EP2935549B1 - Verfahren zur fett- und/oder ölfleckenentfernung - Google Patents

Verfahren zur fett- und/oder ölfleckenentfernung Download PDF

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Publication number
EP2935549B1
EP2935549B1 EP13803053.1A EP13803053A EP2935549B1 EP 2935549 B1 EP2935549 B1 EP 2935549B1 EP 13803053 A EP13803053 A EP 13803053A EP 2935549 B1 EP2935549 B1 EP 2935549B1
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Prior art keywords
arginine
sri
fabric
stain
stain removal
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English (en)
French (fr)
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EP2935549A1 (de
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Ravine Anthony Gungabissoon
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Unilever PLC
Unilever NV
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Unilever PLC
Unilever NV
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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
    • 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 methods 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 invention provides a method for removing a stain comprising fat/oil from a stained fabric, comprising the step of applying to the stain, a fabric stain removal composition comprising an arginine compound and a surfactant.
  • the invention provides a method of the first aspect of the invention, wherein the step of applying the fabric stain removal composition is a pre-treatment step using a pre-treatment device, wherein the pre-treatment device comprises (i) a storage chamber storing said fabric stain removal composition and (ii) a dispenser for locally applying said fabric stain removal composition to a stain on a fabric.
  • 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, at ambient temperatures.
  • 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.
  • 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
  • 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. Genes 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, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).
  • 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:
  • lipases include lipases from Humicola (synonym Thermomyces ), e.g. from other H. lanuginosa ( T. lanuginosus ) strains or from H. insolens, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. stutzeri, P. fluorescens, Pseudomonas sp. strain SD 705 ( WO 95/06720 and WO 96/27002 ), P. wisconsinensis, a Bacillus lipase, e.g. from B.
  • subtilis ( Dartois et al. (1993), Biochemica et Biophysica Acta, 1131, 253-360 ), B. stearothermophilus ( JP 64/744992 ) or B. pumilus ( WO 91/16422 ).
  • lipase enzymes include LipolaseTM and Lipolase UltraTM, and the Bacterial enzyme, Lipomax ® ex Genecor. This is a bacterially derived Lipase, of variant M21L 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).
  • 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.
  • phospholipases A1 and A2 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.
  • 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.
  • Preferably 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. Biotech. Biochem. 58:947-949 ).
  • 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 SCOURZYMETM L from Novozymes A/S, Denmark.
  • 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. 11, 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 97/11164 .
  • WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active.
  • mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp., and Humicola insolens disclosed in WO 99/64619 .
  • 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.
  • the biosurfactant preferably comprises a microbially-derived biosurfactant.
  • it comprises 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. Phosphatidylethanolamine produced by Rhodococcus erythropolis grown on n-alkane resulted in the lowering of interfacial tension between water and 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 11.
  • Preferred anionic biosurfactants are rhamnolipds and lactonic forms of sophorolipids. 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.
  • R 1 (R 2 ) x Y + R 3 Z - wherein R 1 contains an alkyl, alkenyl or hydroxyalkyl 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 hydroxyalkyl 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 hydroxyalkyl 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 C 18 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.
  • Preferred 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 12 -C 14 alkyl-amidopropyldimethylammonium)-2-hydroxy-1-propane sulfonate; and 3-(cocodimethylammonium)-1-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); (dodecyloxymethyldimethylammonium) acetate; and (cocoamidopropyldimethylammonium) acetate (also known as cocoamido-propyl betaine or CAPB).
  • dodecyldimethylammonium acetate also known as lauryl betaine
  • tetradecyldimethylammonium) acetate also known as myristyl betaine
  • cocodimethylammonium) acetate also known as coconut betaine
  • oleyldimethylammonium
  • the sulfoniumbetaines such as: (dodecyldimethylsulfonium) acetate; and 3-(cocodimethyl-sulfonium)-1-propane sulfonate.
  • the phosphoniumbetaines such as 4-(trimethylphosphonium)-1-hexadecane sulfonate; 3-(dodecyldimethylphosphonium)-1-propanesulfonate; and 2-(dodecyldimethylphosphonium)-1-ethane sulfate.
  • 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.
  • detergent formulations according to the invention were tested to determine their ability to treat i.e. remove beef fat stains from cotton fabric.
  • Test Mixture according to the invention Composition A 5 mg/L 100 ⁇ l Arginine dilution* 20 ⁇ l Distilled water 60 ⁇ l *Arginine diluted to the following mg/ml concentrations in distilled water: 0.16, 0.32, 0.64, 1.28, 2.56, 5.12 and 10.24.
  • Control Mixture Compostion A 5 mg/L 100 ⁇ l Distilled water 100 ⁇ l
  • 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.
  • 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.
  • the volume was made up to 500 ml with demineralised water.
  • the volume was made up to 500 ml with demineralised water.
  • 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).
  • Table 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 5 The results of table 5 are shown in Figure 5 : a Bar chart displaying the average SRI for replicates 1-4 from Table 5 vs arginine concentration. Error bars display standard deviation between the four replicates for each concentration.
  • 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 Tergotometerpot).
  • 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).
  • Table 8 The results of table 8 are shown in Figure 8 : a Bar chart displaying the average SRI for replicates 1-4 from Table 8 vs arginine concentration. Error bars display standard deviation between the four replicates for each concentration.
  • arginine improves removal of the fat-based stains tested.
  • Pre-treatment of the stained cloth with arginine prior to washing in a surfactant containing composition A also improves stain removal.

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Claims (8)

  1. Verfahren zum Entfernen eines Fett/Öl umfassenden Flecks aus einem verschmutzten Stoff, umfassend den Schritt des Aufbringens einer Textilfleckentfernungszusammensetzung, die eine Argininverbindung und ein Tensid umfasst, auf den Fleck.
  2. Verfahren nach Anspruch 1, wobei das Tensid ein anionisches Tensid umfasst.
  3. Verfahren nach Anspruch 2, wobei das Tensid ein Rhamnolipid umfasst.
  4. Verfahren nach irgendeinem vorhergehenden Anspruch, wobei die Textilfleckentfernungszusammensetzung umgebungs-aktiv ist.
  5. Verfahren nach irgendeinem vorhergehenden Anspruch, umfassend den Schritt der Zugabe von Wasser zu der Textilfleckentfernungszusammensetzung, um eine wässrige Waschlauge zu bilden.
  6. Verfahren nach irgendeinem der Ansprüche 1 bis 4, umfassend die lokalisierte Aufbringung der Textilfleckentfernungszusammensetzung wie in den Ansprüchen 1-4 definiert auf einen Fett/Öl umfassenden Fleck auf einem verschmutzten Stoff.
  7. Verfahren nach irgendeinem vorhergehenden Anspruch, wobei der Schritt des Aufbringens der Textilfleckentfernungszusammensetzung ein Vorbehandlungsschritt ist, bei dem eine Vorbehandlungsvorrichtung verwendet wird, wobei die Vorbehandlungsvorrichtung (i) eine Aufbewahrungskammer, in der die Textilfleckentfernungszusammensetzung wie in irgendeinem der Ansprüche 1-4 definiert gelagert wird, und (ii) einen Spender zum lokalen Aufbringen der Textilfleckentfernungszusammensetzung auf einen Fleck auf einem Stoff umfasst.
  8. Verwendung einer Argininverbindung bei der Entfernung eines Öl-/Fettflecks aus einem verschmutzten Stoff bei Umgebungstemperaturen, bevorzugt in Kombination mit Tensid.
EP13803053.1A 2012-12-20 2013-12-13 Verfahren zur fett- und/oder ölfleckenentfernung Active EP2935549B1 (de)

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EP13803053.1A EP2935549B1 (de) 2012-12-20 2013-12-13 Verfahren zur fett- und/oder ölfleckenentfernung
PCT/EP2013/076514 WO2014095617A1 (en) 2012-12-20 2013-12-13 Stain removal compositions

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EP2935549B1 true EP2935549B1 (de) 2018-09-26

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EP2935549A1 (de) 2015-10-28
CN104903433A (zh) 2015-09-09
BR112015013067B1 (pt) 2021-11-30
BR112015013067A8 (pt) 2019-10-08
WO2014095617A1 (en) 2014-06-26
BR112015013067A2 (pt) 2017-07-11

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