compositions d'élimination de taches - Google Patents

Compositions d'élimination de taches Download PDF

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Publication number
WO2014095617A1
WO2014095617A1 PCT/EP2013/076514 EP2013076514W WO2014095617A1 WO 2014095617 A1 WO2014095617 A1 WO 2014095617A1 EP 2013076514 W EP2013076514 W EP 2013076514W WO 2014095617 A1 WO2014095617 A1 WO 2014095617A1
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WO
WIPO (PCT)
Prior art keywords
fabric
stain removal
arginine
removal composition
stain
Prior art date
Application number
PCT/EP2013/076514
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English (en)
Inventor
Ravine Anthony Gungabissoon
Original Assignee
Unilever Plc
Unilever N.V.
Conopco, Inc., D/B/A Unilever
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
Application filed by Unilever Plc, Unilever N.V., Conopco, Inc., D/B/A Unilever filed Critical Unilever Plc
Priority to CN201380067688.9A priority Critical patent/CN104903433A/zh
Priority to BR112015013067-4A priority patent/BR112015013067B1/pt
Priority to EP13803053.1A priority patent/EP2935549B1/fr
Publication of WO2014095617A1 publication Critical patent/WO2014095617A1/fr

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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
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/26—Organic compounds containing nitrogen
    • C11D3/33—Amino carboxylic acids

Definitions

  • This invention relates to fabric stain removal compositions for ambient-active fat/oil based stains, particularly but not exclusively as a pre-treatment or direct application.
  • aqueous substrate cleaning is performed at cold or ambient temperatures. These temperatures are a challenge for fat/oil stain removal technology which relies on water temperatures of 40 - 70 degrees. In the case of modern washing machines, stain removal mainly relies largely on the heating of water above ambient temperatures in the washing machine. This accounts for a large proportion of the laundry related greenhouse gas footprint which needs reducing for environmental reasons.
  • the objective of the invention is the removal of fabric stains from stained fabric, where the fabric stains comprise fat/oil.
  • the present invention provides a fabric stain removal composition comprising an arginine compound and a surfactant.
  • the invention provides a method for removing a stain from a stained fabric, comprising the step of applying to the stain, the fabric stain removal composition of the first aspect of the invention.
  • a pre-treatment device comprising (i) a storage chamber storing the fabric stain removal composition of the first aspect of the invention and a (i) dispenser for applying said composition to a stain on a fabric, the pre-treatment device preferably being suitable for use in the method of the second aspect.
  • the invention provides use of arginine compound, preferably in combination with a surfactant, in the removal of oil/fat stains from a stained fabric, preferably in the removal of fat stains.
  • the removal of oil/fat stains at low temperatures is radically improved and so offers improved laundry cleaning in regions where ambient washing occurs out of habit or necessity. Improved washing performance at lower temperatures is generally desirable but increased low temperature performance may also help inhibit the adoption of hot water washing in these countries, a rising trend as standards of living increase and more people are able to afford washing machines.
  • the invention provides stain removal performance of fat based soil and/or stains in an ambient temperature cleaning processes (with low temperature wash liquor) without serious consideration to the temperature sensitivity of ingredients during storage.
  • the formulation can therefore be designed more freely, on the basis of other considerations.
  • the term “substrate” includes fabric, and clothing and other surfaces such as cutlery, crockery and other domestic hard surfaces.
  • arginine compound is intended to include any suitable arginine compound, including stereoisomeric and racemic forms, derivatives, and substituted derivative and mixtures thereof.
  • ambient-active is intended to mean less that 25 degrees Celcius and preferably 22 degrees Celcius or less, more preferably 15 degrees or less but always greater than 1 degree Celcius and "active" means effective in achieving stain removal.
  • stain removal is means removal as measured in terms of
  • Remission units or a Remission index For a visible (by the human eye) effect, effective stain removal is represented by remission equal to or greater than 2 Remission units and preferably greater or equal to 5 units.
  • wt% means “% by weight”. Unless specified otherwise, all percentages mentioned herein are by weight calculated relative to the total composition.
  • the stain may comprise oil or fat, preferably fat. However, it is often found that other biological material may be included in the stain.
  • the method of the invention preferably comprises an aqueous washing process. Accordingly it is preferred that the method comprises the step of adding water to the composition to form an aqueous wash liquor Preferably the method comprises localised application of the composition to a stain or stained area of the fabric.
  • the method may be pre-treatment method, and be followed by a subsequent aqueous washing step. Pre-treatment steps may take place without further addition of any water (beyond any contained in the composition).
  • the pre-treatment process may comprise the step of soaking the substrate in an aqueous solution to which the treatment composition has been added.
  • the second step of the method of the invention may be a 'main' wash and may be a manual washing process or a washing process in a washing machine.
  • the second step may use any suitable detergent composition.
  • this detergent composition comprises one or more surfactants and/or other functional ingredients, adjuncts etc. as described below.
  • the method of the invention is less than 90 minutes in duration, more preferably less than 60 minutes and most preferably less than 30 minutes.
  • the pre-treatment step is preferably less than 5 minutes, and more preferably less than 2 minutes.
  • the pre-treatment device may be by any suitable device such as roll-on applicator or tube, sprays, aerosols, pastes, a pump-operated dispenser or the like.
  • the pre-treatment device may comprise a scrubbing member having brush, bristles, tufts, projections, embossments etc or any combination thereof to further aid application of the detergent composition to a substrate.
  • the treatment composition is ambient-active. Accordingly, the temperature of the wash liquor step of aqueous washing process is therefore less than 40 °C and preferably less than 30 °C and more preferably less than 25 °C and more preferably less than or equal to 22 °C further more preferably 15°C or less at all times during the washing but excluding drying. Encouraging low temperature wash liquor is advantageous environmentally and financially.
  • the treatment composition of the invention and/or any detergent composition used subsequently may comprise any of the following ingredients.
  • Compositions may comprise enzymes.
  • the enzymes are preferably present at 0.001 - 5%wt more preferably 0.01 - 3%.
  • Enzymes may be from animal, vegetable, bacterial origin (derived from bacteria) or fungal origin (derived from fungus) however enzymes from bacterial origin are preferred. Chemically modified or protein engineered mutants are included.
  • enzymes encoding such enzymes can be transferred from one host to a preferred expression production host which may or may not be the same as the original host.
  • the term "enzyme” includes enzyme variants (produced, for example, by recombinant techniques) are included. Examples of such enzyme variants are disclosed, e.g., in EP 251 ,446 (Genencor), WO 91 /00345 (Novo Nordisk), EP 525,610 (Solvay) and WO 94/02618 (Gist-Brocades NV).
  • the one or more enzymes preferably comprise a protease.
  • Preferred proteases are serine proteases or metallo proteases, preferably an alkaline microbial protease or a trypsin-like protease.
  • protease enzymes include AlcalaseTM, SavinaseTM, PrimaseTM, DuralaseTM, DyrazymTM, EsperaseTM, EverlaseTM, PolarzymeTM, and KannaseTM, (Novozymes A/S), MaxataseTM, MaxacalTM, MaxapemTM,
  • the one or more enzymes preferably comprises an amylase.
  • Suitable amylases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
  • Amylases include, for example, alpha-amylases obtained from Bacillus, e.g. a special strain of B. licheniformis, described in more detail in GB 1 ,296,839, or the Bacillus sp. strains disclosed in WO 95/026397 or WO 00/060060.
  • amylases are DuramylTM, TermamylTM, Termamyl UltraTM, NatalaseTM, StainzymeTM, FungamylTM and BANTM (Novozymes A/S), RapidaseTM and PurastarTM (from Genencor International IncCommercially available amylases include StainzymeTM (Novozymes).
  • the one or more enzymes preferably comprise a lipase and in such cases, the preferred lipases include first wash lipases which comprise a polypeptide having an amino acid sequence which has at least 90 percent sequence identity with the wild-type lipase derived from Humicola lanuginosa strain DSM 4109 and compared to said wild-type lipase, comprises a substitution of an electrically neutral or negatively charged amino acid within 15 A of E1 or Q249 with a positively charged amino acid; and may further comprise: (I) a peptide addition at the C-terminal;
  • i. comprises a negatively charged amino acid in position E210 of said wild-type lipase
  • ii. comprises a negatively charged amino acid in the region corresponding to positions 90-101 of said wild-type lipase
  • iii. comprises a neutral or negatively charged amino acid at a position corresponding to N94 of said wild-type lipase
  • iv. has a negative charge or neutral charge in the region corresponding to positions 90-101 of said wild-type lipase
  • lipases from Humicola (synonym Thermomyces), e.g. from other H. lanuginosa ( ⁇ . lanuginosus) strains or from H. insolens, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes, P.
  • P. wisconsinensis a Bacillus lipase, e.g. from B. subtilis (Dartois et al. (1993), Biochemica et Biophysica Acta, 1 131 , 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91 /16422).
  • B. subtilis Dartois et al. (1993), Biochemica et Biophysica Acta, 1 131 , 253-360
  • B. stearothermophilus JP 64/744992
  • B. pumilus WO 91 /16422
  • lipase enzymes include LipolaseTM and Lipolase UltraTM, and the Bacterial enzyme, Lipomax ® ex Genecor.
  • the one or more enzymes preferably comprise 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 which 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
  • Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
  • the one or more enzymes preferably 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.
  • the one or more enzymes preferably comprise a cellulase preferably including those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g.
  • the one or more enzymes preferably comprise a peroxidase/oxidase are especially of bacterial origin. Chemically modified or protein engineered mutants are included.
  • An example of an oxidative bacterium is, but not limited to, are Aeromonas sp wherefrom oxidases can be sourced.
  • the one or more enzymes preferably comprise a pectate lyase (also called polygalacturonate lyases):
  • pectate lyases include pectate lyases that have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, as well as from Bacillus subtilis (Nasser et al. (1993) FEBS Letts. 335:319-326) and Bacillus sp. YA-14 (Kim et al. (1994) Biosci.
  • the pectate lyase comprises the pectate lyase disclosed in Heffron et al., (1995) Mol. Plant-Microbe Interact. 8: 331 -334 and Henrissat et al., (1995) Plant Physiol. 107: 963-976.
  • pectatel lyases are disclosed in WO 99/27083 and WO 99/27084.
  • pectate lyases derived from Bacillus licheniformis
  • US patent no. 6,284,524 which document is hereby incorporated by reference
  • pectate lyase variants are disclosed in WO 02/006442, especially the variants disclosed in the Examples in WO 02/006442 (which document is hereby incorporated by reference).
  • alkaline pectate lyases include BIOPREPTM and
  • the one or more enzymes preferably comprise a Mannanase:
  • mannanases include mannanases of bacterial and fungal origin.
  • the mannanase is derived from a strain of the filamentous fungus genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus (WO 94/25576).
  • WO 93/24622 discloses a mannanase isolated from Trichoderma reseei. Mannanases have also been isolated from several bacteria, including Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol.56, No. 1 1 , pp.
  • JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp.
  • JP-A- 63056289 describes the production of an alkaline, thermostable beta-mannanase.
  • JP-A-63036775 relates to the Bacillus microorganism FERM P-8856 which produces beta-mannanase and beta-mannosidase.
  • JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001 .
  • a purified mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/1 1 164.
  • WO 91 /18974 describes a hemicellulase such as a glucanase, xylanase or
  • mannanase active Contemplated are the alkaline family 5 and 26 mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp., and Humicola insolens disclosed in WO 99/64619. Especially contemplated are the Bacillus sp. mannanases concerned in the Examples in WO 99/64619. Examples of commercially available mannanases include MannawayTM available from Novozymes A/S Denmark.
  • the enzyme and any perfume/fragrance or pro-fragrance present may show some interaction and should be chosen such that this interaction is not negative. Some negative interactions may be avoided by encapsulation of one or other of enzyme and pro-fragrance and/or other segregation within the product.
  • the enzymes may be provided as an enzyme system.
  • the surfactant may be a synthetic surfactant or a biosurfactant which is mircrobially synthesized e.g. from bacteria, fungi or other microbe.
  • biosurfactant preferably comprises a microbially-derived biosurfactant.
  • a glycolipid biosurfactant which may be a rhamnolipid or sophorolipid or trehalolipid or a mannosylerythritol lipid (MEL).
  • MEL mannosylerythritol lipid
  • the biosurfactant may advantageously comprise a cellobiose, peptide based biosurfactants, lipoproteins and lipopeptides e.g. surfactin, fatty acids e.g. corynomucolic acids (preferably with hydrocarbon chain C12-C14) , phospholipids e.g.
  • hexadecane to less than 1 mN m-1 and CMC of 30 mg L-1 (Kretschner et al., 1982) and Spiculisporic acid; polymeric biosurfactants including emulsan, liposan, mannoprotein and polysaccharide-protein complexes.
  • the biosurfactant comprises a rhamnolipid.
  • the surfactant may be present by weight in the compositions at a level of from 3 to 85% by weight, preferably from 3 to 60% by weight, more preferably from 3 to 40% by weight, most preferably from 3 to 35% by weight.
  • the anionic surfactant is present at a level of from 0.1 to 95% by weight, preferably from 1 to 50% by weight, more preferably from 1 .5 to 25% by weight based on total weight of surfactants present.
  • the surfactant is an anionic surfactant.
  • Anionic surfactants are defined herein as amphiphilic molecules comprising one or more functional groups that exhibit a net anionic charge when in aqueous solution at the normal wash pH of between 6 and 1 1 .
  • Preferred anionic biosurfactants are rhamnolipds and lactonic forms of
  • Biosurfactants which are not expressed biologically in anionic form but have been modified to provide/improve anionic properties are included in the invention.
  • Preferred synthetic anionic surfactants are the alkali metal salts of organic sulphur reaction products having in their molecular structure an alkyl radical containing from about 6 to 24 carbon atoms and a radical selected from the group consisting of sulphonic and sulphuric acid ester radicals.
  • anionic surfactant hereinafter described can be used, such as alkyl ether sulphates, soaps, fatty acid ester sulphonates, alkyl benzene sulphonates, sulphosuccinate esters, primary alkyl sulphates, olefin sulphonates, paraffin sulphonates and organic phosphate; preferred anionic surfactants are the alkali and alkaline earth metal salts of fatty acid carboxylates, fatty alcohol sulphates, preferably primary alkyl sulfates, more preferably they are ethoxylated, for example alkyl ether sulfates; and alkylbenzene sulfonates or mixtures thereof.
  • Amphoteric surfactants and/or zwitterionic surfactants may be present in the compositions according to the invention.
  • the pH of the wash liquor is preferably of between 6 and 10.
  • an amphoteric or zwitterionic surfactant is present at a level of from 0.1 to 20% by weight, more preferably from 0.25 to 15% by weight, even more preferably from 0.5 to 10% by weight.
  • Suitable zwitterionic surfactants are exemplified as those which can be broadly described as derivatives of aliphatic quaternary ammonium, sulfonium and phosphonium compounds with one long chain group having about 8 to about 18 carbon atoms and at least one water solubilizing radical selected from the group consisting of sulfate, sulfonate, carboxylate, phosphate or phosphonate.
  • a general formula for these compounds is:
  • R contains an alkyl, alkenyl or hydroxyalkyi group with 8 to 18 carbon atoms, from 0 to 10 ethylene-oxy groups or from 0 to 2 glyceryl units;
  • Y is a nitrogen, sulfur or phosphorous atom;
  • R 2 is an alkyl or hydroxyalkyi group with 1 to 3 carbon atoms;
  • x is 1 when Y is a sulfur atom and 2 when Y is a nitrogen or phosphorous atom;
  • R 3 is an alkyl or hydroxyalkyi group with 1 to 5 carbon atoms and Z is a radical selected from the group consisting of sulfate, sulfonate, carboxylate, phosphate or phosphonate.
  • Preferred amphoteric surfactants are amine oxides, for example coco dimethyl amine oxide.
  • Preferred zwitterionic surfactants are betaines, and especially amidobetaines.
  • Preferred betaines are C 8 to ds alkyl amidoalkyl betaines, for example coco amido betaine. These may be included as co-surfactants, preferably present in an amount of from 0 to 10 wt %, more preferably 1 to 5 wt %, based on the weight of the total composition.
  • amphoteric or zwitterionic surfactants for incorporation in the
  • composition according to the present invention are betaine surfactants. Examples of these are mentioned in the following list.
  • the sulfatobetaines such as 3-(dodecyldimethylammonium)-1 -propane sulfate; and 2-(cocodimethylammonium)-1 -ethane sulfate.
  • the sulfobetaines such as: 3-(dodecyldimethyl-ammonium)-2-hydroxy-1 -propane sulfonate; 3-(tetradecyl-dimethylammonium)-1 -propane sulfonate; 3-(C-i 2 -C-i 4 alkyl- amidopropyldimethylammonium)-2-hydroxy-1 -propane sulfonate; and 3- (cocodimethylammonium)-l -propane sulfonate.
  • the carboxybetaines such as (dodecyldimethylammonium) acetate (also known as lauryl betaine); (tetradecyldimethylammonium) acetate (also known as myristyl betaine); (cocodimethylammonium) acetate (also known as coconut betaine); (oleyldimethylammonium) acetate (also known as oleyl betaine);
  • the sulfoniumbetaines such as: (dodecyldimethylsulfonium) acetate; and 3- (cocodimethyl-sulfonium)-l -propane sulfonate.
  • the phosphoniumbetaines such as 4-(trimethylphosphonium)-1 -hexadecane sulfonate; 3-(dodecyldimethylphosphonium)-1 -propanesulfonate; and
  • compositions according to the present invention preferably comprise carboxybetaines or sulphobetaines as amphoteric or zwitterionic surfactants, or mixtures thereof. Especially preferred is lauryl betaine.
  • compositions may further comprise, colorants, pearlisers and/or opacifiers, and shading dye.
  • Shell C-
  • LAS acid C-
  • detergent formulations according to the invention were tested to determine their ability to treat i.e. remove beef fat stains from cotton fabric. End-point Stain Removal Assay
  • Reagents - CS46B (Beef fat, coloured) stained cloth (Testfabrics Inc.) was hole punched into discs and transferred to 300 ⁇ I 96 well plates.
  • composition A 5 mg/L 100 ⁇ I
  • Control Mixture Compostion A 5 mg/L 100 ⁇ I
  • deltaE [ ( ⁇ L) 2 + ( ⁇ a) 2 + ( ⁇ b) 2 ] 1/2
  • ⁇ L is a measure of the difference in darkness between the washed and white cloth
  • ⁇ a and ⁇ b are measures for the difference in redness and yellowness respectively between both cloths.
  • CIE Commission International de I'Eclairage
  • Stain removal is measured in terms of Remission units or a Remission index. For a visible (by the human eye) effect, effective stain removal is preferably represented by remission equal to or greater than 2 Remission units and more preferably greater or equal to 5 units.
  • Table 1 End-point stain removal assays using CS46B stained cloth treated with a range of arginine concentrations in MTS24 formulation. Four replicates were performed in parallel on the same 96 well plate. The plates were scanned and the SRI values calculated
  • figure 1 is a Graph displaying the average SRI for replicates 1 -4 from Table 1 vs arginine concentration. Error bars display standard deviation between the four replicates for each concentration.
  • the tergotometer (SR Lab Instruments) allows a scaled reproduction of larger agitator type washers. This device was used to assess the cleaning activity of arginine on different fat-based stained cloth in Composition A.
  • Arginine was applied using two different approaches: (i) by including it in the formulation containing wash mixture or (ii) pre-treating the cloth with a solution of arginine before washing.
  • the volume was made up to 500 ml with demineralised water.
  • composition A 0.57 ml
  • the volume was made up to 500 ml with demineralised water. Wash conditions: 1 hour at 22 C
  • composition A 0.57 ml
  • the volume was made up to 500 ml with demineralised water. Wash conditions: 1 hour at 22 C After washing the cloths were rinsed for 5 X 2 mins in demineralised water and air dried over night. When fully dry, the cloths were digitally scanned, their delta E measured and SRI calculated as described previously.
  • Table 2 Tergotometerassay using CS46B stained cloth washed with 1 mg/ml and 10 mg/ml arginine in MTS24 formulation. 4 replicates were performed in parallel (2 X replicate per Tergotometerpot).
  • Figure 2 is a Bar chart displaying the average SRI for replicates 1 -4 from Table 2 vs arginine concentration. Error bars display standard deviation between the four replicates for each concentration.
  • Table 3 Tergotometerassay using CS46B stained cloth pre-treated with 1 mg/ml and 10 mg/ml arginine and then washed in MTS24 formulation. 4 replicates were performed in parallel (2 X replicate per Tergotometerpot).
  • Results of Table 3 are shown in Figure 3: a Bar chart displaying the average SRI for replicates 1 -4 from Table 3 vs arginine concentration. Error bars display standard deviation between the four replicates for each concentration.
  • Table 4 Tergotometerassay using Lard & Violet Dye stained cloth washed with 1 mg/ml and 10 mg/ml arginine in MTS24 formulation. 4 replicates were performed in parallel (2 X replicate per Tergotometerpot).
  • Results of table 4 are shown in Figure 4: a Bar chart displaying the average SRI for replicates 1 -4 from Table 4 vs arginine concentration. Error bars display standard deviation between the four replicates for each concentration.
  • Table 5 Tergotometerassay using Lard & Violet Dye stained cloth pre-treated with 1 mg/ml and 10 mg/ml arginine and then washed in MTS24 formulation. 4 replicates were performed in parallel (2 X replicate per Tergotometerpot).
  • Table 6 Tergotometerassay using Hamburger Grease & Violet Dye stained cloth washed with 1 mg/ml and 10 mg/ml arginine in MTS24 formulation. 4 replicates were performed in parallel (2 X replicate per Tergotometerpot).
  • Table 6 The results of table 6 are shown in Figure 6: a Bar chart displaying the average SRI for replicates 1 -4 from Table 6 vs arginine concentration. Error bars display standard deviation between the four replicates for each concentration.
  • Table 7 Tergotometerassay using Hamburger Grease & Violet Dye stained cloth pre-treated with 1 mg/ml and 10 mg/ml arginine and then washed in MTS24 formulation. 4 replicates were performed in parallel (2 X replicate per
  • Table 7 The results of table 7 are shown in Figure 7: a Bar chart displaying the average SRI for replicates 1 -4 from Table 7 vs arginine concentration. Error bars display standard deviation between the four replicates for each concentration.
  • Table 8 Tergo-O-tometer assay using Artificial Sebum stained cloth washed with 1 mg/ml and 10 mg/ml arginine in MTS24 formulation. 4 replicates were performed in parallel (2 X replicate per Tergo-O-tometer pot).
  • arginine improves removal of the fat-based stains tested, treatment of the stained cloth with arginine prior to washing in a surfactant containing composition A also improves stain removal.

Abstract

La présente invention concerne une composition d'élimination de taches sur un tissu comprenant un composé à base d'arginine et un agent tensioactif.
PCT/EP2013/076514 2012-12-20 2013-12-13 Compositions d'élimination de taches WO2014095617A1 (fr)

Priority Applications (3)

Application Number Priority Date Filing Date Title
CN201380067688.9A CN104903433A (zh) 2012-12-20 2013-12-13 去污组合物
BR112015013067-4A BR112015013067B1 (pt) 2012-12-20 2013-12-13 Método para remover uma mancha compreendendo gordura/óleo de um tecido manchado e uso de um composto de arginina
EP13803053.1A EP2935549B1 (fr) 2012-12-20 2013-12-13 Méthode d'élimination de taches de graisse et/ou d'huile

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EP12198568.3 2012-12-20
EP12198568 2012-12-20

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WO2014095617A1 true WO2014095617A1 (fr) 2014-06-26

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WO2016066464A1 (fr) * 2014-10-28 2016-05-06 Henkel Ag & Co. Kgaa Détergents à base de mannosylérythritollipide
US11918680B2 (en) 2015-12-31 2024-03-05 Colgate-Palmolive Company Cleansing compositions

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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2016066464A1 (fr) * 2014-10-28 2016-05-06 Henkel Ag & Co. Kgaa Détergents à base de mannosylérythritollipide
US11918680B2 (en) 2015-12-31 2024-03-05 Colgate-Palmolive Company Cleansing compositions

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EP2935549A1 (fr) 2015-10-28
BR112015013067B1 (pt) 2021-11-30
EP2935549B1 (fr) 2018-09-26
CN104903433A (zh) 2015-09-09
BR112015013067A8 (pt) 2019-10-08
BR112015013067A2 (pt) 2017-07-11

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