JP2000017287A - Detergent composition for clothes - Google Patents

Abstract

PROBLEM TO BE SOLVED: To obtain a detergent compsn. for clothes which is excellent in detergency by compounding a surfactant, a proteolytic enzyme, and a specified amt. of an org. compd. which cuts disulfide bonds. SOLUTION: An org. compd. which cuts disulfide bonds is compounded. As the surfactant, anionic, nonionic, cationic, and ampholytic surfactants can be used, a nonionic surfactant being pref. As the proteolytic enzyme, one having serine at its active center is pref. An org. reducing agent is used as the org. compd. which cuts disulfide bonds of protein, thio compds. being pref. and mercapto compds. being still pref. Among mercapto compds., dithiothreitol, thioglycerin, and cysteine are esp. pref. A suitable amt. of the proteolytic enzyme compounded is 0.01-10 wt.%. An enzyme stabilizer may also be compounded.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

TECHNICAL FIELD The present invention relates to a detergent composition for clothing containing a protease.

[0002]

2. Description of the Related Art In the field of detergents for clothing, it is common practice to mix enzymes such as proteases to improve the detergency. Various techniques have been proposed for further improvement. For example, a protease that satisfies conditions such as being not deactivated in a detergent or a cleaning solution and exhibiting detergency even at a low temperature has been searched for in nature (book "Industrial Enzymes", written by Takayuki Uejima, Maruzen Co., Ltd. Published, 1995
Year). Also, the formulation of detergent components that are less likely to inactivate proteases has been discussed (26th Wash Symposium Abstracts, p. 83). Furthermore, it has been reported that a reducing agent is blended in order to prevent the inactivation of the protease by available chlorine contained in tap water (Japanese Patent Publication No. 47-202).
No. 35).

On the other hand, it is known that an inactive protein such as keratin can be solubilized by cleaving a disulfide bond of a protein with a reducing agent such as sodium sulfite, sodium thiosulfate, or 2-mercaptoethanol (Yamauchi). Kiyoshi, Magazine "Polymer Processing", 4
3, p14, 1994). In addition, it has been reported that a reducing agent is blended with a detergent to solubilize protein stains and increase the detergency of protease (EP233721). However, in this publication, the amount of the reducing agent is 10 to 40%.
And the like, the level of the compounding amount is different from the present invention, and the technical concept is different from the present invention. In the present invention, 2
If it exceeds 0%, the stability of the preparation deteriorates, especially the liquid (stability) when used as a liquid detergent.

[0004]

SUMMARY OF THE INVENTION The present invention provides a detergent composition for clothing having excellent detergency. The present invention also provides a detergent composition for clothing having excellent storage stability, especially a liquid detergent composition for clothing.

[0005]

The detergent composition for clothing of the present invention comprises the following components (a), (b) and (c). (A) a surfactant; (B) Proteolytic enzymes. (C) an organic compound that cleaves a disulfide bond: 0.0
1-20% by weight.

[0006]

DETAILED DESCRIPTION OF THE INVENTION As the surfactant of the component (a), an anionic, nonionic or cationic amphoteric surfactant is used, and a nonionic surfactant is preferably used.
Specifically, the following surfactants are exemplified. (1) Nonionic surfactant An EO obtained by adding an average of 4 to 25 mol of ethylene oxide (EO) to a primary or secondary alcohol having 8 to 18 carbon atoms.
An addition type nonionic surfactant (alkyl ether ethoxylate). An average of 4 to 25 moles of ethylene oxide (EO) in a primary or secondary alcohol having 8 to 18 carbon atoms,
An EO-PO addition type nonionic surfactant to which propylene oxide (PO) is added in an average of 3 to 15 mol.

An alkyl glucoside represented by the following chemical formula 1

## STR1 ## RO (R'O) y (Z) x (z: a residue derived from a reducing sugar having 5 to 6 carbon atoms R: an alkyl group, an alkenyl group, an alkylphenyl group,
A hydroxyalkyl group, a hydroxyalkylphenyl group or a mixture thereof, wherein the alkyl group or the alkenyl group has 8 to 20 carbon atoms R ': an alkylene group having 2 to 4 carbon atoms y: 0 to 30 x: 1.0 -1.42 sugar residues include monosaccharides such as glucose, galactose, xylose, mannose, lyxose, and arabinose;
Examples include polysaccharides such as artose, xylopiose, lactose, and sucrose.

A sugar fatty acid ester-based surfactant represented by the following formula (2)

Embedded image (R ₁ : a linear or branched alkyl or alkenyl group having 5 to 17 carbon atoms R ₂ : a hydrogen atom or an alkyl group having 1 to 4 carbon atoms)

An ester type nonionic surfactant represented by the following formula (3)

Embedded image (R₁CO: 6 to 22 carbon atoms, preferably 10 to 10 carbon atoms
18 saturated or unsaturated fatty acid residues, straight chain
Or a branch. R_Two: Having 2 to 4 carbon atoms, ethylene oxide alone
Or with ethylene oxide and propylene oxide
Are mixed and added to OR_TwoIt is preferable to configure R_Three: An alkyl group having 1 to 4 carbon atoms, preferably 1 carbon atom
To 2 alkyl groups n: OR_TwoAnd the number of added moles of 5 to 30
(Preferably n = 5 to 20)

The ester surfactant of the above formula (4) is structurally an alkyl ether of an alkylene oxide adduct of a fatty acid, and is prepared by adding an alkylene oxide to an alcohol by a conventional method, followed by esterification with a fatty acid.
The trivalent aluminum (A
l) ion, gallium (Ga) ion, indium (I
n) ion, thallium (Tl) ion, cobalt (C
o) fatty acid alkyl ester in the presence of a catalyst comprising magnesium oxide to which at least one metal ion selected from ions, scandium (Sc) ion, lanthanum (La) ion and divalent manganese (Mn) ion is added. Those produced by a one-step method of reacting R ₁ COOR ₃ with an alkylene oxide are preferred. (JP-A-4-
279552). These nonionic surfactants may be used alone or may be mixed at an appropriate ratio.

The following are examples of the anionic surfactant. 1) α-Sulfo fatty acid salt. It is shown in the following chemical formula 4.

Embedded image (R: alkyl group or alkenyl group having 8 to 20 carbon atoms Y: alkyl group having 1 to 3 carbon atoms or counter ion Z: counter ion)

2) Alkyl ether sulfates having a linear or branched alkyl or alkenyl group having an average of 10 to 20 carbon atoms and having an average of 0.5 to 8 mol of ethylene oxide added thereto. 3) A linear alkylbenzene sulfonate having an alkyl group having an average of 8 to 16 carbon atoms.

4) α-olefin sulfonate having an average of 10 to 20 carbon atoms. 5) Alkyl sulfates having an average of 10 to 20 carbon atoms. 6) A saturated or unsaturated fatty acid salt having an average of 10 to 22 carbon atoms. A substituted or unsubstituted ammonium salt or amine salt, wherein the fatty acid residue has 8 to 22 carbon atoms,
~ 20 are preferred. This fatty acid salt directly saponifies natural animal fats and vegetable fats such as beef tallow, palm oil, coconut oil, palm kernel oil and the like, or neutralizes fatty acids or synthetic fatty acids derived from them. Therefore, it is manufactured.

Examples of the salt in the anionic surfactant include alkali metal salts such as sodium and potassium, ammonium salts, substituted ammonium salts such as methylammonium, dielammonium and trimethylammonium, and monoethanolamine salts. Particularly preferred are alkali metal salts such as sodium salt and potassium salt, and alkanolamine salts. An amphoteric surfactant and a cationic surfactant can also be blended.

As the organic compound capable of cleaving the disulfide bond of the protein (c), an organic reducing agent is used, preferably a thio compound, and more preferably a mercapto compound. Specific examples of these include:
Geothiothreitol @ HSCH ₂ (CHOH) ₂ C
H ₂ }, thioglycerin {C ₃ H ₃ O ₂ S}, thiourea {CH ₄ N ₂ S}, cysteine {HSCH ₂ CH (NH ₂ )
COOH}, cystine _{{C 6 H 12 N 2 O} 4 S 2}, mercaptoethanol, thioglycolic acid salts, thioglycolic amide, glutathione, thioglycolic hydrazide, etc. mercaptoethylamine are the recited mercapto compounds are particularly preferred.

Specific examples of the mercapto compound include dithiothreitol, thioglycerin, cysteine, mercaptoethanol, thioglycolic acid, thioglycolamide, glutathione, thioglycolhydrazide, mercaptoethylamine and the like. Among them, dithiothreitol, thioglycerin and cysteine are preferred. The compounding amount of the component (c) is 0.01% to 20%, preferably 0.01% to 10%, and particularly preferably 0.1% to 8%. If the amount is too small, the effect of addition cannot be obtained,
On the other hand, if the amount is too large, the stability of the preparation deteriorates. In the present invention, the effect cannot be obtained with the following inorganic reducing agents having no carbon atom. Na sulfite (Na ₂ SO ₃ ),
Na thiosulfate (Na ₂ S ₂ O ₃ ), hydroylfight (Na ₂ S ₂ O ₄ ), and sodium bisulfite (NaHSO ₃ ).

The protease of component (b) is not particularly limited, but is preferably a protease having serine at the active center. As a specific example, “Savinase L16 EX” from Novo Nordisk Bioindustry
(Savinase), “Alcalase” (Alcal
case), "esperase",
"Durazyme", "Everase" (Everase), "Kannase" (Kann)
Nase) Genencor's “Maxacal” (Maxa
cal), "Maxapem" (Maxapem), "Purafect", "Opticlean" (Opticlean). Further, an alkaline protease produced from Bacillus sp. Strain Y (Microtechnical Laboratories No. 8088) and the like are exemplified. The amount of the protease used as the component (b) is preferably from 0.01% to 10%, more preferably from 0.0% to 10%.
It is 5 to 10%, more preferably 0.1 to 10%.

Further, an enzyme stabilizer may be added. Specific examples thereof include a boron compound, formic acid, a polyol, a calcium salt, glycerin and the like, and the compounding amount is preferably 1.0 to 10%. In addition, a protein denaturing agent can be blended, and examples thereof include urea and guanidine hydrochloride. The blending amount is preferably 0.1 to 30% by weight.

Organic chelating agents: calcium ion trapping builders such as sodium citrate, sodium ethylenediaminetetraacetate, nitrilotriacetate, sodium polyacrylate, sodium acrylate-sodium maleate anhydride copolymer, polyacetal carboxylate, etc. Chelating agent: Further, in the present invention, a chelating agent, an alkali agent and other additives are exemplified.

A crystalline or amorphous aluminosilicate represented by the following formula 5, or a mixture thereof is preferred.

## STR5 ## x (M ₂ O or M′O) .Al ₂ O ₃ .y (S
iO ₂ ) .z (H ₂ O) (wherein M is an alkali metal atom, M ′ is an alkaline earth metal atom exchangeable with calcium, and x, y and z are arbitrary numbers.) Aluminosilicate Is preferably 5 μm or less, more preferably 1 μm or less from the viewpoint of detergency. Sodium tripolyphosphate and sodium pyrophosphate

Alkaline agent Alkanolamine such as sodium carbonate, potassium carbonate, sodium silicate, crystalline silicate, monoethanolamine, diethanolamine and triethanolamine.
Examples include hydroxides of alkali metals such as sodium hydroxide and potassium hydroxide.

Other additives: Anti-redeposition agents such as carboxymethylcellulose and polyethylene glycol; and viscosity modifiers such as paratoluenesulfonate, toluenesulfonate, xylenesulfonate, lower alcohols, polyhydric alcohols, and urea. Softening agents such as quaternary ammonium salts and bentonite. Sodium sulfate, optical brightener, fragrance, coloring matter, white carbon, etc.
As enzymes other than the present invention, hydrolases, oxidases,
Reductase, transferase, lyase, isomerase, ligase, synthetase and the like can be added. More preferably, keratinase, lipase, esterase, cellulase, amylase, pullulanase, pectinase, cutinase, glucosidase, glucanase, cholesterol oxidase, peroxidase,
Laccase and the like.

[0023]

According to the present invention, an excellent detergency can be obtained in a protein-containing clothing detergent, and when a liquid detergent composition is used, the storage stability of the preparation is good.
The cleaning agent of the present invention is suitable for a liquid cleaning agent.

[0024]

EXAMPLES The liquid detergents shown in Tables 1, 2 and 3 were prepared and evaluated. (1) Detergency evaluation method Sample: A cotton cloth (face plaque) on which facial dirt was evenly rubbed was divided into test stained cloths. Washing conditions: Twenty samples each were sewn on a skin shirt, and the composition was applied at 0.05 mL per one test contaminated cloth, and then placed in a washing tub for washing. Washing condition: Using a two-tub washing machine, 15 g of Super Top (manufactured by Lion Corporation) as a detergent, tap water 3
0L, 25 ° C, 10 minutes, 20 cleaning cloths, 7 skin shirts,
Washing was performed at a bath ratio of 30. Rinsing: Performed twice for 3 minutes under the same conditions as for washing. Detergency:

Calculated by the following equation (1).

(Equation 1) K / S = (1−R / 100) / (2R / 100) R is the reflectance (%) The detergency test method is based on Oil Chemistry 30.432 (198
1) According to “Research on New Artificial Soil (Method 1)”.

Quantification of residual amount of protein: Each washing cloth was treated with 0.
The solution was kept warm in 5 mL of 1N NaOH for 2 hours, and the solution was subjected to a Lowry method (OH Lowry, J. Biol. C).
hem. , 193 265 (1951)) and averaged. Reducing agent sample: dithiothreitol: HSCH ₂ (CHOH) ₂ CH ₂ thioglycerin: C ₃ H ₃ O ₂ S thiourea: CH ₄ N ₂ S cysteine: HSCH ₂ CH (NH ₂ ) COOH cystine: C ₈ H ₁₂ N ₂ O ₄ S ₂ Sulfite Na: Na ₂ SO ₃ Thiosulfate Na: Na ₂ S ₂ O ₃ Hydrosulfite: Na ₂ S ₂ O ₄ Pyrosulfite Na: Na ₂ S ₂ O ₅ Bisulfite Na: NaHSO ₃

[0027]

[Table 1] Table 1: Composition and evaluation results Example Comparative Example 1 2 3 4 5 Composition (% by weight) Nonionic surfactant 10 10 10 10 10 Diethanolamine 10 10 10 10 10 Savinase 16L EX 0.1 0.1 0.1 0.1 0.1 Dithio Threitol 0.1 1 8 30 0.003 Water balance Detergency 93 95 96 97 91 Residual protein (mg) 0.45 0.37 0.33 0.28 0.49 Storage stability ○ ○ ○ × ○

[0028]

[Table 2]Table 2: Composition and evaluation results Example Comparative example  6 7 8 9 10 11 Composition (% by weight) Nonionic surfactant 10 10 10 10 10 10 Diethanolamine 10 10 10 10 10 10 Savinase 16L EX 0.1 0.1 0.1 0.1 0.1 0.1 Dithiothreitol 1 0 0 0 0 0 Thioglycerin 0 1 0 0 0 0 Thiourea 0 0 1 0 0 0 Cysteine 0 0 0 1 0 0 Cystine 0 0 0 0 1 0 Urea 1 10 30---Guanidine hydrochloride--1 10--Calcium chloride 0 0 0.1 0.1 0.1- Water balance Detergency 97 97 96 97 96 91 Residual protein (mg) 0.31 0.29 0.33 0.30 0.35 0.49 

[0029]

[Table 3]Table 3: Composition and evaluation results Comparative example 12 13 14 15 16 17 Composition (% by weight) Nonionic surfactant 10 10 10 10 10 10 Diethanolamine 10 10 10 10 10 10 Savinase 16L EX 0.1 0.1 0.1 0.1 0.1 0.1 Na sulfite 1 0 0 0 0 0 0 Na thiosulfate 0 1 0 0 0 0 Hydrosul Fight 0 0 1 0 0 0 Na pyrosulfite Na 0 0 0 1 0 0 Na bisulfite 0 0 0 0 1 0 Water balance Detergency 91 90 90 91 91 91 Residual protein (mg) 0.50 0.48 0.47 0.49 0.50 0.49 Comparative Examples 12 to 16 are the same as Comparative Example 17 in terms of detergency and protein.
And the same amount of residual material, and the effect of the present invention is
No fruit is observed.

Claims (1)

[Claims] 1. An organic compound capable of cleaving a disulfide bond, (a) a surfactant, (b) a protease, and (c) a disulfide bond.
1 to 20% by weight of a detergent composition for clothing.