Detergent composition

Details Detergent composition Detergent composition

2000-03-17

2001-03-06

Fries, Kery (Department: 1751)

Cleaning compositions for solid surfaces, auxiliary compositions

Cleaning compositions or processes of preparing

Enzyme component of specific activity or source

C510S320000, C510S321000, C510S226000, C510S392000, C510S530000, C510S305000, C510S307000, C510S306000, C510S357000, C510S350000

Reexamination Certificate

active

06197740

ABSTRACT:

TECHNICAL FIELD
The present invention relates to a detergent composition.
1. Prior Art
Incorporating an enzyme into a detergent composition has been practiced, and, for example, JP-A 1-501486 discloses a detergent composition using two or more specific kinds of proteases. However, since enzymatic activity is lowered under the laundering condition at a low temperature, a satisfactory washing-performance cannot be obtained and this problem is particularly remarkable in protein-related dirt of soiled socks, necks, and so on. Although JP-A 62-68898 discloses a detergent composition in which enzyme is stabilized by a sulfite, this composition does not satisfactorily solve the two problems of enzyme deactivation and washing-performance at a low temperature, either.
2. Disclosure of the Invention
The object of the present invention is to provide a detergent composition which is almost free from enzyme deactivation, which is excellent in detergency under laundering conditions at a lower temperature, and which is effective particularly for protein-related dirt (of) on soiled socks and other items.
The present invention provides a detergent composition comprising
(a) 15 to 40% by weight of an anionic surfactant,
(b) 0.5 to 5% by weight of a chlorine scavenger,
(c) a protease whose a-keratin-hydrolyzing activity at 10° C. is not less than 0.09×10
−3
&mgr;g/mPU·min and
(d) a protease whose &agr;-keratin-hydrolyzing activity at 10° C. is less than 0.09×10
−3
&mgr;g/mPU·min,
wherein (c)+(d)=0.01 to 0.5% by weight (as powdered enzyme product), (c)/(d)=1/5 to 5/1 and [(c)+(d)]/(b)=1/100 to 1/2 (weight ratio as powdered enzyme product).
Herein, the term “enzyme powder” means the enzyme product powdered by lyophilizing the supernatant of the fermenter broth concentrated by ultrafiltration.
MODE FOR CARRYING OUT THE INVENTION
An anionic surfactant is the “(a)” component in the present invention. Examples of the anionic surfactant include an alkylbenzenesulfonate, an alkylsulfate, an alkylethersulfate, an olefinsulfonate, an alkanesulfonate, a fatty acid salt, an alkyl or alkenyl ether carboxylate and an &agr;-sulfofatty acid salt or an ester thereof. Among them, an alkylbenzenesulfonate whose alkyl group has 10 to 20 carbon atoms, an alkylsulfate having 8 to 18 (preferably 10 to 14) carbon atoms, an alkylethersulfate having 8 to 18 (preferably 10 to 14) carbon atoms, and a fatty acid salt being derived from palm oil or tallow and having 8 to 18 (preferably 10 to 18) carbon atoms, are preferable. The average molar number of ethylene oxide added in the alkylethersulfate is preferably 1 to 20, more preferably 1 to 10 and particularly preferably 1 to 5. As the salts, a salt of an alkaline metal such as sodium and potassium is preferable. The incorporated amount of the “(a)” component is 15 to 40% by weight, preferably 20 to 40% by weight, in the composition from the standpoint of detergency and foaming property.
In the present invention, in order to prevent the enzyme from being deactivated by chlorine which is present in water, a chlorine scavenger is the “(b)” component. Specific examples of the scavenger include an amine such as a primary amine, a secondary amine and an alkanol amine; an inorganic peroxide such as hydrogen peroxide, sodium percarbonate and sodium perborate; a reducing agent such as a sulfite. Among them, a sulfite is preferable from the standpoint of stability in the composition and enzyme-stabilizing effect in a laundering bath. From standpoint of the stability of enzyme, the “(b)” component is incorporated in an amount of 0.5 to 5% by weight, preferably 0.5 to 2% by weight, in the composition.
A protease, whose &agr;-keratin-hydrolyzing activity at 10° C. is not less than 0.09×10
−3
&mgr;g/mPU·min, preferably not less than 0.10×10
−3
&mgr;g/mPU·min, more preferably not less than 0.12×10
−3
&mgr;g/mPU·min and furthermore preferably not less than 0.13×10
−3
&mgr;g/mPU·min and whose &agr;-keratin-hydrolyzing activity at 30° C. is preferably not less than 0.40×10
−3
&mgr;g/mPU·min, more preferably not less than 0.44×10
−3
&mgr;g/mPU·min and furthermore preferably not less than 0.47×10
−3
&mgr;g/mPU·min, is used as the “(c)” component in the present invention.
In addition, a protease, whose &agr;-keratin-hydrolyzing activity at 10° C. is less than 0.09×10
−3
&mgr;g/mPU·min and preferably less than 0.07×10
−3
&mgr;g/mPU·min and whose &agr;-keratin-hydrolyzing activity at 30° C. is preferably less than 0.40×10
−3
&mgr;g/mPU·min, more preferably less than 0.35×10
−3
&mgr;g/mPU·min, furthermore preferably less than 0.30×10
−3
&mgr;g/mPU·min and particularly preferably less than 0.20×10
−3
&mgr;g/mPU·min, is used as the “(d)” component.
Here, the &agr;-keratin-hydrolyzing activity was expressed as a soluble material (calculated as based on tyrosine) formed from &agr;-keratin for 1 minute per casein hydrolyzing activity of 1 mPU shown in the following (ii). That is, the &agr;-keratin-hydrolyzing activity was measured according to the following (i) to (iii) methods.
(i) Preparation of &agr;-keratin
A part of skin of human heel (horny layer) was cut off with a surgical knife, and, after being cut into pieces with a pair of scissors, washed with distilled water. One gram of this horny skin was suspended in 20 to 50 ml of a 50 mM Tris-HCl buffer (pH: 8.0) containing 8 M of urea and 25 mM of &bgr;-mercaptoethanol, and stirred overnight. The swollen horny skin was sufficiently ground by a TEFLON HOMOGENIZER™ and subjected to centrifugal separation at 30,000×g for 30 minutes. The supernatant liquid obtained by the centrifugal separation was filtered through a filter paper (No.2 supplied by Whatman International Ltd.). The filtrate underwent dialysis to a 50 mM Tris-HCl buffer (pH: 8.0) and was then subjected to centrifugal separation at 100,000×g for 2 hours. The precipitate obtained was dissolved in a 50 mM Tris-HCl buffer (pH: 8.0) containing 8 M of urea and 25 mM of &bgr;-mercaptoethanol. The solution thus obtained again underwent dialysis to a 50 mM Tris-HCl buffer (pH: 8.0) and was then subjected to centrifugal separation at 100,000×g for 2 hours. After the supernatant liquid was removed, the precipitate was dissolved in a 50 mM Tris-HCl buffer (pH: 8.0) containing 8 M of urea and 25 mM of &bgr;-mercaptoethanol. The solution thus obtained underwent dialysis to distilled water and was pulverized to prepare powder after lyophilizing. The powder product was used as &agr;-keratin.
(ii) Measurement of Casein-hydrolyzing Activity
After 1 ml of a 50 mM boric acid buffer (pH: 10.5) containing 1% (w/v) of casein (Hammarsten, supplied by Merck) was held at 30° C. for 5 minutes, 0.1 ml of an enzyme solution was added and incubated at 30° C. for 15 minutes. Next, 2 ml of a TCA solution (0.11 M trichloroacetic acid, 0.22 M sodium acetate and 0.33 M acetic acid) was added thereto. After the resulting solution was left to stand for 10 minutes at room temperature, the acid-denatured protein was eliminated by filtration and the acid-soluble peptides contained in the filtrate were quantified by the Lowry method. That is, 2.5 ml of an alkaline copper solution [a 1:1: 100 (v/v) mixture of a 1% (w/v) potassium sodium tartrate aqueous solution, a 1% (w/v) copper sulfate aqueous solution, and a solution prepared by dissolving sodium carbonate in a 0.1 M sodium hydroxide aqueous solution (sodium carbonate concentration: 2% (w/v))] was added to 0.5 ml of the filtrate. After the resulting solution was kept at 30° C. for 10 minutes, 0.25 ml of a diluted phenol reagent (obtained by 2-fold dilution of folin-ciocalteu's phenol reagent with distilled water) was further added. Then, after the resulting solution was kept at 30° C. for 30 minutes, the absorbance at 660 nm was measured. Meanwhile, the result, obtained by adding the enzyme solution after adding

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