CN104903433A - Stain removal compositions - Google Patents
Stain removal compositions Download PDFInfo
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- CN104903433A CN104903433A CN201380067688.9A CN201380067688A CN104903433A CN 104903433 A CN104903433 A CN 104903433A CN 201380067688 A CN201380067688 A CN 201380067688A CN 104903433 A CN104903433 A CN 104903433A
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- fabric
- decontaminating composition
- composition
- spot
- arginine
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Classifications
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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
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- 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)
- Cosmetics (AREA)
Abstract
A fabric stain removal composition comprises an arginine compound and a surfactant.
Description
Technical field
The present invention relates to the fabric decontaminating composition of the fats/oils base spot of environment activity, particularly but not exclusively as pre-treatment or directly use.
Background technology
In many weathers and in developing country, sole cleaning is carried out at low or ambient temperatures.It is a challenge that the fats/oils spot of these temperature concerning the water temperature depending on 40-70 degree removes technology.With regard to modern laundry machine, decontamination depends on to a great extent and is heated on envrionment temperature by water in washing machine.This accounts for the significant proportion of the relevant greenhouse gases footprint of laundry, and for environment reason, these footprints need to reduce.
Summary of the invention
The object of the invention is to remove textile stains from staining fabric, wherein said textile stains comprises fats/oils.
In first, the invention provides a kind of fabric decontaminating composition, described composition comprises arginine compounds and tensio-active agent.
In second, the invention provides a kind of method from staining fabric and remove spot, described method comprises the step of the fabric decontaminating composition using the present invention first aspect to spot.
In the 3rd, the invention provides a kind of pretreatment unit, described device comprises (i) and stores the storage vault of the fabric decontaminating composition of the present invention first aspect and (i) for the divider to the spot applying said compositions on fabric, and described pretreatment unit is preferably suitable in the method for second aspect.
In yet another aspect, the invention provides arginine compounds, preferably combining ground with tensio-active agent, for from staining in fabric the purposes removing oil/fatty spot, preferred fat spot.
Embodiment
Use the present invention, the improvement that oil/fatty spot removing at low temperatures obtains fundamentally therefore out of habit or needs and carry out providing in the area of environment washing the clothes washing of improvement.Scourability under the lesser temps improved normally is expected, but the low-temperature performance improved also can contribute to suppressing the employing of hot wash in these countries, along with the raising of the standard of living and more people can afford washing machine, hot wash is in rising trend.To the invention provides in envrionment temperature cleaning process the fatty group dirt of (using cold washing liquid) and/or spot detergency ability and temperature sensitivity without the need to considering composition in storage process carefully.Therefore formula can more freely design based on other consideration.
As used herein, term " substrate " comprises fabric and clothing and other surface as cutter, pottery and other homecare hard surface.
As used herein, term " arginine compounds " is intended to comprise any suitable arginine compounds, comprises stereoisomerism and racemic form, derivative and is substituted derivative and their mixture.
Term " environment activity " be intended to refer to lower than 25 degrees Celsius and preferably 22 or lower, more preferably 15 degrees centigrade or lower but height overall in 1 degree Celsius and " activity " refer to realize in decontamination effective.
As used herein, what " decontamination " referred to alleviate unit (Remission unit) or alleviated that index (Remission index) measures removes.For (passing through human eye) visible effect, effective decontamination alleviates units and alleviation preferably greater than or equal to 5 units represents by being equal to or greater than 2.
As used herein, abbreviation " wt% " refers to " % by weight ".Unless otherwise noted, otherwise all percentage ratios mentioned herein all with the weighing scale calculated relative to total composition.
Described spot can comprise oil or fat, preferred fat.But, usually find may comprise other biological substance in spot.
Method of the present invention preferably includes water washing process.Correspondingly, preferably described method comprises the step adding water to be formed water-washing liquid in described composition.
Preferably, described method comprises to composition described in the spot of fabric or soiled area topical application.Described method can be pretreatment process, heel water-washing step subsequently.Pre-treatment step can be carried out when not adding further any water (except any water contained in the composition).Or or in addition, preprocessing process can comprise step substrate being immersed in and adding wherein in the aqueous solution for the treatment of compositions.
The second step of method of the present invention can be " master " and washes and can be the washing process in hand washing process or washing machine.Second step can use any suitable detergent composition.Preferably this detergent composition comprises one or more tensio-active agents and/or other functional component, auxiliary agent etc., and this will be described below.
With regard to pre-treatment according to the present invention, step subsequently can not need to use arginine compounds further.
Preferably, the method time length of the present invention less than 90 minutes, more preferably less than 60 minutes, most preferably less than 30 minutes.In pre-treatment embodiment, pre-treatment step preferably less than 5 minutes, more preferably less than 2 minutes.
Pretreatment unit can be any suitable device as roller applicator or pipe, atomizer, aerosolizer, paste body, pump-type distributor etc.Pretreatment unit can comprise the scouring component with brush, bristle, tuft, thrust, relief etc. or their any combination, and to help further, detergent composition is based to be used.
Preferably, described treatment compositions is environment activity.Correspondingly, the temperature of the washings step of water washing process therefore in washing process (but not comprising drying) always lower than 40 DEG C, preferably lower than 30 DEG C, more preferably less than 25 DEG C, more preferably less than or equal 22 DEG C, also more preferably 15 DEG C or lower.Promote that cold washing liquid is that environment and economy is favourable.
Treatment in accordance with the present invention composition and/or any detergent composition used subsequently can comprise any following composition.
Composition can comprise enzyme.Enzyme preferably exists with 0.001-5 % by weight, more preferably 0.01-3%.
Enzyme can from animal, plant, bacterial origin (being derived from bacterium) or fungic origin (being derived from fungi), but preferably from the enzyme of bacterial origin.Comprise chemically modified or protein engineering mutant.The gene of this fermentoid of encoding can transfer to preferred Expression product host from a host, and the latter can or can not be identical with initial host.As used herein, term " enzyme " comprises enzyme variant (such as being produced by recombinant technology).The example of this type of enzyme variant is at such as EP 251, have open in 446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525,610 (Solvay) and WO 94/02618 (Gist-Brocades NV).
One or more enzymes described preferably comprise proteolytic enzyme.Preferred proteolytic enzyme is serine protease or metalloprotease, preferably alkaline microbial protease or trypsin like proteases.
Commercially available proteolytic enzyme comprises Alcalase
tM, Savinase
tM, Primase
tM, Duralase
tM, Dyrazym
tM, Esperase
tM, Everlase
tM, Polarzyme
tMand Kannase
tM(Novozymes A/S), Maxatase
tM, Maxacal
tM, Maxapem
tM, Properase
tM, Purafect
tM, Purafect OxP
tM, FN2
tMand FN3
tM(Genencor International Inc.).
One or more enzymes described preferably comprise amylase.Suitable amylase (α and/or β) comprises those of bacterium or fungic origin.Comprise chemically modified or protein engineering mutant.Amylase comprises and such as derives from genus bacillus as GB 1,296, the α-amylase of Bacillus strain disclosed in the special bacterial strain of the Bacillus licheniformis described in more detail in 839 or WO 95/026397 or WO 00/060060.
Commercially available amylase has Duramyl
tM, Termamyl
tM, Termamyl Ultra
tM, Natalase
tM, Stainzyme
tM, Fungamyl
tMand BAN
tM(Novozymes A/S), Rapidase
tMand Purastar
tM(from Genencor International Inc.).Commercially available amylase comprises Stainzyme
tM(Novozymes).
One or more enzymes described preferably comprise lipase, and under these circumstances, preferred lipase comprises the first washing lipase, it comprises the polypeptide that aminoacid sequence and the wild type lipase being derived from Humicola lanuginosa (Humicola lanuginosa) strain DSM 4109 have at least 90% sequence iden, and compared with described wild type lipase, it is included in electric neutrality in the 15A of E1 or Q249 or electronegative amino acid by the amino acid whose replacement of positively charged; And can also comprise:
(I) in the peptide addition of C-end;
(II) in the peptide addition of N-end;
(III) limit below:
I. in the position E210 of described wild type lipase, electronegative amino acid is comprised;
Ii. in the region corresponding to the position 90-101 of described wild type lipase, electronegative amino acid is comprised; With
Iii. the position corresponding to the N94 of described wild type lipase comprises electric neutrality or electronegative amino acid;
Iv. in the region corresponding to the position 90-101 of described wild type lipase, there is negative charge or neutral charge; With
Iv. their mixture.
These lipase can Lipex
tMtrade mark derives from Novozymes.Novozymes is with title Lipoclean
tMdisclose from Novozymes but it is believed that the similar enzyme outside superincumbent definition, and this enzyme is also preferred.
Other possible lipase comprises from Humicola (Humicola, synonym Thermomyces) lipase, such as, from other Humicola lanuginosa (H.lanuginosa or T.lanuginosus) bacterial strain or from Humicola insolens (H.insolens); Pseudomonas Lipases, such as, belong to bacterial strain SD 705 (WO 95/06270 and WO 96/27002), winconsin pseudomonas (P.wisconsinensis) from Pseudomonas alcaligenes (P.alcaligenes) or pseudomonas pseudoalcaligenes (P.pseudoalcaligenes), pseudomonas cepacia (P.cepacia), Pseudomonas stutzeri (P.stutzeri), Pseudomonas fluorescens (P.fluorescens), pseudomonas (Pseudomonas); Genus bacillus lipase, such as from subtilis (the B.subtilis) (people (1993) such as Dartois, Biochemica et Biophysica Acta, 1131,253-360), bacstearothermophilus (B.stearothermophilus) (JP 64/744992) or bacillus pumilus (B.pumilus) (WO 91/16422).
Commercially available lipase comprises Lipolase
tMwith Lipolase Ultra
tMand bacterial enzyme
(from Genecor).This is the bacterial origin lipase of the mutation M21L of the lipase of Pseudomonas alcaligenes, as authorized Gist-Brocades (M.M.M.J.Cox, H.B.M.Lenting, L.J.S.M.Mulleners and J.M.van der Laan) WO 94/25578 described in.
One or more enzymes described preferably comprise the Phospholipid hydrolase classifying as EC 3.1.1.4 and/or EC 3.1.1.32.As used herein, term Phospholipid hydrolase is to the activated enzyme of phosphatide tool.Phosphatide, as Yelkin TTS or Phosphatidycholine, is formed by the glycerine of Phosphation in the 3rd position by two fatty acid esterifications by outside (sn-1) and middle (sn-2) position; Described phosphoric acid then can esterified one-tenth amino alcohol.Phospholipid hydrolase is the enzyme of the hydrolysis participating in phosphatide.Can distinguish the phospholipase activity of some types, comprise: phospholipase A1 and A2, an aliphatic acyl groups (respectively in sn-1 and sn-2 position) hydrolysis is formed lysophospholipid by it; With lysophospholipase (or phospholipase B), the residue aliphatic acyl groups in its hydrolyzable lysophospholipid.Phospholipase C and Phospholipase D (phosphodiesterase) will discharge DG or phosphatidic acid respectively.
One or more enzymes described preferably comprise the at ranged in EC 3.1.1.74.At used according to the invention can be any source.Preferably, at is microbe-derived, particularly bacterium, fungi or yeast sources.
One or more enzymes described preferably comprise cellulase, and described cellulase preferably includes those of bacterium or originated from fungus.Comprise chemically modified or protein engineering mutant.Suitable cellulase comprises from bacillus, Rhodopseudomonas, Humicola, fusarium, Thielavia, the cellulase of Acremonium, such as US 4, 435, 307, US 5, 648, 263, US 5, 691, 178, US 5, 776, 757, WO 89/09259, Humicola insolens (Humicola insolens) is originated from disclosed in WO 96/029397 and WO98/012307, autochthonal shuttle spore mould (Thielavia terrestris), the fungal cellulase of thermophilic fungus destroyed wire (Myceliophthora) and Fusarium oxysporum (Fusarium oxysporum).Commercially available cellulase comprises Celluzyme
tM, Carezyme
tM, Endolase
tM, Renozyme
tM(Novozymes A/S), Clazinase
tMwith Puradax HA
tM(Genencor International Inc.) and KAC-500 (B)
tM(Kao Corporation).
One or more enzymes described preferably comprise the peroxidase/oxydase of especially bacterial origin.Comprise chemically modified or protein engineering mutant.The example of oxidizing bacteria has but is not limited to the Aeromonas (Aeromonas sp) that oxydase can stem from.
One or more enzymes described preferably comprise pectate lyase (also claiming Polygalacturonate lyase): the example of pectate lyase comprises and belonging to as erwinia from different bacterium, Rhodopseudomonas, Klebsiella and xanthomonas and the pectate lyase of cloning from subtilis (people (1993) the FEBS Letts.335:319-326 such as Nasser) and bacillus YA-14 (people (1994) Biosci.Biotech.Biochem.58:947-949 such as Kim).By bacillus pumilus (Bacillus pumilus) (Dave and Vaughn (1971) J.Bacteriol.108:166-352), poly-viscosity bacillus (B.polymyxa) (Nagel and Vaughn (1961) Arch.Biochem.Biophys.93:344-352), bacstearothermophilus (B.stearothermophilus) (Karbassi and Vaughn (1980) Can.J.Microbiol.26:377-384), the purifying within the scope of the pH of 8-10 with the pectate lyase of maximum activity that bacillus (Bacillus sp.) (Hasegawa and Nagel (1966) J.Food Sci.31:838-845) and bacillus RK9 (Bacillus sp.RK9) (Kelly and Fogarty (1978) Can.J.Microbiol.24:1164-1172) produce also is shown in description.When implementing of the present invention, any above-mentioned pectate lyase and divalent cation dependent/non-dependent and/or thermostability pectate lyase can be used.In preferred embodiments, pectate lyase comprises the people such as Heffron, (1995) people such as Mol.Plant-Microbe Interact.8:331-334 and Henrissat, pectate lyase disclosed in (1995) Plant Physiol.107:963-976.The pectate lyase clearly contained has open in WO99/27083 and WO 99/27084.Other pectate lyase clearly contained (being derived from Bacillus licheniformis), at United States Patent (USP) the 6th, has open in 284, No. 524 (this file is incorporated herein by reference).The pectate lyase mutation clearly contained has open in WO02/006442, mutation disclosed in the embodiment especially in WO 02/006442 (this file is incorporated herein by reference).The example of commercially available alkaline pectin hydrochlorate lyase comprises the BIOPREP from Denmark Novozymes A/S
tMand SCOURZYME
tMl.
One or more enzymes described preferably comprise mannase: the example of mannase (EC3.2.1.78) comprises the mannase of bacterium and originated from fungus.In a specific embodiment, mannase is derived from the bacterial strain (WO 94/25576) that filamentous fungus belongs to aspergillus tubigensis, preferably aspergillus niger or microorganism Aspergillus aculeatus.WO 93/24622 discloses a kind of mannase be separated from Trichodermareesei.Mannase also from some bacteria distribution, comprises genus bacillus organism.Such as, the people such as Talbot, Appl.Environ.Microbiol., Vol.56, No.11, pp.3505-3510 (1990) describe a kind of 'beta '-mannase being derived from bacstearothermophilus.The people such as Mendoza, World J.Microbiol.Biotech., Vol.10, No.5, pp.551-555 (1994) describe a kind of 'beta '-mannase being derived from subtilis.JP-A-03047076 discloses a kind of 'beta '-mannase being derived from bacillus.JP-A-63056289 describes the production of a kind of alkalescence, thermally-stabilised 'beta '-mannase.JP-A-63036775 relates to micro-organisms bacillus FERM P-8856, and it produces 'beta '-mannase and beta-Mannosidase.JP-A-08051975 discloses the alkaline ' beta '-mannase belonging to AM-001 from Alkaliphilic bacillus.A kind of purified mannanase from bacillus amyloliquefaciens has open in WO 97/11164.WO 91/18974 describes a kind of hemicellulase as dextranase, zytase or Mannanase Activity thing.Contain alkaline family 5 and 26 mannase being derived from glutinous agar genus bacillus (Bacillus agaradhaerens), Bacillus licheniformis (Bacillus licheniformis), salt tolerant Alkaliphilic bacillus (Bacillus halodurans), Bacillus clausii (Bacillus clausii), bacillus (Bacillus sp.) and Humicola insolens (Humicola insolens) disclosed in WO 99/64619.What especially contain is the bacillus mannase related in the embodiment of WO 99/64619.The example of commercially available mannase comprises the Mannaway that can derive from Denmark Novozymes A/S
tM.
The enzyme existed and any spices/fragrant substance or front perfume (or spice) may demonstrate certain interaction, therefore should be chosen as and make this interaction not be negative.Some negative interactions are by encapsulating one or more enzymes and front perfume (or spice) and/or avoiding with other isolation method in product.Enzyme can provide as enzyme system.
Described tensio-active agent can be synthetic surfactant or with biological mode such as from the bio-surfactant of bacterium, fungi or other Microbe synthesis.Bio-surfactant preferably comprises the bio-surfactant being derived from microorganism.Preferably, it comprises Glycolipids Biosurfactants via, and described Glycolipids Biosurfactants via can be rhamnolipid or sophorolipid or marine alga glycolipid or mannosylerythritol lipid (MEL).Or, bio-surfactant advantageously can comprise cellobiose, bio-surfactant, lipoprotein and lipopeptid based on peptide (such as, Surfactin), lipid acid (such as, corynomucolic acid) (preferably there is hydrocarbon chain C12-C14), phosphatide (such as, by the phosphatidylethanolamine that the Rhodococcus of growth on normal paraffin produces, it causes interfacial tension lowering between water and n-Hexadecane to the CMC lower than 1mN m-1 and 30mg L-1) people such as (, 1982) Kretschner and spiculisporic acid; Polymer-type bio-surfactant, comprises Tego Care PS (emulsan), Thioctic Acid (liposan), Mannoproteins and polysaccharide-protein mixture.
Preferably, bio-surfactant comprises rhamnolipid.
Tensio-active agent can 3 to 85 % by weight, preferably 3 to 60 % by weight, more preferably 3 to 40 % by weight, most preferably 3 to 35 % by weight weight level be present in composition.
Preferably, based on the total weight of the tensio-active agent existed, aniorfic surfactant exists with the level of 0.1 to 95 % by weight, preferably 1 to 50 % by weight, more preferably 1.5 to 25 % by weight.
Preferably, described tensio-active agent is aniorfic surfactant.
Aniorfic surfactant is defined as the amphiphile, amphiphilic molecule comprising one or more functional group in this article, and when when being in the aqueous solution under the Normal Wash pH between 6 and 11, it has clean anionic charge.
Preferred anionic bio-surfactant has the lactonic acid form of rhamnolipid and sophorolipid.Be modified as provide/improve the bio-surfactant of anionic nature to comprise in the present invention not with anionic form biological expression.
Preferred synthetic anionic tensio-active agent is an alkali metal salt of the organosulfur reaction product in its molecular structure with the alkyl radicals containing about 6 to 24 carbon atoms and the atomic group being selected from sulphonate atomic group and sulfuric ester atomic group.
Although any aniorfic surfactant hereinafter described such as sulfated alkyl ether, soap, fatty sulfonate, alkylbenzene sulfonate, sulfosuccinic ester, primary alkyl sulphates, alkene sulfonate, paraffin sulfonate and organophosphate all can use, but preferred aniorfic surfactant is alkali and alkaline earth metal ions salt, the aliphatic alcohol sulfate of fatty acid carboxylate ester, preferred primary alkyl sulphates, more preferably they are ethoxylations, such as sulfated alkyl ether; With alkylbenzene sulfonate or their mixture.
Amphoterics and/or zwitterionics can be present in according in composition of the present invention.For amphoterics, the pH of washings is preferably between 6 and 10.Preferably, both sexes or zwitterionics with 0.1 to 20 % by weight, more preferably 0.25 to 15 % by weight, even more preferably 0.5 to 10 % by weight level exist.
The example of suitable zwitterionics be can broadly be described as having have a long chain alkyl group of about 8 to about 18 carbon atoms and at least one be selected from those of the derivative of the aliphatic quaternary ammonium of the water solubilising atomic group of sulfate radical, sulfonate radical, carboxylate radical, phosphate radical or phosphonate radical, sulfonium and phosphonium compounds.The general formula of these compounds is:
R
1(R
2)
xY
+R
3Z
-
Wherein R
1containing having the alkyl of 8 to 18 carbon atoms, thiazolinyl or hydroxyalkyl group, 0 to 10 ethyleneoxy group group or 0 to 2 glycerol unit; Y is nitrogen, sulphur or phosphorus atom; R
2for having alkyl or the hydroxyalkyl group of 1 to 3 carbon atom; When Y is sulphur atom, x is 1, when Y be nitrogen or phosphorus atom time, x is 2; R
3for there is the alkyl of 1 to 5 carbon atom or hydroxyalkyl group and Z is the atomic group being selected from sulfate radical, sulfonate radical, carboxylate radical, phosphate radical or phosphonate radical.
Preferred amphoterics is amine oxide, such as coco dimethyl amine oxide.Preferred zwitterionics is trimethyl-glycine, especially amido betaines.Preferred trimethyl-glycine is C
8to C
18alkyl amido alkyl betaine, such as cocoamido trimethyl-glycine.These can be used as cosurfactant and introduce, and based on the weighing scale of total composition, preferably exist with the amount of 0 to 10 % by weight, more preferably 1 to 5 % by weight.
Be beet alkali surface activator for introduction into the preferred both sexes in composition according to the present invention or zwitterionics.The example of these tensio-active agents is mentioned in enumerating below.
Sulfatobetaine, as 3-(dodecyl dimethyl ammonium)-1-propane vitriol; With 2-(coco dimethyl ammonium)-1-ethanesulfonate.
Sultaine, as: 3-(dodecyl dimethyl ammonium)-2-hydroxyl-1-propane sulfonate; 3-(dodecyldimethylamine base ammonium)-1-propane sulfonate; 3-(C
12-C
14alkylamidopropyl group Dimethyl Ammonium)-2-hydroxyl-1-propane sulfonate; With 3-(coco dimethyl ammonium)-1-propane sulfonate.
Carboxybetaine, as (dodecyl dimethyl ammonium) acetate (also claiming lauryl betaine); (dodecyldimethylamine base ammonium) acetate (also claiming myristyl betaine); (coco dimethyl ammonium) acetate (also claiming coconut trimethyl-glycine); (oleyl dimethyl ammonium) acetate (also claiming oil-based betaine); (dodecyloxy methyl dimethoxy base ammonium) acetate; (cocoamidopropyl dimethyl ammonium) acetate (also claiming cocoamido-propyl trimethyl-glycine or CAPB).
Sulfonium trimethyl-glycine, as: (dodecyl dimethyl sulfonium) acetate; With 3-(coco dimethyl-sulfonium)-1-propane sulfonate.
Phosphonium trimethyl-glycine, as: 4-(San Jia Ji Phosphonium)-1-n-Hexadecane sulfonate; 3-(Shi bis-Wan base Er Jia Ji Phosphonium)-1-propane sulfonate; With 2-(Shi bis-Wan base Er Jia Ji Phosphonium)-1-ethanesulfonate.
Preferably comprise carboxybetaine or sultaine as both sexes or zwitterionics according to composition of the present invention, or comprise their mixture.Especially preferred is lauryl betaine.
Also optional composition comprises other tensio-active agent as non-ionic type and cationic surfactant, viscosity modifier, profoamer, sanitas (such as, sterilant), pH buffer reagent, polyelectrolyte, antishrinking agent, anti wrinkling agent, antioxidant, sun-screening agent, corrosion inhibitor, drape imparting agents, static inhibitor and ironing aids.Described composition can also contain toner, pearling agent and/or opalizer; With cover dyestuff, fluorescent agent.
Present combination non-limiting example below further describes the present invention.
Embodiment
All values in whole part is % by weight.
Without enzyme detergent formula A
Wherein:
Neodol 25-7 (from Shell)=C
12-C
15alcohol 7-ethoxylate
LAS acid=C
10-C
14alkyl benzene sulphonate (ABS);
SLES=C12-C13 alcohol 3-polyethoxylate sulfates, Na salt :=sodium lauryl tri(oxyethyl) sulfate (there are average 3 ethyleneoxy group groups);
Embodiment 1
In this embodiment, detergent formulation according to the present invention is tested to determine that namely its process removes the ability of tallow spot from cotton fabric.
End-point method detergency test
Reagent:
-CS46B (tallow, coloured) stained cloth (Testfabrics Inc.) to be punching into and to coil and transfer to 300I 96 orifice plate.
-composition A
-DL-arginine (number: 230-571-3) by Sigma catalog number 11020, EC
Program:
-the pre-rinsing of cloth (before being added to orifice plate) will be stained to remove the free spot of any remnants:
-in each hole, add 200l distilled water
-under 900rpm jolting plate 10 minutes
-remove water
Add following purging compound:
According to test mixture of the present invention:
Composition A 5mg/L 100l
Arginine diluent * 20l
Distilled water 60l
* in distilled water, the arginine of following mg/ml concentration is diluted to: 0.16,0.32,0.64,1.28,2.56,5.12 and 10.24.
Control mixture:
Composition A 5mg/L 100l
Distilled water 100l
-reactant is cultivated 1 hour while jolting under 900rpm under 22 degree.
-by adding 200l distilled water in each hole, then under 900rpm, jolting carrys out rinsing cloth in 5 minutes.Then liquid is removed.Repeat this program continuous four times.
-40 degree will be distributed under dry 3 hours
After-drying, digital scanning spot plate also measures its Δ E.This value is used to express cleaning effect and be defined as calico and the aberration stained between cloth after washing.Mathematically, Δ E is defined as:
ΔE=[(·L)
2+(·a)
2+(·b)
2]
1/2
Wherein L is measuring through darkness difference between washing cloth and calico; A and b is respectively measuring of redness and yellowing difference between two cloth.From this formula clearly, the value of Δ E is lower, and cloth will be whiter.About this colour examining technology, with reference to Commission International de I'Eclairage (CIE); Recommendation on Uniform Colour Spaces, colour difference equations, psychometric colour terms, supplement no.2to CIE Publication, no.15, Colormetry, Bureau Central de la CIE, Paris 1978.
Result
Cleaning effect is have expressed with the form of decontamination index (SRI) in following table:
SRI=100-ΔE
SRI is higher, then cloth is more clean, SRI=100 (white)." decontamination " is to alleviate unit or to alleviate Index measurement.For (passing through human eye) visible effect, effective decontamination preferably by be equal to or greater than 2 alleviate units and more preferably greater than or the alleviation that equals 5 units represent.
Table 1: use the end-point method detergency test through staining cloth with the CS46B of a series of arginine concentrations process in MTS24 formula.Same 96 orifice plates carry out four replicate(determination)s abreast.Scanning board also calculates SRI value.
The result of table 1 is shown in Figure 1, and this figure is graphic representation, shows the change of average SRI with arginine concentrations of four replicate(determination) 1-4 in table 1.Error bar shows the standard deviation between four replicate(determination)s of each concentration.
These results illustrate, arginine removes CS46B spot with dose dependent fashion.
Tergotometer tests
Tergotometer (SR Laboratory Instruments) allows the convergent-divergent of relatively large agitator type washing machine to reproduce.This device is used for assessing arginine stains cloth cleaning action to the different fatty group in composition A.
Stain cloth:
-CS46B (tallow, coloured) (Testfabrics Inc.)
-hamburger grease and purple dye (Warwick Equest)
-lard and purple dye (Warwick Equest)
-artificial sebum and carbon black dyestuff (inner preparation)
-composition A (+) tensio-active agent (-) enzyme
-DL-arginine (number: 230-571-3) by Sigma catalog number 11020, EC
Program:
The identical cloth that stains of two panels 10 × 10cm is added in each Tergotometer tank.Also the calico that do not stain of two panels 10 × 10cm is added in each Tergotometer tank to simulate typical wash load.Two kinds of diverse ways are adopted to use arginine: (i) passes through to be included in the formula containing purging compound or (ii) carried out pre-treatment with arginic solution to cloth before washing.
-containing arginic washing:
To stain in 1 liter of Tergotometer tank that cloth transfers to containing following content:
100mg/ml arginine (pH 8.0) 50ml (10mg/ml), 5ml (1mg/ml)
Composition A 0.57ml
France hard water (French Hardness) (50X) 10ml
Volume is supplied to 500ml with softening water.
Wash conditions: at 22 DEG C 1 hour
The pre-treatment of-arginine is washed:
Before transferring to the Tergotometer tank containing following content, within 5 minutes, carry out pre-treatment by immersion in the arginine/aqueous solution (pH 8.0) of 1mg/ml or 10mg/ml and stain cloth:
Composition A 0.57ml
France hard water (50X) 10ml
Volume is supplied to 500ml with softening water.
Wash conditions: at 22 DEG C 1 hour
-contrast washing:
To stain in 1 liter of Tergotometer tank that cloth transfers to containing following content:
Composition A 0.57ml
French Hardness(50X) 10ml
Volume is supplied to 500ml with softening water.
Wash conditions: at 22 DEG C 1 hour
After washing in softening water by cloth rinsing 5 × 2 minutes and air-dry overnight.
When fully dry, digital scanning carried out to cloth, measures its Δ E as previously mentioned respectively and calculate SRI.
Result
Cleaning effect is have expressed with the form of decontamination index (SRI) in following table:
SRI=100-ΔE
SRI is higher, then cloth is more clean, SRI=100 (white).
Table 2: use the Tergotometer test carried out through staining cloth with the CS46B of 1mg/ml and 10mg/ml arginine washing in MTS24 formula.Carry out 4 replicate(determination)s (2 replicate(determination)s of each Tergotometer tank) abreast.
The result of table 2 is shown in Figure 2, and this figure is bar graph, shows the change of average SRI with arginine concentrations of replicate(determination) 1-4 in table 2.Error bar shows the standard deviation between four replicate(determination)s of each concentration.
Table 3: use through with the pre-treatment of 1mg/ml and 10mg/ml arginine and then in MTS24 formula the CS46B of washing stain the Tergotometer test that cloth carries out.Carry out 4 replicate(determination)s (2 replicate(determination)s of each Tergotometer tank) abreast.
The result of table 3 is shown in Figure 3, and this figure is bar graph, shows the change of average SRI with arginine concentrations of replicate(determination) 1-4 in table 3.Error bar shows the standard deviation between four replicate(determination)s of each concentration.
Table 4: use through staining with the lard of 1mg/ml and 10mg/ml arginine washing in MTS24 formula and purple dye the Tergotometer test that cloth carries out.Carry out 4 replicate(determination)s (2 replicate(determination)s of each Tergotometer tank) abreast.
The result of table 4 is shown in Figure 4, and this figure is bar graph, shows average SRI from the replicate(determination) 1-4 of table 4 with the change of arginine concentrations.Error bar shows the standard deviation between four replicate(determination)s of each concentration.
Table 5: use through staining with the lard of the pre-treatment of 1mg/ml and 10mg/ml arginine and then washing in MTS24 formula and purple dye the Tergotometer test that cloth carries out.Carry out 4 replicate(determination)s (2 replicate(determination)s of each Tergotometer tank) abreast.
The result of table 5 is shown in Figure 5, and this figure is bar graph, shows the change of average SRI with arginine concentrations of replicate(determination) 1-4 in table 5.Error bar shows the standard deviation between four replicate(determination)s of each concentration.
Table 6: use through staining with hamburger grease of 1mg/ml and 10mg/ml arginine washing in MTS24 formula and purple dye the Tergotometer test that cloth carries out.Carry out 4 replicate(determination)s (2 replicate(determination)s of each Tergotometer tank) abreast.
The result of table 6 is shown in Figure 6, and this figure is bar graph, shows the change of average SRI with arginine concentrations of replicate(determination) 1-4 in table 6.Error bar shows the standard deviation between four replicate(determination)s of each concentration.
Table 7: use through staining with hamburger grease of the pre-treatment of 1mg/ml and 10mg/ml arginine and then washing in MTS24 formula and purple dye the Tergotometer test that cloth carries out.Carry out 4 replicate(determination)s (2 replicate(determination)s of each Tergotometer tank) abreast.
The result of table 7 is shown in Figure 7, and this figure is bar graph, shows the change of average SRI with arginine concentrations of replicate(determination) 1-4 in table 7.Error bar shows the standard deviation between four replicate(determination)s of each concentration.
Table 8: use the Tergo-O-tometer test carried out through staining cloth with the artificial sebum of 1mg/ml and 10mg/ml arginine washing in MTS24 formula.Carry out 4 replicate(determination)s (2 replicate(determination)s of each Tergo-O-tometer tank) abreast.
The result of table 8 is shown in Figure 8, and this figure is bar graph, shows the change of average SRI with arginine concentrations of replicate(determination) 1-4 in table 8.Error bar shows the standard deviation between four replicate(determination)s of each concentration.
Conclusion:
Arginic introducing improves removing of tested fatty group spot.To be in the composition A containing tensio-active agent to carry out pre-treatment with arginine also improve decontamination to staining cloth before washing.
Claims (10)
1. a fabric decontaminating composition, described fabric decontaminating composition comprises arginine compounds and tensio-active agent.
2. fabric decontaminating composition according to claim 1, wherein said tensio-active agent comprises aniorfic surfactant.
3. fabric decontaminating composition according to claim 2, wherein said tensio-active agent comprises rhamnolipid.
4., according to fabric decontaminating composition in any one of the preceding claims wherein, wherein said fabric decontaminating composition is environment activity.
5. a pretreatment unit, described device comprises the storage vault of the fabric decontaminating composition of (i) storage according to any one of claim 1-4 and (i) for the divider to fabric decontaminating composition described in the spot topical application on fabric.
6., from a method of staining fabric and remove spot, described method comprises the step using the fabric decontaminating composition according to any one of claim 1-4 to described spot.
7. method according to claim 6, described method comprises the step adding water to be formed water-washing liquid in described fabric decontaminating composition.
8. the method according to any one of claim 6 or 7, described method comprises to the fabric decontaminating composition of the spot topical application of staining on fabric according to any one of claim 10-4.
9. the method according to any one of claim 6-8, the wherein said step using described fabric decontaminating composition is the pre-treatment step using pretreatment unit according to claim 5 to carry out.
10. arginine compounds, preferably combines ground, for removing the purposes of oil/fatty spot with tensio-active agent.
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EP12198568 | 2012-12-20 | ||
EP12198568.3 | 2012-12-20 | ||
PCT/EP2013/076514 WO2014095617A1 (en) | 2012-12-20 | 2013-12-13 | Stain removal compositions |
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EP (1) | EP2935549B1 (en) |
CN (1) | CN104903433A (en) |
BR (1) | BR112015013067B1 (en) |
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CN108219677A (en) * | 2017-12-06 | 2018-06-29 | 王建东 | A kind of tableware dryer and preparation method thereof |
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DE102014221889B4 (en) * | 2014-10-28 | 2023-12-21 | Henkel Ag & Co. Kgaa | Detergents with mannosylerythritol lipid, enhancing the cleaning performance of detergents through mannosylerythritol lipid, and washing processes using mannosylerythritol lipid |
CA3009197A1 (en) | 2015-12-31 | 2017-07-06 | Colgate-Palmolive Company | Cleansing compositions |
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- 2013-12-13 WO PCT/EP2013/076514 patent/WO2014095617A1/en active Application Filing
- 2013-12-13 BR BR112015013067-4A patent/BR112015013067B1/en active IP Right Grant
- 2013-12-13 EP EP13803053.1A patent/EP2935549B1/en active Active
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EP2935549B1 (en) | 2018-09-26 |
WO2014095617A1 (en) | 2014-06-26 |
BR112015013067A2 (en) | 2017-07-11 |
BR112015013067A8 (en) | 2019-10-08 |
EP2935549A1 (en) | 2015-10-28 |
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