JPH02208400A - Bleaching agent composition - Google Patents

Abstract

PURPOSE:To obtain the title composition which can prevent the lipase activity from decreasing due to protease and has excellent bleaching power and detergency for staining with protein and oil by using an H2O2 adduct, a lipase, a protease, and a specified nonionic surface active agent as constituents. CONSTITUTION:The title composition contains an H2O2 adduct (e.g. sodium percarbonate); a lipase comprising an alkaline lipase having a lipase activity at pH9 of at least 30% of that at pH7; a protease; and a nonionic surface active agent (e.g. a polyoxyethylene stearyl ether nonionic surface active agent) having an HLB of 8 to 15.

Description

DETAILED DESCRIPTION OF THE INVENTION [Field of Industrial Application] The present invention relates to a bleach composition containing lipase and protease as enzymes. More specifically, the present invention relates to a bleach composition that suppresses a decrease in lipase activity due to lipase being predated by protease when the bleach is dissolved in water or hot water.

[Conventional technology]

Peroxide compounds such as sodium percarbonate and sodium perborate can be used on more types of clothing than chlorine bleaches such as hypochlorite, and can also be used on colored and patterned items. Because it does not have the characteristic odor of chlorine, it is widely used as the main ingredient in oxygen bleaches, including clothing bleaches, kitchen bleaches, and commercial bleaches.

Incidentally, there are various types of stains and stains that adhere to clothing, tableware, etc., and it is also true that there are many types of stains that cannot be sufficiently removed by oxidative bleaching alone using an oxygen-based bleach. Representative examples of such stains include protein stains and oil stains. In order to effectively remove these stains, it is effective to incorporate enzymes, and various techniques have been proposed to stably incorporate enzymes into oxygen-based bleaches (for example,
1-16319, JP-A-59-129300, etc.).

However, in general, enzymes are relatively stable in bleach baths and are not significantly deactivated during normal bleaching treatment times, so these enzymes are primarily intended for storage stabilization of enzymes in bleach products.

On the other hand, for various stains, multiple enzymes are used rather than a single enzyme.
Furthermore, it is advantageous to mix enzymes that target different decomposition targets, since they can be more effective against various types of dirt. However, there is no problem when combining multiple enzymes with different purposes, such as amylase and cellulase.
When protease is added as an enzyme, other enzymes are also proteins and are therefore eaten by the protease, rapidly losing their enzymatic activity in the bleaching bath.

Looking at the history of the development of enzymes for detergents and bleaches, first an alkaline protease was developed that is effective in weak alkalinity, the same as detergents and bleach processing solutions, and recently, alkaline proteases that are effective even in weak alkalinity have been developed. Lipases have been proposed (eg, Japanese Patent Laid-Open No. 63-68697, etc.).

It is true that when these enzymes are added alone to a weakly alkaline bleach composition, they exhibit a good cleaning (bleaching) effect on target stains, but when both are added to a bleach composition at the same time, lipase Because it was predated by protease, it could not be sufficiently effective against oil and fat stains. In order to solve this problem, JP-A-68697 discloses a method using propylene glycol.

This method of using propylene glycol is for liquid detergents, and its effect is significant in aqueous bleach solutions where a large amount of peroxide is present: 8). Also, since it is a solvent for propylene glycol liquid,
Powdered detergents and bleaches require granulation and addition.
Adding an effective amount of propylene glycol requires adding a large amount of granules, which is uneconomical, and there are also problems with stability during oral storage.

[Problem that the invention seeks to solve]

Therefore, the object of the present invention is to provide a bleach composition that suppresses the decrease in lipase activity caused by protease in a bleach bath and has good bleaching and cleaning power against both protein stains and oil stains.

[Means to solve the problem]

The present invention was completed based on the finding that when a nonionic surfactant having specific physical properties is used at the same time, the decrease in lipase activity caused by protease is significantly improved.

That is, the present invention uses (A) a hydrogen peroxide adduct, (B) a lipase, (C) a protease, and (D) a nonionic surfactant with an HLB value (balance of parent wood groups and lipophilic groups) of 8 to 15. An object of the present invention is to provide a solid bleach composition comprising: The bleach composition of the present invention may be in any solid form, ie, powder, granules, granules, tablets, or the like.

As the hydrogen peroxide adduct of component (A.) used in the present invention, any substance that releases hydrogen peroxide in an aqueous solution can be used. Such substances include percarbonates,
Peroxides such as perborates and perphosphates, hydrogen peroxide adducts such as sodium sulfate, urea, and sodium citrate, and solid superoxide borates as described in Japanese Patent Publication No. 63-41842. There is. The amount of these hydrogen peroxide adducts is not particularly specified, but in order to obtain an effective bleaching effect, the amount of effective oxygen present in the bleaching agent should be 3% or more, preferably 5% or more. Should. If the amount of effective oxygen is below this value, it is necessary to add a hydrogen peroxide bleach activator as described below, or to use other peroxides (e.g. potassium monopersulfate). be. The hydrogen peroxide adduct is preferably granulated by a known method, and preferably has an average particle size of about 500 μm.

As the lipase of component (B), any lipase can be used, but in particular, the lipase activity at pH 9 is 30% or more of the lipase activity at pH 7, preferably 50%.
% or more is preferable.

Most of the previously known lipases have their maximum activity when used at a slightly acidic pH, and their enzyme activity decreases significantly in weakly alkaline solutions such as detergent and bleach solutions. were the majority. However, recently, alkaline lipases that have high enzymatic activity in weakly alkaline aqueous solutions have been developed, and among them, alkaline lipases, which are commercially available from Novo Industries under the trademark Lipolase, have an optimal pH of 8. ~11,
It is an enzyme suitable for use in detergents and bleaches. Therefore, it is particularly preferable to use such alkaline lipase in the present invention. However, if the amount used is large, ordinary lipase can also be used. However, with lipase whose activity at pH 9 is less than 30% of the activity at pH 7, it is necessary to add a considerable amount of lipase to remove oil stains in detergent or bleach aqueous solutions, which is costly. This is not very preferable compared to other points. The lipase activity can be determined by using, for example, olive oil as a substrate and quantifying fatty acids liberated by the action of lipase by alkaline titration. Preferred lipases of the present invention include Cancli
da cylindracea.

Humicola lanuginosa, The
rmomyces lanuginosus.

Pseudomonas fragi, Pseud
omonas cepacia.

Pseudomonas n1troreducens
SPseudomonas gladioli, Pse
udomonas fluorescens , λIu
comb+ehei, 51ucor sp, , Ch
romobacterium viscosum.

Aspergillus niger
There are those of microbial origin such as U.S. japonics.
Lipase MY! J-pase ○F (manufactured by Meito Sangyo ■,
Origin Candidacylindracea), Lipase P1 Lipase CBS (Origin Ps)
eudomonas fluorescens), lipase CE (manufactured by Ohno Pharmaceutical Co., Ltd., Origin Humicolal
anuginosa), lipase sp (Novo Industries, Origin'; Iucor sp,), lipolase (Novo Industries, Origin'), lipolase (Novo Industries, Origin'), recombinant Aspe
rgillusoryzae), lipase (manufactured by Toyo Sanzo Co., Ltd., origin Chromobacterium v
iscosum va, r, lipolyti
cum), Oliverase (Osaka Bacteria Research New Co., Ltd., Origin Rh
1 zopus japonics), lipase B (Sarapolobir flank, origin Pseuclomonas genus), and the like.

Also, in Special Publication No. 53-49394, Humicola
Cultivating lipase-producing filamentous fungi belonging to the genus Thermomyces (including the genus Thermomyces), collecting lipase from the culture, and using Humicol as an example of this producing fungus.
alanug+nosus S-33 strain (Feikoken Bibori No. 1045) has been reported, but such lipases can also be used.

Furthermore, lipases produced from genetically modified microorganisms can also be used. As an example of this, JP-A-62-27
In issue 2988, Aspergillus soryzae
It has been reported that lipase can be produced by using the host as a host, transforming it using recombinant DNA technology, and culturing it in a culture substrate. The blending amount of the lipase of component (B) is 0.01% to 5%, preferably 0.05% to 1% for those whose lipase activity has enzyme units of 1000 to 1,000,000 units.
It is suitable to mix them. Further, these enzymes usually have an average particle size of about 100 to 1000 μm; it is preferable to use granulated ones. In addition, the enzyme unit referred to here is 37℃
The amount of enzyme that releases 1 μmol of fatty acid per minute from the substrate olive oil is defined as 1 unit.

As the protease of component (C), serine protease, pepsin, trypsin, chymotrypsin, cola-
Examples include genase, keratinase, esterase, subtilisin, papain, carboxypeptidase A and B1 aminobebutidase, among which serine protease' is preferred.

These enzymes include Alcalase, Esperase, Savinase (Novo Industrie), and Bioplase (
It can be obtained as commercial products such as Nagashio Sangyo ■), Maxatase (Gist Procades), Sperase (Pfizer), and ALP-2 (Meiji Seika 01). The blending amount of the protease of component (C) is 0.05% to 10%, preferably 0.05% to 10% of the weight of the bleach composition of the present invention, with an enzyme level of protease activity of 1 to 50 units.
It is suitable to mix 0.1% to 3%. Usually, it is preferable to use particles granulated to an average particle size of about 100 to 1000 μm. In addition, the enzyme amount/level mentioned here is 37℃
One unit is the amount of enzyme that liberates an amino acid equivalent to 1 milliequivalent of tyrosine (181.19 mg/dm') from the substrate casein in 1 minute.

The nonionic surfactant of component (D) is an alkylene oxide addition type nonionic surfactant whose HLB value (
Hydrophile-1pophile Ba1an
Any material having a ce woodphilicity/oleophilicity balance of 8 to 15 can be used. Note that several methods have been proposed for the formula for calculating the HLB value (for example, Gri
ffin formula, Davies formula, world formula, etc.), but the HLB value referred to in the present invention is calculated from an organic conceptual diagram. Organic concept diagram! The hard part is “The domain of chemistry” Vol. 11.
No. 10 (October 1957 issue) p. 719
It is described in detail in ``Organic Concept Diagram - Basics and Applications'' written by Yoshio Koda (Sankyo Publishing (1985), etc.), but organic compounds are composed of hydrocarbons consisting of covalent bonds between carbon chains. Focusing on the fact that it is composed of two factors: ``characteristic'' and ``inorganic'' due to the influence of electrostatic properties present in substituents (functional groups), individual organic compounds can be classified into ``organic'' and ``inorganic''. ”, and H calculated from the organic conceptual diagram
The LB value is expressed by the following formula.

HLB - (inorganic value/organic value) x 10 where the organic value is calculated as 20 per carbon atom in the structural formula of the compound, and the inorganic value is calculated as 20 per carbon atom in the structural formula of the compound, and the inorganic value is calculated as It is calculated using a fixed value. Incidentally, the inorganic value of the ether group is usually 20, but COCH2CH2
] - The inorganic value of 〇- in the group and 〇- in the ○ heteromonocycle is,
Japanese Patent No. 1362396 (Special Publication No. 1986-3)
75 described in Japanese Patent Publication No. 9791). Therefore, for example, in the case of polyethylene ethylene (average degree of polymerization 10) lauryl ether, Cl28250CH2
CH2 (OCH2CH2) 9 leaves, organic value = 2
0X32-640, inorganic value -20+75X9+100
-795, HLB=12.4. This value is the HLB value 12.1 according to the above formula (World formula HLB = 711, 7
(Hydrophilic group molecular weight) = 44XIO+16÷IMo (Lipophilic group molecular weight) 12X14+1).

Examples of such nonionic surfactants include higher alcohols with 8 to 24 carbon atoms, polyhydric alcohol/basic fatty acids,
It is an alkylene oxide adduct of a synthetic alcohol obtained by converting fatty acid amide, fatty acid amine, alkylphenol, n-paraffin, or α-olefin into M. As the alkylene oxide, ethylene oxide, propylene oxide, and butylene oxide are used. Specifically, POE (lower-10) lauryl ether [:HL
Bl2.4'l, POE (lower = 9) C,2,4 secondary alkyl ether [:HLB = 11.8], POE (
〒15) Hexyldecyl ether [HLB=12.9]
, POE (bottom = 20) nonylphenyl ether [:H
LBL 4.61, POE (un-11) stearyl ether [HLB=10.9:], POE (lower=10
) Glyceryl monostearate [HLB-11,0)
, PO8 (lower-=10) isostearyl ether [HL
B-10, 6, POE (lower-50) trimethylolpropane I: HLB=12. O], POE (〒-30)
Hydrogenated castor oil [HLB=11.0'J, FOE (lower 6
0), hydrogenated castor oil monolaurate [:HLBl2.6
), POE (Bottom-20) Sorbitan monooleate [:
HLB=13.9], POE (lower-30) Glycertriisostearate) ['HLB=9.81, POE
(p-20) Glyceryl monostearate [:HLB
=13.51, POE (〒=10) monostearate [11,0], POE (〒=6) stearylamine [:HLB= 15.0:l, lauroylgetanolamide I:HLB=12.5] , POE penalty 10)
Stearylamide, POE (lower = 9) POP (un-
b) Cl2-14 secondary alkyl ether [HLB
=9.0] etc. In addition, POE represents polyoxyethylene, POP represents polyoxypropylene, and p represents the average number of added moles of alkylene oxide.

If the HLB value of the nonionic surfactant is below this value, the predation inhibitory effect on protease lipase will be rapidly lost, and if the HLB value is higher than this value, the predation inhibitory effect will be lost, so it is necessary to add a large amount of nonionic surfactant. Not economical. The amount of component (D) to be blended is approximately 0.05 to 10%, preferably 0.5 to 5%, based on the weight of the bleach composition of the present invention. The required amount of component (D) is:
It varies somewhat depending on the amount of protease in component (C).
As the amount of component (C) increases, the required amount of component (D) also tends to increase. Therefore, the amount of component (D) necessary for component (C) to suppress predation of component (B) is
/ component (D) ratio is 1/30 to 1/1, preferably,
It is preferable to determine the blending amounts of component (C) and component (D) so that the amount falls within the range of 1/10 to 1/2. However, the component (D
Among the nonionic surfactants (), those with 8 to 12 carbon atoms and an average of 8 to 20 moles of ethylene oxide can be used as cleaning agents. D) may be 10% or more. Therefore, it may be determined by considering the performance, cost, and stability of the hydrogen peroxide adduct of component (A) of the bleach composition. Component (D) may be in a solid state, but it is usually in a liquid or paste state, and it is not preferable to add it to the bleach composition as it is. Therefore, it is desirable to granulate it by an appropriate means before adding it. There are various known granulation methods, but the easiest method is to dissolve component (D) as it is or in an appropriate solvent (e.g., water or lower alkanol) and granulate it at room temperature to
This is a method in which the material is pulverized and granulated at a temperature of about 100° C. while being rolled over an inorganic bilge, which will be described later. Other granulation methods include, for example, Genga Important Cultural Property, ``Chemical Engineering'' by Heiichi Higashihata.
Although described in ``Tokyo Kagaku Dojin (1977), etc., the component (D>) of the present invention is not limited to these granulation methods.

The bleaching composition of the present invention may contain various other additives. Among such additives, a particularly important one is an enzyme deactivation inhibitor in bleach compositions, as disclosed in Japanese Patent Application Laid-Open No. 129300/1983. Such compounds include anhydrous calcium sulfate;
Examples include calcium sulfate 1/2 hydrate, magnesium chloride, aluminum sulfate, and the like. The blending amount of these enzyme stabilizers varies depending on the blending amount of the bleach component (A) and the blending amount of the enzyme, but 0.1
It is desirable that it be blended in an amount of ~10% by weight, preferably 0.5~5% by weight.

Also, when enzymes are mixed into bleach, the odor peculiar to enzymes (
(hereinafter abbreviated as enzyme odor) may be emitted.

This enzyme odor is generally thought to originate from the culture medium during the enzyme production process, but such odor is not desirable. As a method of masking this enzyme odor, a particularly excellent masking effect can be obtained by using a fragrance as disclosed in Japanese Patent Publication No. 11996/1983, for example.

Furthermore, enzymes other than lipase and protease, such as cellulase and amylase, may be added. Examples of such enzymes include Celluclast, Cellzyme (Novo Industries), [:ellulase
Cellulases such as (Gist Procades), Soluble Sucrase (Sankyo@), Mycellase (Meiji Seika), Coomamil (Novo Industries) and 'J
) and bacterial α-amylase. These can be used in amounts of 0.01 to 5% based on the bleach composition of the present invention.

In the present invention, it is preferable to further add various phosphates, magnesium salts, and silicates as stabilizers of the component (A>.Specifically, phosphates, pyrophosphates, metaphosphates, These include triphosphates, metasilicate, orthosilicate, magnesium silicate, magnesium chloride, magnesium sulfate, and organic chelating agents (e.g., ethylenediaminetetraacetate, sodium nitriloacetate, diethylenetriaminepentaacetate), etc. It is particularly desirable that the stabilizer be added during granulation of component (A).

In addition, aluminosilicates (e.g., zeolite A), sodium sulfate, sodium carbonate, potassium sulfate, sodium silicate, phosphates (tripolyphosphate), ethylenediaminetetraacetate, nitriloacetic acid, which are known as cleaning agents Virgoo. Sodium, diethylenetriamine pentaacetate, citric acid, malic acid, 1-hydroxyethane-1,1 diphosphonate, acrylic acid, maleic anhydride, copolymer acrylic acid salt, methacrylic acid copolymer salt, etc. It is more preferable to add various inorganic and organic builders from the viewpoint of improving detergency. These builders can generally be added in an amount of 0 to 30% by weight based on the bleach composition of the present invention.

Furthermore, in order to enhance the cleaning effect, various surfactants can be added in addition to the nonionic surfactant as a protease predation inhibitor specified in component (D). Such surfactants include alkylbenzene sulfonates, olefin sulfonates, polyoxyethylene (p-
-0,5-8) Anionic surfactants such as alkyl ether'&Ae salts, alkyl (alkenyl) sulfates, saturated or unsaturated fatty acid salts and α-sulfo fatty acid salts or esters, polyoxyethylene (p-40) alkyl Nonionic surfactants such as phenyl ether and polyoxyethylene (50) alkyl ether; cationic surfactants such as dialkyldimethylammonium chloride and alkyltrimethylammonium chloride; amphoteric surfactants such as alkylami7betaine;
These include semipolar surfactants such as alkyl dimethylamine oxide and mono- or jetanolamide having an N-acyl group, and fluorine-based surfactants. The term "alkyl group" or "acyl group" as used herein is a general term for a saturated, unsaturated, or branched alkyl group or acyl group having an average carbon number of 8 to 20. Incidentally, the amount of the surfactant to be blended can generally be 20% or less based on the weight of the bleach composition of the present invention.

Further, in order to further enhance the bleaching effect, a peroxide compound other than the hydrogen peroxide adduct can be added.

Such compounds include potassium persulfate, potassium peroxy-sulfate (complex salt of 2 moles of potassium peroxyhydrogensulfate, 1 mole of potassium hydrogensilicate, and 1 mole of potassium sulfate, commercially available from DuPont under the trade name Oxone); It is a peroxide compound such as Furthermore, compounds such as organic peracids can also be used if they are in granulated form. Such organic peracids include dodecane diperacid, monoperphthalic acid, etc., and these organic peracids and inert inorganic salts (e.g., sodium sulfate, sodium chloride, IJum, etc.)
Particularly preferred are organic peracids in the form of granules with various binders.

In addition, in order to enhance the bleaching effect, a known activator for hydrogen peroxide may be used. Such activators include N-acynope O-, which reacts with hydrogen peroxide to produce organic peracids.
Acyl type peracid precursors are known. Specifically, they include tetraacetylglycoluril, pencacetylglucose, tetraacetylethylenediamine, sodium nonanoyloxybenzenesulfonate, alkyloxycarbonyloxybenzenesulfonate, and the like. Also, Japanese Patent Application Laid-Open No. 61270800 and West German Patent DE
-Nitrogen-containing heteroalicyclic compounds and non-heterocyclic N-halo hindered amine compounds in which the hydrogen atom of the secondary amine group in the heterocycle is replaced with a halogen atom, as described in No. 3731506, 4A. There is a method in which singlet oxygen is generated by reacting with hydrogen peroxide. According to this method, not only can excellent bleaching effects be obtained even at low temperatures, but also the revolutionary effect of hardly causing discoloration or fading of colored or patterned clothing can be obtained. Such compounds include 1-chloro-piperidine, 1-chloroisonibecotic acid, 1-chloro-piperidine,
Chloro-4-hydroxy-2゜2.6.6-titramethylpiperidine, 1-chloro-4-[N-acetyl-N-
methylamino]2,2,6,6-titramethylpiperidine, 2(N-chloro-t-butylamino)-ethanol, and the like. The blending amount of these activators is 1 of H2O2 contained in the hydrogen peroxide adduct of component (A) to be used.
It is desirable to add the activator in an amount of about 0.02 to 1 mole per mole.

In addition, the product of the present invention further contains appropriate amounts of various trace additives such as coloring agents such as pigments and dyes, silicone, bactericides, antioxidants, fluorescent whitening agents, and ultraviolet absorbers (the bleaching agent of the present invention). Each of them can be added in an amount of about 0 to about 2% by weight based on the agent composition.

〔Effect of the invention〕

According to the present invention, even if lipase and protease are used at the same time, the lipase is hardly eaten by the protease, so the bleach composition has an excellent bleaching effect on both protein stains and oil and fat stains. can get things.

The present invention will be explained below with reference to Examples, but the present invention is not limited thereto.

〔Example〕

-Method for measuring enzyme activity (1) Method for measuring lipase activity Using olive oil as a substrate, fatty acids liberated by lipase action were quantified by alkaline titration, and lipase activity was determined from the numerical value.

4 ml of olive oil emulsion (containing 25% olive oil) dispersed in water with polyvinyl alcohol and Q, l mol
- Accurately place dm-3 phosphate buffer (pH 7.0) and 4mβ into a 50mβ volume stoppered Erlenmeyer flask, mix well, and preheat for 10 minutes using a 37°C constant temperature water bath. Add 1m+j of enzyme sample solution to this! Add exactly, mix well, and keep at 37°C while shaking. After exactly 10 minutes, add 20 mβ of acetone/ethanol mixture to stop the reaction.
Titrate with 0.05 N hydroxide (IJ) solution using phenoltskurein as an indicator. The same operation was performed in a system that did not contain the sample solution to serve as a control solution.

The difference between the titrations of the test solution and the control solution was defined as the amount of enzyme activity.

In addition, the measurement at pH 9 is Q, 2 mol dm-3
) Liss buffer was used, and the rest was carried out according to the above method.

(2) Protease activity measurement method As a substrate, milk casein (Merck Hamm
The protease activity was determined by measuring the absorbance at 275 nm derived from an amino acid having a phenyl group such as tyrosine produced by the action of a protease.

Accurately weigh 6.0g of casein, add IN-Na[]8
While gradually adding 330 m of
9mp! The solution was added and dispersed, and finally the pH was adjusted to 10.5 with IN-NaOH, and the volume was adjusted to 16 m3. 18m
In a test tube with a diameter of m, add 1 mβ enzyme sample solution and 3
7℃! Add exactly 5 mβ of the strained casein solution, stir for about 10 seconds with a flash mixer, put it in a constant temperature water bath at 37°C, and after exactly 30 minutes, add 0.44 mol/clm-3) IJ.
Accurately add 5 mff1 of chloroacetic acid solution, stir with a flash mixer to stop the reaction, return to the constant temperature water bath, and filter after 30 minutes.

The same operation was performed on a system not containing the sample solution, which was used as a control solution. The absorbance (0, D, value) of this filtrate was measured at a measurement wavelength of 275 nm using a colorimeter, and the difference in absorbance between the test solution and the control solution was defined as the amount of enzyme activity.

・Measurement method for bleaching effect (1) Pretreatment of test cloth A plain woven cotton cloth (#100.20x30cm) was washed at 50°C at 30 times the bath ratio in a household washing machine using a commercially available detergent ('Alpha' manufactured by Lion 0). After washing for 15 minutes, dehydrate for 5 minutes. Wash and dehydrate in the same manner again. Next, perform overflow rinsing for 15 minutes, and then dehydrate for 5 minutes. Overflow rinsing and undressing operations are performed 5 times in total. This was repeated and then air-dried to obtain a pretreated fabric.

(2) Creation of black tea contaminated cloth Boil a 2% solution of black tea (Twining black tea: 0RANGE PEKOE 几A) for 5 minutes, filter the tea, then soak the pretreated cloth in the solution at 30 times the bath ratio and boil for 30 minutes. death,
After leaving it at 40℃ for 30 minutes and air drying, it becomes 5x5cm! The test cloth was cut into pieces (tea-contaminated cloth).

(3) Making milk tea contaminated cloth Black tea (Twink tea: 0RANGE PEK mouth ET
Boil the % solution to E8) for 5 minutes, filter the tea, add commercially available milk from a colleague (Meiji Dairies ■: Meiji 3.4 milk), and soak the pretreated cloth in this at 30 times the bath ratio. 30 at 60℃
After being left to air dry for a minute, it was cut into 5 x 5 cm pieces to obtain a test cloth (milk black tea stained cloth).

(4) Preparation of oil-contaminated cloth 30 g of pharmacopoeial soybean oil in 1 Lindl of benzene (grade 1 reagent)
and 0.25 g of carbon black were ultrasonically dispersed for 5 minutes to create a stable dispersion, which was used as a dirt bath. The pretreated cloth is immersed in this dirt bath and air dried. After dry-smoking this dirty cloth at 105℃ for 30 minutes, both sides of the dirty cloth were
Rub 5 times each. It was cut into 5 x 5 cm to prepare a test cloth (oil-stained cloth).

(5) Measurement of bleaching rate Dissolve the bleach composition in water at 20°C (hardness: 3°DH) to a concentration of 0.5%, and soak various contaminated cloths in the solution at a concentration of 100 times the bath ratio. The sample was left for a predetermined period of time (30 minutes).

The test fabric thus treated was sequentially dehydrated for 1 minute, overflow rinsed for 1 minute, and undressed for 1 minute in a household washing machine, and then dried by ironing to obtain a bleached fabric. Measure the reflectance (Z value) of pre-treated fabrics, various contaminated fabrics, and bleached fabrics using a color difference meter (manufactured by Nippon Juishoku ■'1-80).
), and the bleaching rate was calculated using the following formula.

Example 1 (A) Sodium percarbonate (effective oxygen amount 14.0%,
average particle diameter of 500 μm) Near 5.0 (wt%) (B) Reverse (manufactured by Novo Industries; Rivolase 30T granulated product) (C) Protease (manufactured by Novo Industries;
Alcalase 2.0T, granulated product) (D) Polyoxine ethylene stearyl ether type nonionic activator with different HLB values (E: optional ingredient) carbonic acid) IJum (light ash) 0.5 1.0: Consists of the remainder A bleach composition was prepared. In addition, the nonionic surfactant of component (D) is sprayed onto sodium carbonate (light ash) at 80 to 90°C, thoroughly stirred, and the average particle size is approximately 150μ.
m powder detergent. This and ingredients (A) and (B)
, (C) were powder blended to prepare a bleach composition. As a result of bleaching various contaminated fabrics with these bleach compositions,
Table 1 shows the amount of enzyme activity remaining in the solution after storing the 1.5% bleach solution at 37°C for 30 minutes.

Comparative examples were prepared in which a nonionic surfactant with an HLB value of 16.1 was used in the same proportion, and one in which no nonionic surfactant was used at all.

As can be seen from Table 1, when a nonion with an HLB of 8 to 14 is used, the amount of lipase remaining in the bleach solution increases, and as a result, the bleaching rate, especially for oil stains, increases.

Example 2 Next, compositions were prepared with various blending amounts and their performance was evaluated. Note that the lipase used here was an ungranulated product, and was granulated and used as follows.

100g of various lipases, 500g of table salt and Ca5O<
・Add 300 g of 2H20, and add 100 g of a 1% aqueous solution of carboxymethyl cellulose to a mixing granulator (
20 Orp using λ, IA-10 type manufactured by Nara Manufacturing Co., Ltd.
It was granulated at m. After drying the particles in a fluidized bed and adjusting the moisture content to 3%, 30g of PEG #600 and 50g of titanium oxide were added.
g was added to coat the surface. After cooling, it was sieved to obtain lipase particles with an average particle size of 500 μm. The method for granulating component (D) was the same as in Example 1.

The results are summarized in Table 2. These bleach compositions are
As shown in Table 2, it exhibited excellent bleaching effects.

Lipase ■; Lipase P (Pseuchromonas
Lipase produced from Humicola lanuginos) Activity ratio -100% (pH 9/pt17) Lipase ■: Lipase CE (Humicola lanuginos
Lipase produced from Amano Seiyaku) Activity ratio = 70% (pH 9/ρ117) Lipase ゛■; Lipase ゛AP
Amano Pharmaceutical) Activity ratio = 20% (pH 9/pH 7) Potassium monopersulfate; Oxon (Dupont) Anionic detergent; Contains 30% sodium linear alkylbenzene sulfonate Detergent procedure amendment 1, Display of the case 1999 Patent Application No. 27956 2, Name of the invention Bleach composition 3, Person making the amendment Relationship to the case

Claims (2)

[Claims] (1) (A) Hydrogen peroxide adduct (B) Lipase (C) Protease (D) HLB value (balance between hydrophilic group and lipophilic group) is 8 to 1
A solid bleach composition comprising a nonionic surfactant of No. 5. (2) The bleach composition according to claim 1, wherein the lipase of component (B) is an alkaline lipase whose lipase activity at pH 9 is 30% or more of the lipase activity at pH 7.