JPH11323392A - Detergent composition - Google Patents

Abstract

PROBLEM TO BE SOLVED: To obtain a composition exhibiting excellent detergency for muddy stain by formulating an enzyme having pectinase activities, a surfactant and at least one selected from amino acids and sugars. SOLUTION: As an enzyme having pectinase activities (A) is particularly preferable a pectinase derived from genus bacillus. As surfactants (B) are preferable anionic surfactants and nonionic surfactants. As amino acids (C) are preferable neutral amino acids such as tyrosine, glycine, alanine and the like, acidic amino acids such as aspartic acid, glutamic acid and the like and basic amino acids such as histidine, lysine, arginine and the like. Further, as sugars are preferable glucose and galactose which are monosaccharide, and sucrose, trehalose and lactose which are disaccharide. Preferably the total composition comprises formulating 0.001-30 wt.% of the component A which has an activity of at least 100 U/g solid content, 0.01-60 wt.% of the component B and 0.001-10 wt.% of the component C.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

[0001] The present invention relates to a detergent composition exhibiting excellent detergency against mud stains.

[0002]

BACKGROUND OF THE INVENTION Patent applications relating to pectinase include WO95 / 25790,
Japanese Patent Publication No. 6-39596 and WO 97/11146 describe that pectinase has an excellent cleaning effect on inorganic soil and food stains. However, the cleaning effect of the pectinases disclosed in these publications is still insufficient, and it is necessary to incorporate a considerable amount of the enzyme in order to obtain the desired effect.

On the other hand, pectinase conventionally found in nature often does not have sufficient enzyme productivity, and even if the productivity is sufficient, the production cost is relatively high, so that it has the desired effect. It is economically difficult to design a suitable detergent.

[0004] In order to cope with such a problem, in addition to improving the enzyme productivity, a method for improving the reaction rate of the enzyme in an enzyme reaction system has been conventionally used for the purpose of sufficiently reacting with a short reaction time and a small amount of the enzyme. Although it has been studied, many of them are related to cellulase and amylase (JP-A-60-2
No. 10984, Japanese Translation of PCT International Publication No. 5-507615, Biotechnol. Bio
eng., 29, 901-902 (1987), JP-A-8-256768), and pectinase has not been reported much and its activity is still insufficient.

[0005]

The present invention provides a detergent comprising the following components: (a) an enzyme having pectinase activity, (b) a surfactant, and (c) at least one selected from amino acids and sugars. It provides a composition.

[0006]

DETAILED DESCRIPTION OF THE INVENTION The pectinase activity of component (a)
As an enzyme, 1 μmol / g
The amount of enzyme that produces cucuronic acid equivalent reducing sugar is defined as 1U
In this case, the activity of at least 100 U / g solid content or more
Enzymes that have protopectinase activity
Enzymes that have a combination are preferred. Protopectinase is Ca
²⁺, Mg ²⁺Of pectin molecules by intermolecular bonding and
Alternatively, the pec insolubilized by binding to cellulose molecules, etc.
Protin pectin (insoluble natural pectin)
A general term for enzymes that act, their activity is based on the use of cotton pectin as a substrate.
Has a cotton pectin release power of 0.2mg / g cotton or more
Enzymes are preferred. Here, the cotton pectin release force is
The enzyme (0.4 mg / ml) was added to the yarn (20 mg / ml) at pH 8.0.
At 1 hour at 30 ° C for 1 hour
Pectin amount (mg). The substrate used in this assay
Pectic acid content of ammonium oxalate
A yarn that becomes 1.5 to 2.5 mg / g cotton by a rubber extraction method is used.
Details of pectinase activity and protopectinase activity
Detailed measurement methods and the activity values of each enzyme are described in the Examples below.
Put on.

[0007] The pectinase component (a) used in the present invention, but its origin is not particularly limited, the plant can be used those which are widely distributed in bacteria and fungi, for example, bacteria such as Bacillus (Bacillus) Genus Tricosporon , Endomyces ,
End Maiko-flops cis genus (Endomycopsis), Saccharomyces (Saccharomyces), Schizosaccharomyces genus (S
chizosaccharomyces), the genus Pichia (Pichia), Hansenula (Hansenula), Debaryomyces genus (Debaryomyce
s), Hanseniasupora genus (Hanseniaspora), Torulopsis (Torulopsis), yeast such as Candida (Candida), Kluyveromyces (Kluyveromyces); the genus Fusarium (Fusarium), Garakutomaisesu genus (Galact
omyces), Aspergillus (Aspergillus), Rhizopus (Rhizopus), such as filamentous fungi such as Trametes sp (Trametes) and the like. Among them, pectinase derived from Bacillus is particularly preferred.

In the present invention, the following pectinase using these various origin bacteria can be used. Sucrase N (Sankyo Co., Ltd.), Pecturiase (Kikkoman Co., Ltd.), Pectinase SS (Yakult Co., Ltd.), Pectinase Tanabe (Tanabe Seiyaku Co., Ltd.), Pectinase HL (Yakult Co., Ltd.) and the like. Further, an enzyme having both protopectinase activity in an alkaline region is preferable. Particularly, Bacillus sp. Strain KSM-P15 (FERM BP-6241) and Bacillus sp.
Enzymes having protopectinase activity derived from SM-366 strain (FERM BP-6262) are more preferred.

The amount of the enzyme having pectinase activity of the component (a) to be added to the detergent composition of the present invention may be an amount capable of exhibiting the enzyme activity. It is advisable to add 0.001 to 30% by weight, preferably 0.01 to 10% by weight of the total composition.

As the surfactant of the component (b) to be blended in the present invention, an anionic surfactant and a nonionic surfactant are preferable from the viewpoint of improving the detergency. In particular, as the anionic surfactant, a linear alkyl benzene sulfonate having an alkyl chain having 10 to 18 carbon atoms, an alkyl sulfate, a polyoxyalkylene alkyl ether sulfate, and an alpha sulfo sulfate are preferable, and tallow and coconut oil are preferable. A small amount of a fatty acid salt derived therefrom may be blended. Further, polyoxyalkylene alkyl ether is preferable as the nonionic surfactant.

The surfactant of the component (b) accounts for 0.0% of the total composition.
It is preferable to add 1 to 60% by weight, particularly 10 to 45% by weight.

The amino acids of component (c) used in the present invention are preferably neutral amino acids such as tyrosine, glycine and alanine, acidic amino acids such as aspartic acid and glutamic acid, and basic amino acids such as histidine, lysine and arginine. It may be salt. As the salt, a sodium salt, a potassium salt, and an ammonium salt are preferable.
As the sugar, glucose and galactose which are monosaccharides, sucrose which is a disaccharide, trehalose and lactose are preferable. Amino acids and sugars may be used in combination.

The amount of component (c) is preferably 0.001 to 10% by weight, more preferably 0.01 to 5% by weight, based on the total composition, from the viewpoint of improving the detergency.

In addition to the above essential components, the cleaning composition of the present invention comprises a zeolite, a crystalline aluminosilicate,
Sequestering agents such as crystalline silicates (eg, SKS-6) described in Examples of JP-A-7-89712 and JP-A-60-227895, and organic metals such as ethylenediaminetetraacetic acid (EDTA) and citrate Ion sequestering agents, polyacrylic acid, copolymers of acrylic acid and maleic acid, carboxylic acid polymers such as carboxymethyl cellulose, polyethylene glycol (PEG), polyvinylpyrrolidone (PV
P), alkali metal carbonates such as soda ash, JIS1,
Alkali agents such as alkali metal silicates such as sodium silicates No. 2 and 3, bulking agents such as sodium sulfate, bleaching agents such as sodium percarbonate, and the general formula (I-2) described in JP-A-6-316700 , (I-3), (I-4), (I-
5) Compounds represented by (I-6) or (I-2), bleach activators such as tetraacetylethylenediamine (TAED), enzymes such as proteases, cellulases, amylases and lipases, boron compounds and sodium sulfites JP-A-8-2180 such as enzyme stabilizers, biphenyl type and stilbene type fluorescent dyes, defoamers such as silicone / silica, antioxidants, bluing agents and fragrances
No. 93, page 4, column 5, line 18 to page 7, column 11, line 17 can be used.

As a method for producing the cleaning composition of the present invention, a conventionally known production method can be used, and the production conditions can be appropriately selected according to the composition and the like.

[0016]

According to the present invention, a detergent composition having excellent mud stain cleaning power can be obtained.

[0017]

[Examples] 1. Measurement method of pectinase activity Polygalacturonic acid (PG; ICN Biomed) in the reaction system
icals, Ohio) 0.9 ml of substrate lysis buffer so that the final concentration is 0.5% and the final concentration of CaCl ₂ is 0.5 mM.
, 0.1 ml of an enzyme solution having an appropriate concentration was added thereto, and the mixture was added at 30 ° C and 2 ml.
The reaction was performed for 0 minutes. The buffer solution of the substrate solution is used when the enzyme to be measured is an alkaline enzyme ( Bacillus sp. KSM-366).
, KSM-P15-derived enzyme) has a final concentration of 50 mM glycine-NaOH
When the buffer (pH 10.0) is an acidic enzyme (commercially available pectinase), a final concentration of 10 mM citrate buffer (pH 5.0) is used.
0) was used. After the reaction, 1 ml of a DNS solution (3,5-dinitrosalicylic acid 0.5%, NaOH 1.6%, potassium sodium tartrate 30%) was added, and the mixture was boiled for 5 minutes to develop the reducing sugar. Cool on ice immediately after color development (about 15 minutes), 4
ml of ion-exchanged water was added, mixed, and centrifuged (3000
rpm, 10 min) and the absorbance at 535 nm of the supernatant was measured. The amount of reducing sugars generated was calculated from the simultaneously prepared calibration curve of D-galacturonic acid, and the enzyme activity value was determined. The enzyme activity was defined as 1 U, which is the amount of enzyme that produces 1 μmol of galacturonic acid equivalent reducing sugar per minute.

2. Method for measuring protopectinase activity 1.9 ml of a substrate solution (final concentration 50 mM Tris-HCl buffer / solution) so that the final concentration of cotton thread in the reaction system becomes 2% (w / v).
0.1 ml of an enzyme solution having a final concentration of 0.4 mg / ml was added to the mixture (pH 8.0), and the mixture was reacted at 30 ° C. for 1 hour. The supernatant obtained by centrifuging the reaction solution (3000 rpm, 5 minutes, 4 ° C.) 0.2
3 ml of ice-cold concentrated sulfuric acid (96%) was added to 5 ml and mixed.
Further, 0.25 ml of a carbazole solution (0.2% carbazole / 100% ethanol) was added and mixed.
In a hot water bath for 20 minutes. After water cooling for 20 minutes, the absorbance at 525 nm was measured. The amount of released pectin was calculated from the calibration curve of D-galacturonic acid prepared simultaneously. From this value, the amount of pectin released from 1 g of cotton was calculated and defined as the cotton pectin release force at pH 8.0. Cotton pectin is protopectin, and the enzyme having a cotton pectin releasing power is an enzyme having protopectinase activity. In addition, as a cotton yarn as a substrate used in the present measurement method, a yarn having a pectin content of 1.5 to 2.5 mg / g cotton by an ammonium oxalate extraction method is used. Ammonium oxalate extraction is a method in which shredded cotton is added to a 0.5% ammonium oxalate solution to a concentration of 1% (w / v) to perform an extraction operation, and the amount of pectin extracted from cotton fibers is determined by a carbazole sulfate method. The way to do it. The extraction and quantitative operation was performed according to the method described in Shizuoka Prefectural Hamamatsu Industrial Technology Center Research Report No. 4 P17-22 (1994). In the present invention, Kanebo Catan yarn 30th or 40th is used.

3. Enzymes Used and Enzyme Activities As enzymes having pectinase activity used in the experiments, sucrase N (Sankyo), pectinase tanabe (Tanabe Seiyaku Co., Ltd.), pectolyase (Kikkoman)
And enzymes that have both protopectinase activity
Protopectinase A derived from Bacillus sp. KSM-366 strain and protopectinase B derived from Bacillus sp. KSM-P15 strain were used. In addition, protopectinase A and B
Is obtained by culturing the Bacillus sp. KSM-366 strain and the Bacillus sp. KSM-P15 strain in a 0.8% nutrient broth containing 0.5% pectin and 0.5% sodium carbonate, respectively, for a total of 72 hours. The liquid was centrifuged to remove the cells, and the resulting supernatant was subjected to ultrafiltration (molecular weight cut off 600
0) and concentrated by freeze-drying. Table 1 shows the pectinase activity and protopectinase activity of each enzyme used in the washing test.

[0020]

[Table 1]

1) Measurement with polygalacturonic acid substrate using Briton-Robinson broad buffer. However, * indicates that the activity cannot be measured in the same buffer, so the measurement was performed with glycine-NaOH buffer. 2) Protopectinases A and B are glycine-NaOH buffer (pH 10.0), other enzymes are citrate buffer (pH
Measured in 5.0). 3) Measured with Tris-HCl buffer (pH 8.0).

4. Cleaning Test Method An artificial mud-contaminated cloth was prepared by attaching Kanuma Akadama clay to a cotton knitted cloth. A detergent having the following composition is dissolved in 4 ° DH hard water (71.2 mg CaCO ₃ / l) to a concentration to be used, 1 L of a detergent solution is prepared and transferred to a stainless steel beaker for tergotometer. Five artificially stained cloths were added to the detergent solution, and 100
Wash by stirring at 20 ° C. for 10 minutes at r / min. After rinsing under running water, it was iron-pressed and subjected to reflectance measurement. The reflectance of the original cloth of the stained cloth and the reflectance of the stained cloth before and after washing were measured by a self-recording colorimeter (Shimadzu Corporation), and the washing rate (%) was calculated by the following equation.

[0023]

(Equation 1)

5. Composition of used detergent The composition of the used detergent is shown below.

[0025]

[Table 2]

LAS: straight-chain alkyl (C _12-14 ) sodium benzenesulfonate (liquid detergent is compounded in acid form) AS: dodecyl alcohol sulfate sodium AE-1: polyoxyethylene lauryl ether (average number of moles of EO added: 4) ) AE-2: polyoxyethylene alkyl (C _12-14 ) ether (average number of moles of added EO: 6) AEP: polyoxyethylene polyoxypropylene lauryl ether (average number of moles of EO added: 8, average number of moles of PO added: 3) AES : Polyoxyethylene alkyl (C _10-12 ) ether sodium sulfate (EO average addition mole number 2.5) Fatty acid salt: Palm oil-derived fatty acid soda Zeolite: 4A zeolite, average particle size 3 μm Amorphous aluminosilicate: Sodium carbonate: dense grain ash Amorphous silicate: JIS No. 2 sodium silicate crystalline silicic acid : SKS-6 (Clariant, former Hoechst Tokuyama) ground product, average particle size 15 μm AA-MA: Sokaran CP5, acrylic acid-maleic acid copolymer (BASF) PEG: polyethylene glycol, average molecular weight 8, 00
0 Enzyme: Sabinase 12.0 TW (protease), ribolase 100T (lipase), Termamyl 60T (amylase) (the above enzymes are manufactured by Novo Nordisk), and KAC500 (cellulase, manufactured by Kao) in a weight ratio of 2: 1: 1: 1 mixture (Note: Liquid detergent contains only 16.0 L of Savinase (protease, Novo Nordisk))

(Method for producing amorphous aluminosilicate) Aqueous sodium aluminate solution (1.55% by weight of Na ₂ O, Al
₂ O ₃ 2.30 wt%, and heated _{Na 2 O / Al 2 O 3} = 1.11 (molar ratio) 1010 g to 40 ° C., with stirring at a rotation speed of 1500 rpm, there, sodium silicate solution ( Na ₂ O 2.75 wt%, SiO ₂ 7.88 wt%, SiO ₂
/ Na ₂ O = 2.96 (molar ratio)), and 1.2 g of calcium chloride dihydrate were dropped and reacted over 20 minutes. After the completion of the dropwise addition, a heat treatment was further performed for 15 minutes, and then the solid was separated by filtration and washed. The obtained wet cake,
After drying at 105 ° C. and 300 torr for 10 hours and pulverizing, an X-ray amorphous aluminosilicate fine powder was obtained. As a result of atomic absorption analysis and plasma emission analysis, the composition of the obtained amorphous aluminosilicate was Al ₂ O ₃ = 21.
1% by weight, SiO ₂ = 57.2% by weight, Na ₂ O = 20.8% by weight, CaO = 0.9% by weight (1.65Na ₂ O · 0.1%).
_{08CaO · Al 2 O 3 · 4.75SiO} 2). The oil absorption capacity was 210 ml / 100 g.

6. Washing Result To the detergents (A) to (C) having the above-mentioned composition, component (a) an enzyme having pectinase activity and component (c) one or more selected from amino acids and sugars were added and washed. The results are shown in Tables 3 to 5. In Tables 3 to 5, the horizontal axis represents the blank and the enzyme exhibiting the component (a) pectinase activity, and the vertical axis represents the blank and the type of one or more additives selected from the component (c) amino acids and sugars, and the weight per detergent. The values in the table where the vertical and horizontal axes intersect were taken as the cleaning rate (%) of the mud-contaminated cloth when each was added. In addition, the amount of the enzyme of component (a) added in the washing test was 80 mg / L.
And

(1) Results of cleaning test with detergent (A) Cleaning conditions: 100 g / min of targotometer, 10 minutes,
20 ° C washing

[0030]

[Table 3]

(2) Results of cleaning test with detergent (a) Cleaning conditions: 100 g / min of targotometer, 10 minutes,
20 ° C washing

[0032]

[Table 4]

(3) Results of washing test with detergent (c) Washing conditions: Targotometer 100 r / min, 10 minutes,
20 ° C washing

[0034]

[Table 5]

As is clear from the results of Tables 3 to 5, the addition of one or more amino acids and sugars to the detergent containing pectinase shows a higher washing effect than when no detergent is added. This effect is observed in enzymes exhibiting pectinase activity, and an enzyme exhibiting protopectinase activity can provide a greater cleaning effect.

──────────────────────────────────────────────────の Continued on the front page (51) Int.Cl. ⁶ Identification symbol FI C11D 1/722 C11D 1/722 3/22 3/22 3/33 3/33 10/02 10/02 (72) Inventor Yomo Shitsu 1334 Minato, Wakayama-shi, Wakayama Pref.

Claims (2)

[Claims] 1. A detergent composition comprising: (a) an enzyme having pectinase activity, (b) a surfactant, and (c) at least one selected from amino acids and sugars. 2. Component (c) is present in an amount of 0.001 to 10 in the total composition.
The cleaning composition according to claim 1, which is contained by weight.