CN106459838A - Enzyme treatment composition - Google Patents

Enzyme treatment composition Download PDF

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Publication number
CN106459838A
CN106459838A CN201580033105.XA CN201580033105A CN106459838A CN 106459838 A CN106459838 A CN 106459838A CN 201580033105 A CN201580033105 A CN 201580033105A CN 106459838 A CN106459838 A CN 106459838A
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Prior art keywords
enzyme
composition
textile stains
spot
remove
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CN201580033105.XA
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Chinese (zh)
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R·A·冈加比松
J·T·佩特科夫
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Unilever PLC
Unilever NV
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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
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/86—Mixtures of anionic, cationic, and non-ionic compounds
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/26—Organic compounds containing nitrogen
    • C11D3/30—Amines; Substituted amines ; Quaternized amines
    • 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
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/04—Detergent materials or soaps characterised by their shape or physical properties combined with or containing other objects
    • C11D17/041—Compositions releasably affixed on a substrate or incorporated into a dispensing means
    • 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
    • C11D3/02—Inorganic compounds ; Elemental compounds
    • C11D3/04—Water-soluble compounds
    • C11D3/046—Salts
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2041—Dihydric alcohols
    • C11D3/2044—Dihydric alcohols linear
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2065—Polyhydric alcohols
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2075—Carboxylic acids-salts thereof
    • C11D3/2086—Hydroxy carboxylic acids-salts thereof
    • 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
    • C11D3/34—Organic compounds containing sulfur
    • C11D3/3427—Organic compounds containing sulfur containing thiol, mercapto or sulfide groups, e.g. thioethers or mercaptales
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38609—Protease or amylase in solid compositions only
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/12—Sulfonic acids or sulfuric acid esters; Salts thereof
    • C11D1/22—Sulfonic acids or sulfuric acid esters; Salts thereof derived from aromatic compounds
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/38—Cationic compounds
    • C11D1/40—Monoamines or polyamines; Salts thereof
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/66—Non-ionic compounds
    • C11D1/72—Ethers of polyoxyalkylene glycols
    • C11D2111/12—

Abstract

An enzymatic fabric treatment composition comprising the combination of: one or more enzymes; and one or more diamine compounds. A pretreatment device comprising said composition. A process for removing a stain from a stained fabric. The use of a diamine compound in the removal of a stain from a stained fabric.

Description

Enzyme-treated composition
The present invention relates in fabric spot enzyme process greasiness removal.Particularly but not exclusively, the present invention relates to passing through straight Connect the spot being applied on pollution fabric or the spot textile stains that pre-processed and removed spot on pollution fabric are gone Except composition.
Enzyme is used in washing composition of detergent to help cleaning and greasiness removal.
In many weathers and in developing country, laundry is carried out at low or ambient temperatures.These temperature for according to The laundry greasiness removal product relying the enzyme most preferably working between 50-70 degree is a challenge.For modern laundry machine, Greasiness removal depends on to a great extent and heats the water on environment temperature in washing machine, and this accounts for the related temperature of laundry For environment reason, these footprints need to reduce the significant proportion of room gas footprint.
The purpose of the present invention is to improve the low temperature/environment temperature enzyme greasiness removal of the spot on pollution fabric.
In the first aspect, the invention provides a kind of textile stains remove composition, described composition comprises with the following group The combination dividing：
(i) one or more enzyme；With
(ii) one or more diamine compound.
In second aspect, the invention provides the textile stains comprising the combination of following components remove composition：
(i) one or more enzyme；With
(ii) comprise the compound of following structure for one or more：
Wherein
X1 and X2 is hydrogen bond donor or acceptor groups, and it is independently selected from NH2, OH, SH and NH；With
R is independently selected from following connector：
a.–CH-
b.–CH-CH2-
c.–CH-CH2-CH2-
And n is the integer of wherein n=0 to 10.
Preferably, described spot comprises biological substance, is preferably deposited in the protein-based and/or starch kind material on fabric Matter.
Preferably, described composition is active at ambient conditions.
Preferably, described composition comprises one or more surfactant.
In second aspect, the invention provides a kind of from pollution fabric substrate remove spot method, methods described bag The step including the compositions-treated spot with present invention one side.
Preferably, this is environment coolant-temperature gage at ambient conditions and preferably for methods described generation.
Preferably, the method for second aspect include add or without water in the case of, to pollution fabric directly apply Step with described composition.The step of applying said compositions can using itself be main washed journey or its can be used as further Subsequently (" leading ") washes the pre- step (as pretreatment) of process steps.Such further subsequent wash step mainly includes appointing Any washing process in what hand washing process or fabric washing machine.
Correspondingly, at the 3rd aspect, the invention provides a kind of textile stains remove processing meanss, described device includes Store the storeroom of composition of present invention one side and for direct applying said compositions to suprabasil process structure Part, the method that described administration preferably employs second aspect.
In yet another aspect, the invention provides diamine compound enzyme process removes the purposes of textile stains.
In further aspect of the invention, there is provided the compound enzyme process comprising following structure removes the use of textile stains On the way：
Wherein X1 and X2 is hydrogen bond donor or acceptor groups, and it is independently selected from NH2, OH, SH and NH；And R is independently It is selected from (a). CH- (b). CH-CH2- (c). the connector of CH-CH2-CH2- and n are the integers of wherein n=0 to 10.
Using the present invention, the enzyme process removal of the spot being present on fabric is enhanced and is effective at a lower temperature 's.This provides laundry (that is, fabric) cleaning of the improvement for pollution fabric in the universal area of environment water washing.Relatively low At a temperature of improve scourability suppression can be helped in these countries to adopt hot wash；With growth in the living standard with more Many people can bear washing machine, and hot wash is the trend rising.The invention provides (using in environment temperature clean method Cold washing liquid) in dirt based on protein and/or starch and/or spot enzyme process performance, and exist without thinking better of enzyme Temperature sensitivity during storage.Enzyme therefore can be considered based on other and more freely be selected.
The removal for the spot having substrate therefore can significantly drop at ambient temperature of the composition for improved of the present invention The cost of energy of low each washing.
As used herein, term " substrate " includes fabric, clothing etc..
As used herein, term " diamine compound " is intended to including any suitable diamine compound, and it includes standing Body isomery and racemic form, derivative and substitutive derivative, its salt, and its any mixture.
Diamines preferably includes any one in following structure:
1,4 diaminobutane dihydrochlorides (Sigma, CAS 333-93-7)；1,3 diaminopropanes (Sigma, No. CAS 109-76-2), propane -1,2- diamines, propane -1,3- diamines, pentane -1,3- diamines, 2- ethylaminoethanol, 2- aminopropan-1-ols, 2- amino butyl- 1- alcohol, 2- amino amyl- 1- alcohol, 2- amino hex- 1- alcohol, 2- amino decyl- 1- alcohol, 2- amino 11-1- alcohol, 2- ammonia Base 12-1- alcohol, 3- aminopropan-1-ols, 2- aminoothyl mercaptan, 2- ethylaminoethanol, 1- amino propan-2-ol, 3- amino propyl- 1- Alcohol, 4- amino butyl- 2- alcohol, ethane -1,2- glycol, propane -1,2- glycol, butane -1,2- glycol, pentane -1,2- glycol, oneself Alkane -1,2- glycol, octane -1,2- glycol, decane -1,2- glycol, dodecane -1,2- glycol, propane -1,3- glycol, butane -1, 3- glycol, 2 mercapto ethanol, 1- sulfydryl propan-2-ol, 3- sulfydryl propyl- 1- alcohol, 2- aminoothyl mercaptan, 2 mercapto ethanol, 3- sulfydryl Propyl- 1- alcohol, ethane -1,2- two mercaptan, propane -1,3- two mercaptan, butane -1,3- two mercaptan.
Preferably, the compound of the present invention with 0.01mg/ml 10mg/ml in the range of, more preferably with 0.01 0.32mg/ml In the range of, the concentration in the range of more preferably 0.08-0.16mg/ml is present in any cleaning solution.
Preferably, diamines includes the diaminopropanes existing with scope 0.1-10mg/ml (cleaning solution) and enzyme is protease. Alternatively or additionally it is preferable that diamines includes the diaminobutane existing with scope 0.15-0.62 (cleaning solution) and enzyme is Protease.
Preferably, diamines includes the diaminobutane existing with scope 0.1-10mg/ml (cleaning solution) and enzyme is amylase. Alternatively or additionally it is preferable that diamines includes the diaminobutane existing with scope 0.15-0.62 (cleaning solution) and enzyme is Amylase.
Preferably, with the 5000mg/ agent of scope 40mg, the concentration of preferably 320mg 4000mg/ agent is present in this to compound In bright any combinations thing.Composition can be provided as unit dose form or apply, by consumer's use, the multi-agent freedom that agent device measures Liquid form (powder, liquid, gel, paste etc.).Dosage can be 10ml to 100ml.
For the pretreatment unit for local stain treatment/pretreatment, the concentration in composition can be higher and every dose Concentration can be higher than in main washing composition of detergent, therefore can be every in every dose of 300-5000mg, preferred 500mg to 2000mg In the range of agent.Pretreatment unit dosage level can change in 0.1-10ml.
Term " activity at ambient conditions " is intended to refer to less than 25 degrees Celsius, preferably shorter than 22 degrees Celsius or lower, more Preferably shorter than 15 degree or lower, but be always above 1 degree Celsius, and " active " refer to effective in terms of realizing greasiness removal.
As used herein, in the context of enzyme process fabric treatment composition, term " process " preferably refers to clean, more preferably Refer to greasiness removal.
Preferably, " greasiness removal " is to alleviate unit (Remission unit) or to alleviate index (Remission Index) measure.When existing equal to or more than 2 alleviation units, the more preferably equal to or greater than alleviations of 5 units, excellent Choosing illustrates " greasiness removal ".This represents effective greasiness removal of (human eye) visual effects.
As used herein, term " enzyme " includes enzyme variant (for example producing) by recombinant technique.The example of such enzyme variant In such as EP 251,446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525,610 (Solvay) and WO Disclosed in 94/02618 (Gist-Brocades NV).
Unless otherwise noted, all percentages otherwise referred to herein are calculated by weight all in accordance with total composition.Abbreviation " wt% " is interpreted as weight % of total composition.
Preferably, described pretreatment compositions are active at ambient conditions.Correspondingly, the cleaning solution step of water-washing process Rapid temperature is always below 40 DEG C therefore during washing (but not including drying), preferably shorter than 30 DEG C, more preferably less than 25 DEG C, More preferably less than 22 DEG C, even more preferably from 15 DEG C or lower.Cold washing liquid is encouraged to be environment and economical interest.
Correspondingly, described enzymatic treatment composition preferred packaging is described book, with low temperature for example with as herein described Method uses described compositions-treated substrate, and described low temperature is preferably shorter than 40 DEG C, is more preferably less than 30 DEG C, is even more preferably less than 25 DEG C, preferably at 22 DEG C or lower, most preferably at 15 DEG C.
For wherein needing enzyme process cleaning spot in environment temperature cleaning process (that is, use environment temperature washes liquid) but Wherein composition is inevitably stored in the particular condition under higher temperature, and the present invention is especially advantageous.Thermophilic cold enzyme is at low temperature Effectively, but sensitive to the temperature raising because of its adaptability.Mesophilic (and thermophilic) enzyme is stable at elevated temperatures, but in low temperature Hydraulic performance decline under wash conditions.The invention provides the low temperature enzyme process cleaning of the substrate using mesophilic enzyme.
Correspondingly, enzyme system preferably comprises mesophilic or thermophilic enzyme system.Enzyme system alternately comprises mesophilic and/or thermophilic And/or thermophilic cold enzyme system.
Enzyme may be from animal, plant, bacterial origin (from bacterium) or fungal source (from fungi), but is preferred from bacterium The enzyme in source.Including chemical modification or protein engineered mutant.The gene encoding this fermentoid can shift from a host To preferred Expression product host, the latter may or may not be identical with initial host.
Described one or more enzyme preferably comprises protease.
Preferably protease is serine protease or metalloproteinases, preferably alkaline microbial protease or trypsase Sample protease.
Commercially available protease includes AlcalaseTM、SavinaseTM、PrimaseTM、DuralaseTM、DyrazymTM、 EsperaseTM、EverlaseTM、PolarzymeTMAnd KannaseTM(Novozymes A/S)、MaxataseTM、MaxacalTM、 MaxapemTM、ProperaseTM、PurafectTM、Purafect OxPTM、FN2TMAnd FN3TM(Genencor International Inc.).
Described one or more enzyme preferably comprises amylase.
Suitable amylase (α and/or β) includes those of bacterium or fungal source.Including chemical modification or protein work The mutant of journey.Amylase includes for example deriving from bacillus such as GB 1,296,839 lichens gemma bar in greater detail The AMS of the Bacillus species strain disclosed in the special bacterial strain of bacterium or WO 95/026397 or WO 00/060060.
Commercially available amylase is DuramylTM、TermamylTM、Termamyl UltraTM、NatalaseTM、 StainzymeTM、FungamylTMAnd BANTM(Novozymes A/S)、RapidaseTMAnd PurastarTM(from Genencor International Inc.).Commercially available amylase includes StainzymeTMAnd ResilienceTM(Novozymes).
Described one or more enzyme can include the protease combining with amylase, and described diamine compound is not spread out Biochemical diamines.
Described enzyme is preferably existed with 0.001-5 weight %, more preferably 0.01-3%.
Described composition preferably comprises other enzyme.
Described composition preferably comprises lipase；Preferably lipase includes so-called " the first washing " lipase, its bag Containing amino acid sequence and the wild type lipase tool from Humicola lanuginosa (Humicola lanuginosa) strain DSM 4109 There is the polypeptide of at least 90% sequence iden, and compared with described wild type lipase, it comprises in the 15A of E1 or Q249 Electroneutral or electronegative amino acid are by the 49-Phe ,82-Ser,115-Arg,144-Met,145-Asn ,161-Arg,169-Met Human Connective tissue growth factor of positively charged；And can also comprise：
(I) peptide at C- end increases；
(II) peptide at N- end increases；
(III) limit below：
I. the position E210 in described wild type lipase comprises electronegative amino acid；
Ii. comprise electronegative amino acid in the region of the position 90-101 corresponding to described wild type lipase；With
Iii. electroneutral or electronegative amino acid are comprised at the position of the N94 corresponding to described wild type lipase； And/or
Iv. in the region of the position 90-101 corresponding to described wild type lipase, there is negative electrical charge or neutral charge； With
V. their mixture.
These lipase can be with LipexTMTrade mark derives from Novozymes.Novozymes is with title LipocleanTMPublic Open from Novozymes the similar enzyme it is believed that falling outside above-mentioned restriction, and this has been also preferred.
Other possible lipase include the lipase from humicola lanuginosa (Humicola, synonym Thermomyces), example As from other Humicola lanuginosa (H.lanuginosa or T.lanuginosus) bacterial strain or from Humicola insolens (H.insolens)；Pseudomonas Lipases, for example, be derived from Pseudomonas alcaligenes (P.alcaligenes) or false pain alkali vacation unit cell Bacterium (P.pseudoalcaligenes), Pseudomonas cepacia (P.cepacia), Pseudomonas stutzeri (P.stutzeri), fluorescence Pseudomonad (P.fluorescens), pseudomonad (Pseudomonas) plant bacterial strain SD 705 (WO 95/06720 and WO 96/ 27002)、P.wisconsinensis；Bacillus lipase, for example, be derived from bacillus subtilis (B.subtilis) (Dartois et al. (1993), Biochemica et Biophysica Acta, 1131,253-360), stearothermophilus gemma bar Bacterium (B.stearothermophilus) (JP 64/744992) or bacillus pumilus (B.pumilus) (WO 91/16422).
Commercially available lipase includes LipolaseTMWith Lipolase UltraTMAnd bacterial enzyme(it is derived from Genecor).This is the bacterial origin lipase of the mutation M21L of lipase of Pseudomonas alcaligenes, such as authorizes Gist- The WO of Brocades (M.M.M.J.Cox, H.B.M.Lenting, L.J.S.M.Mulleners and J.M.van der Laan) Described in 94/25578.
Described composition preferably comprises the phosphatidase classifying as EC 3.1.1.4 and/or EC 3.1.1.32.As this paper institute With term phosphatidase is the enzyme active to phosphatide.Phosphatide, such as lecithin or Phosphatidycholine, by outside (sn-1) and Middle (sn-2) position is esterified and is formed by the glycerine of Phosphation in the 3rd position by two aliphatic acid；Described phosphoric acid then may be used Esterified one-tenth amino alcohol.Phosphatidase is the enzyme of the hydrolysis participating in phosphatide.If the activity of phospholipase of dry type can be distinguished, including：Phosphorus Lipase A1 and A2, aliphatic acyl groups (respectively in sn-1 and sn-2 position) are hydrolyzed to form lysophosphatide by it；And haemolysis Phosphatidase (or phospholipase B), the remaining aliphatic acyl groups in its hydrolyzable lysophosphatide.Phospholipase C and phospholipase D (phosphoric acid Diesterase) discharge DG or phosphatidic acid respectively.
Described composition preferably comprises the cutinase ranging in EC 3.1.1.74.Cutinase used according to the invention Can have any source.Preferably, cutinase has microbe-derived, particularly bacterium, fungi or yeast sources.
Described composition preferably comprises cellulase, and described cellulase includes those of bacterium or originated from fungus.Including Chemical modification or protein engineered mutant.Suitable cellulase include from bacillus, pseudomonas, Humicola, Fusarium, Thielavia, the cellulase of Acremonium, such as US 4,435,307, US 5,648,263, Originating from disclosed in US 5,691,178, US 5,776,757, WO 89/09259, WO 96/029397 and WO 98/012307 Humicola insolens (Humicola insolens), autochthonal shuttle spore shell (Thielavia terrestris), thermophilic fungus destroyed wire (Myceliophthora thermophila) and the fungal cellulase of Fusarium oxysporum (Fusarium oxysporum).Can Commercially available cellulase includes CelluzymeTM、CarezymeTM、EndolaseTM、RenozymeTM(Novozymes A/S)、 ClazinaseTMWith Puradax HATM(Genencor International Inc.) and KAC-500 (B)TM(Kao Corporation).
Described composition preferably comprises peroxidase/oxidizing ferment, especially bacterial origin.Including chemical modification or Protein engineered mutant.The example of oxidizing bacteria is but not limited to the Aeromonas kind that oxidizing ferment may originate at (Aeromonas sp).
Described composition preferably comprises pectate lyase (also referred to as Polygalacturonate lyases), and pectate splits Solution enzyme include from different bacterium belong to as Erwinia, pseudomonas, klebsiella and xanthomonas and From bacillus subtilis (Nasser et al. (1993) FEBS Letts.335:319-326) with bacillus kind YA-14 (Kim etc. People (1994) Biosci.Biotech.Biochem.58:Pectate lyase 947-949) cloned.By bacillus pumilus (Bacillus pumilus) (Dave and Vaughn (1971) J.Bacteriol.108:166-174), bacillus polymyxa (B.polymyxa) (Nagel and Vaughn (1961) Arch.Biochem.Biophys.93:344-352), stearothermophilus gemma Bacillus (B.stearothermophilus) (Karbassi and Vaughn (1980) Can.J.Microbiol.26:377-384)、 Bacillus kind (Bacillus sp.) (Hasegawa and Nagel (1966) J.Food Sci.31:838-845) with gemma bar Bacterial classification RK9 (Bacillus sp.RK9) (Kelly and Fogarty (1978) Can.J.Microbiol.24:1164-1172) produce The purifying of the raw pectate lyase in the range of the pH of 8-10 with maximum activity has also been shown in description.Implementing the present invention When, can be split using any of above pectate lyase and bivalent cation dependent/non-dependent and/or heat endurance pectate Solution enzyme.In preferred embodiments, pectate lyase includes Heffron et al., (1995) Mol.Plant-Microbe Interact.8:331-334 and Henrissat et al., (1995) Plant Physiol.107:Pectin disclosed in 963-976 Hydrochlorate lyases.Specifically expected pectate lyase has disclosure in WO 99/27083 and WO 99/27084.Other tools (this document is to quote in U.S. Patent No. 6,284,524 for pectate lyase expected from body (from bacillus licheniformis) Mode is expressly incorporated herein) in have disclosure.Specifically expected pectate lyase mutation has disclosure in WO 02/006442, especially It is the mutation disclosed in the embodiment in WO 02/006442 (this document is herein incorporated by reference).Commercially available alkaline pectin The example of hydrochlorate lyases includes the BIOPREP from Denmark Novozymes A/STMAnd SCOURZYMETML.
Described composition preferably comprises mannase：The example of mannase (EC 3.2.1.78) include bacterium and The mannase of originated from fungus.In a specific embodiment, mannase belongs to aspergillus, preferably from filamentous fungi The bacterial strain (WO 94/25576) of aspergillus niger or microorganism Aspergillus aculeatus.WO 93/24622 discloses from trichoderma reesei (Trichoderma Reseei) detached mannase.Mannase also from some bacteria distribution, including bacillus organism.For example, Talbot et al., Appl.Environ.Microbiol., Vol.56, No.11, pp.3505-3510 (1990) describe one kind 'beta '-mannase from bacillus stearothermophilus.Mendoza et al., World J.Microbiol.Biotech., Vol.10, No.5, pp.551-555 (1994) describe the 'beta '-mannase from bacillus subtilis.JP-A- 03047076 discloses the 'beta '-mannase from bacillus kind.JP-A-63056289 describes alkaline, thermally-stabilised β-sweet The production of dew dextranase.JP-A-63036775 is related to micro-organisms bacillus FERM P-8856, and it produces 'beta '-mannase And beta-Mannosidase.JP-A-08051975 discloses the alkaline ' beta '-mannase from Alkaliphilic bacillus kind AM-001. There is disclosure from the purified mannanase of bacillus amyloliquefaciens in WO 97/11164.It is fine that WO 91/18974 describes half Dimension plain enzyme such as dextranase, zytase or Mannanase Activity thing.Be contemplated that disclosed in WO 99/64619 from glutinous Agar bacillus (Bacillus agaradhaerens), bacillus licheniformis (Bacillus licheniformis), resistance to Salt Alkaliphilic bacillus (Bacillus halodurans), Bacillus clausii (Bacillus clausii), bacillus The alkaline family 5 of kind (Bacillus sp.) and Humicola insolens (Humicola insolens) and 26 mannases.Especially It is contemplated that the bacillus kind mannase being related in the embodiment of WO 99/64619.
The example of commercially available mannase includes being available from the Mannaway of Denmark Novozymes A/STM.
The enzyme existing and any spices/aromatic substance or front aromatic substance may show certain interaction, therefore should select It is not negative for making this interaction.Some are negative, and interact can be by encapsulating a kind of or other enzymes and front in product Aromatic substance and/or avoided with other spacers.
Surfactant
Described composition preferably comprises surfactant.
Described surfactant can be synthetic surfactant or for example micro- from bacterium, fungi or other in microorganism mode Biosynthetic biosurfactant.Biosurfactant preferably comprises the biosurfactant from microorganism.Excellent Selection of land, it comprises Glycolipids Biosurfactantss, and described Glycolipids Biosurfactantss can be rhamnolipid or sophorolipid Or marine alga glycolipid or mannosylerythritol lipid (MEL).Or, biosurfactant can advantageously comprise cellobiose, base In the biosurfactant of peptide, lipoprotein and lipopeptid (for example, Surfactin), aliphatic acid (for example, corynomucolic Acid) (preferably there is hydrocarbon chain C12-C14), the phosphatide (phosphorus for example, being produced by the Rhodococcus erythropolis that are grown on n-alkane Acyl monoethanolamine, it leads to the interfacial tension between water and hexadecane to decrease below the 1mN m-1 and CMC of 30mg L-1) (Kretschner et al., 1982) and spiculisporic acid；Polymer-type biosurfactant, including Emulsan, Liposan, Mannoproteins and polysaccharide-protein compound.Preferably, biosurfactant comprises rhamnolipid.
Surfactant, preferred stain release surfactant are comprised according to the composition of detergent of the present invention.Live in decontamination surface Property agent refers at least one of this surfactant or any surfactant mixture surfactant to as laundry processes The textile fabric that a part is processed provides clean effect, i.e. cleaning effect.Can be or can not be detersive surfactant Other surfactants can serve as the part of described composition.
Detersive surfactant is with by weight 3 to 85 weight %, preferably 3 to 60 weight %, more preferably 3 to 40 weights Amount %, the level of most preferably 3 to 35 weight % are present in laundry detergent composition.Also can be to the laundry composition of the present invention Middle introducing other surfactants；These surfactants can be decontamination or non-detersive surfactant.
Preferably, detersive surfactant comprise anionic surfactant, nonionic surface active agent or the two Mixture.It is highly preferred that detersive surfactant mixture comprises anionic and nonionic surface active agent.Cation The part presence optionally as detersive surfactant for the type surfactant.
If it does, the gross weight based on the surfactant existing is by weight, anionic surfactant is with 0.1 Level to 95 weight %, preferably 1 to 50 weight %, more preferably 1.5 to 25 weight % exists.Based on the surfactant existing Gross weight by weight, if it does, nonionic surface active agent with 0.1 to 95 weight %, preferably 1 to 50 weight %, The level of more preferably 1.5 to 25 weight % introduces.If using comprising both anionic and nonionic surface active agent Detersive surfactant mixture, then preferred anionic type surfactant and the ratio of nonionic surface active agent are 10:1 To 1:10.
Nonionic surface active agent
For purposes of the present invention, unless otherwise noted, otherwise " nonionic surface active agent " should be defined as molecular weight Less than about 10,000 amphiphile, amphiphilic molecule, it is substantially free of any sense showing net charge under the Normal Wash pH of 6-11 Group.
Any kind of nonionic surface active agent can be used.It is highly preferred that having C8-C35, preferred C8-C30, more Preferably C10-C24, especially C10-C18The alkyl chain of carbon atom simultaneously has preferably 3 to 25, more preferably 5 to 15 ethylene oxide groups Fatty acid alkoxylates, especially ethoxylate, for example be derived from Shell (Hague, Detch) Neodols；Can have 1, The ethylene oxide/propylene oxide block polymer of 000 to 30,000 molecular weight, for example, be derived from BASF (Ludwigshafen, Germany) Pluronic (trade mark)；And alkylphenol ethoxylate, for example it is available from Dow Chemical (Michigan, USA Mead Blue) Triton X-100.
The other nonionic surface active agent considering within the scope of the invention include：Alkanolamine and the condensation of aliphatic acid Thing, such as coconut oleoyl amine DEA；Polyalcohol-fatty acid ester, is such as available from the Span series of Uniqema (Dutch person of outstanding talent reaches)；Ethoxylation Polyalcohol-fatty acid ester, is such as available from the Tween series of Uniqema (Dutch person of outstanding talent reaches)；APG, is such as available from The APG series of Cognis (Dusseldorf ,Germany)；With n- alkyl pyrrolidone, such as sold by ISP (New Jersey Wei grace) The Surfadone series of products sold.
Anionic surfactant
" anionic surfactant " is defined herein as being included under the Normal Wash pH being between 6 and 11 The amphiphile, amphiphilic molecule of one or more functional groups of net anionic charge is shown when in the aqueous solution.
Preferably anionic surfactant is the alkyl base having in its molecular structure containing about 6 to 24 carbon atoms Group and the alkali metal salt selected from sulfonate ester group and the organic sulfur product of group of sulfate group.
Although any anionic surfactant being hereinafter described for example alkyl ether sulfate, soap, fatty acid ester sulfonate, Alkylbenzenesulfonate, sulfosuccinate, primary alkyl sulphates, alkene sulfonate, paraffin sulfonate and organic phosphate Use, but preferred anionic surfactant be the alkali and alkaline earth metal ions salt of fatty acid carboxylate, aliphatic alcohol sulfate, Preferably primary alkyl sulphates, it is highly preferred that they are the alkyl ether sulfates as ethoxylation；With alkylbenzenesulfonate or they Mixture.
Cationic, amphoteric surfactant and/or zwitterionic surfactant
In addition, according to there may be cationic, amphoteric surfactant and/or amphion table in the composition of the present invention Face activating agent.
Preferably cationic surface active agent is to have general formula R1R2R3R4N+X-Quaternary ammonium salt, such as wherein R1For C12- C14Alkyl group, R2And R3For methyl group, R4For 2- hydroxyethyl groups, X-For chlorion.This material can be with Praepagen (business Mark) HY is commercially available in the form of the 40 weight % aqueous solution from Clariant GmbH.
In a preferred embodiment, both sexes or amphion surface are comprised according to the composition of detergent of the present invention Activating agent.Amphoteric surfactant is not only to have contained acidic-group but also containing basic group and by under the Normal Wash pH between 6 and 11 The molecule being existed with amphion.Preferably, both sexes or zwitterionic surfactant are with 0.1 to 20 weight %, more preferably 0.25 to 15 weight %, the level of even more preferably 0.5 to 10 weight % exist.
The example of suitable zwitterionic surfactant is can be broadly described as having having about 8 to about 18 carbon former One long chain alkyl group of son is selected from sulfate radical, sulfonate radical, the water solubilizing group of carboxylate radical, phosphate radical or phosphonate radical with least one The derivative of aliphatic quaternary ammonium, sulfonium and compound those.The formula of these compounds is：
R1(R2)xY+R3Z-
Wherein R1Containing alkyl, thiazolinyl or hydroxyalkyl group, 0 to 10 ethylidene-epoxide with 8 to 18 carbon atoms Group or 0 to 2 glycerol unit；Y is nitrogen, sulphur or phosphorus atoms；R2For having alkyl or the hydroxyalkyl group of 1 to 3 carbon atom；When When Y is sulphur atom, x is 1, and when Y is for nitrogen or phosphorus atoms, x is 2；R3For having alkyl or the hydroxyalkyl base of 1 to 5 carbon atom Group and Z is group selected from sulfate radical, sulfonate radical, carboxylate radical, phosphate radical or phosphonate radical.
Preferably amphoteric surfactant is amine oxide, such as coco dimethyl amine oxide.Preferably amphion table Face activating agent is glycine betaine, especially amido betaines.Preferably glycine betaine is C8To C18Alkyl amido alkyl betaine, Such as cocoamido glycine betaine.These can introduce as cosurfactant, based on the weight meter of total composition, preferably with 0 Amount to 10 weight %, more preferably 1 to 5 weight % exists.
For being incorporated into according to the preferred both sexes in the composition of detergent of the present invention or zwitterionic surfactant For beet alkali surface activator.The example of these surfactants will be mentioned in being exemplified below.
Sulfatobetaine, such as 3- (dodecyl dimethyl ammonium) -1- propane sulfate；With 2- (coco dimethyl ammonium)- 1- ethanesulfonate.
Sulfobetaines, such as：3- (dodecyl dimethyl ammonium) -2- hydroxyl -1- propane sulfonate；3- (myristyl two Ammonium methyl) -1- propane sulfonate；3-(C12-C14Alkylamidopropyl group Dimethyl Ammonium) -2- hydroxyl -1- propane sulfonate；With 3- (coco dimethyl ammonium) -1- propane sulfonate.
Carboxybetaine, such as (dodecyl dimethyl ammonium) acetate (also referred to as lauryl betaine)；(dodecyldimethylamine Base ammonium) acetate (also referred to as myristyl betaine)；(coco dimethyl ammonium) acetate (also referred to as coconut glycine betaine)；(oil base two Ammonium methyl) acetate (also referred to as oil-based betaine)；(dodecyloxy methyl dimethoxy base ammonium) acetate；(cocoamido third Base Dimethyl Ammonium) acetate (also referred to as cocoamido-propyl glycine betaine or CAPB).
Sulfonium glycine betaine, such as：(dodecyl dimethyl sulfonium) acetate；With 3- (coco dimethyl-sulfonium) -1- propane sulfonic acid Salt.
Glycine betaine, such as：4- (trimethyl) -1- hexadecane sulfonate；3- (dodecyl dimethyl) -1- propane sulphur Hydrochlorate；With 2- (dodecyl dimethyl) -1- ethanesulfonate.
According to the composition of the present invention be preferably contain as both sexes or zwitterionic surfactant carboxybetaine or Sulfobetaines, or its mixture.Especially preferably lauryl betaine.
Described treatment compositions can comprise common other compositions in detergent liquid.Especially polyester compatibility (substantive) soil release polymer, hydrotrote, opacifier, colouring agent, spices, other enzyme, other surfactant, one-tenth Divide the microcapsules as spices or nursing additive, softening agent, the polymer for anti-redeposition of soil, bleaching agent, bleach activating Agent and bleaching catalyst, antioxidant, pH controlling agent and buffer, thickener, have for rheology modified, visual cues or There is no the external structure agent embedding functional component therein and other composition well known by persons skilled in the art.
Further describe the present invention now with reference to following non-limiting example
Embodiment
In these embodiments, test the process combined to determine them of diamines and enzyme in laundry detergent composition Ability, processes the ability of the spot on bafta in every way.All values are all weight % from start to finish.
Fig. 1-2 shows the result of the ability of diamine compound fat various with enzyme combined treatment spot after tested, such as Under：
Fig. 1：The bafta being polluted with milk, ink and blood (EMPA-117) is at room temperature under certain limit concentration (a) 1,4 diaminobutane dihydrochloride and (b) 1.3 diaminopropanes and protease Savinase 16L and laundry detergent group Wash 1 hour in compound." 0 " value be shown in Savinase 16L and there is no diamines laundry detergent composition in wash.
Fig. 2：The bafta being polluted with coloured potato starch (CS-27) (a) 1,4 under certain limit concentration at room temperature In diaminobutane dihydrochloride and (b) 1,3 diaminopropanes and amylase Stainzyme 12L and laundry detergent composition Washing 1 hour." 0 " value be shown in Stainzyme 12L and there is no diamines laundry detergent composition in wash.
Terminal greasiness removal is tested
Reagent：
● pollution fabric samples are perforated into disk and transfer to 300 μ l 96 orifice plate below：
● proteinaceous stains:Milk, ink, blood (EMPA-117) (Testfabrics Inc)
● starch dirt:Coloured potato starch (CS-27) (Centre from Testmaterials BV)
● fatty dirt:The used frying fat (CS-46) of purple dye, coloured beef fat (CS-61), fat and Blood (CS-75)
● laundry detergent composition：Working concentration liquid storage dilution=1:428 (that is, following liquid storage dilutes in cleaning solution 1:428 times).
Laundry detergent composition
*C12-C15Alkoxylate (9EO) chain group
● enzyme：
● protease:Savinase 16L, 2.5mg/L working concentration (Novozymes)
● amylase:Stainzyme 12L, 4.25mg/L working concentration (Novozymes)
● diamines:
● 1,4 diaminobutane dihydrochlorides (Sigma, CAS 333-93-7)
● 1,3 diaminopropanes (Sigma, CAS 109-76-2)
Program：
Pollute pre-washing of fabric
Pollution piece of cloth disk is pre-washed as follows to remove any residual free spot：
● the distilled water of 200 μ l is added in each hole
● with 250rpm stir plate 2 minutes on plate vibrator
● remove water
Using diamines, main washing is carried out to pollution fabric
Following test and control mixture are added in hole：
● test mixing thing
● control mixture (does not have the negative control of diamines)
● composition of detergent 100ul
● distilled water 100ul
● enzyme 20ul
Pollution fabric is washed 1 hour with 250rpm at room temperature.After washing, then remove cleaning solution, fabric is steamed with 200ul Distilled water washs 4X5 minute with 250rpm on plate vibrator.Then fabric is placed at room temperature with dried overnight, carries out afterwards Scanning.
(3) visual inspection of scrubbed fabric
After drying, pollution fabric 96 orifice plate visual inspection is simultaneously taken pictures.
The whiteness of cloth represents the validity of stain treating composition.
Result shows in fig 1 and 2.
Conclusion
Diamines 1,4 diaminobutane dihydrochloride and 1,3 diaminopropanes and enzyme Savinase and The group of Stainzyme is fated and improves cleaning to fat contamination fabric when being directly included in main washing.Cleaning changes It is usually dose-dependent for entering, but specifically：
● for the combining of protease Savinase, diaminopropanes shows than diaminobutane under all concentration (Fig. 1)；
● diaminobutane when combining with protease Savinase, in 0.15-0.62mg/ml (cleaning solution) concentration range Inside put up the best performance (Fig. 1)；
● combine for diastatic, diaminobutane performs better than (Fig. 2) in whole concentration range；
● the diaminopropanes being combined with amylase is put up the best performance under 0.15-0.62mg/ml (cleaning solution) concentration and (is schemed 2).
Pre-process pollution fabric for test with diamines, the following citing of appropriate method then carrying out main washing provides：
Following test and control mixture are added to orifice plate (as stated above)：
● test mixing thing:
● laundry detergent composition 100ul
● distilled water 80ul
● diamines dilution * 20ul
* diamines is diluted to ultimate density is 5mg/ml
● control mixture (laundry detergent composition, only negative control)
● laundry detergent composition 100ul
● distilled water 100ul
Pollution fabric is cultivated 5 minutes, at room temperature without stirring in preprocessing solution.Then remove pretreatment washing Liquid.
After pretreatment, pollution fabric washs (250rpm, 1 hour, room temperature) in following mixture
● laundry detergent compositions 100ul
● distilled water 100ul
After washing, then remove cleaning solution, fabric washs 4X5 with 250rpm with 200ul distilled water on plate vibrator Minute.Then fabric is placed at room temperature with dried overnight, carries out visual inspection afterwards, takes pictures or scan.

Claims (18)

1. the textile stains comprising the combination of following components remove composition：
(i) one or more enzyme；With
(ii) one or more diamine compound.
2. the textile stains comprising following structure remove composition
Wherein
X1 and X2 is hydrogen bond donor or acceptor groups, and it is independently selected from NH2, OH, SH and NH；With
R is independently selected from following connector：
a.–CH-
b.–CH-CH2-
c.–CH-CH2-CH2-
And n is the integer of wherein n=0 to 10.
3. the textile stains according to any one of claim 1-2 remove composition it is characterised in that it is in environmental condition Lower activity.
4. the textile stains according to any one of claim 1-3 remove composition it is characterised in that it comprises one kind or many Plant surfactant.
5. textile stains according to any one of claim 1-4 remove composition it is characterised in that described one or more Enzyme includes protease.
6. textile stains according to any one of claim 1-5 remove composition it is characterised in that described one or more Enzyme includes amylase.
7. the textile stains according to any aforementioned claim remove composition it is characterised in that described diamines includes diamino Base propane.
8. the textile stains according to any aforementioned claim remove composition it is characterised in that described diamines includes diamino Base butane.
9. textile stains according to claim 7 remove composition it is characterised in that described diamines includes diaminopropanes And described one or more enzyme includes protease.
10. textile stains according to claim 8 remove composition it is characterised in that described diamines includes diaminobutane And described one or more enzyme includes amylase.
A kind of 11. pretreatment units, it includes (i) and stores the textile stains removal combination any one of claim 1-8 The storeroom of thing and (i) are used for the distributor that textile stains described in local application remove the spot to fabric for the composition.
12. are used for the methods removing spot from pollution fabric, and it is included with the composition any one of claim 1-8 The step managing described spot.
13. methods according to claim 10 are it is characterised in that method occurs to make any cleaning solution at ambient conditions It is in environment temperature.
14. methods according to claim 10 or 11 are it is characterised in that described composition is applied directly to described spot, institute Stating step is optionally pre-treatment step.
15. methods according to any one of claim 10-12, wherein said compound is deposited with the scope of 0.01 10mg/ml It is in cleaning solution.
16. methods according to any one of claim 10-13, wherein apply the step that described textile stains remove composition Suddenly it is the pre-treatment step of the pretreatment unit that usage right requires described in 9.
17. diamine compounds combine one or more enzyme from the purposes polluting fabric removal spot, and described one or more enzyme is excellent Choosing is protease and/or amylase.
18. compound groups comprising following structure close one or more enzyme from the purposes polluting fabric removal spot：
Wherein X1 and X2 is hydrogen bond donor or acceptor groups, and it is independently selected from NH2, OH, SH and NH；And R is connector, it is only On the spot it is selected from
a.–CH-
b.–CH-CH2-
c.–CH-CH2-CH2-
And n is the integer of wherein n=0 to 10
Described one or more enzyme is preferably protease and/or amylase.
CN201580033105.XA 2014-06-19 2015-06-12 Enzyme treatment composition Pending CN106459838A (en)

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Citations (5)

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Publication number Priority date Publication date Assignee Title
WO1999063034A1 (en) * 1998-06-02 1999-12-09 The Procter & Gamble Company Dishwashing detergent compositions containing organic diamines
CN1247560A (en) * 1996-12-20 2000-03-15 普罗格特-甘布尔公司 Dishwashing detergent compsns. containing organic diamines
WO2001025379A1 (en) * 1999-10-04 2001-04-12 The Procter & Gamble Company Fluid cleaning compositions having high levels of amine oxide
US20030028974A1 (en) * 2001-03-19 2003-02-13 Moe Kevin David Stain removal methods and products associated therewith
US6740627B1 (en) * 1999-02-08 2004-05-25 The Procter & Gamble Company Diols and polymeric glycols in dishwashing detergent compositions

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6069122A (en) * 1997-06-16 2000-05-30 The Procter & Gamble Company Dishwashing detergent compositions containing organic diamines for improved grease cleaning, sudsing, low temperature stability and dissolution
AR017744A1 (en) * 1999-02-08 2001-09-12 Procter & Gamble POLYMERIC GLYCOLS AND DIOLES FOR IMPROVED DETERGENT COMPOSITIONS FOR THE WASHING OF VAJILLA

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Publication number Priority date Publication date Assignee Title
CN1247560A (en) * 1996-12-20 2000-03-15 普罗格特-甘布尔公司 Dishwashing detergent compsns. containing organic diamines
WO1999063034A1 (en) * 1998-06-02 1999-12-09 The Procter & Gamble Company Dishwashing detergent compositions containing organic diamines
US6740627B1 (en) * 1999-02-08 2004-05-25 The Procter & Gamble Company Diols and polymeric glycols in dishwashing detergent compositions
WO2001025379A1 (en) * 1999-10-04 2001-04-12 The Procter & Gamble Company Fluid cleaning compositions having high levels of amine oxide
US20030028974A1 (en) * 2001-03-19 2003-02-13 Moe Kevin David Stain removal methods and products associated therewith

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