JP3532388B2 - Detergent composition for automatic dishwashers - Google Patents

Description

Detailed Description of the Invention

[0001]

BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a cleaning agent for an automatic dishwasher which does not contain tripolyphosphate and exhibits excellent cleaning power against various stains.

[0002]

2. Description of the Related Art In recent years,
Automatic dishwashers have spread rapidly and have become popular not only for commercial use but also for general households.

In order to remove starchy stains such as cooked rice and pigment stains such as tea shavings, which have been firmly adhered to tableware, α-amylase has been conventionally used as a detergent for automatic dishwashers. Phosphorus-containing detergents containing a starch-degrading enzyme such as and a chlorine-based bleaching agent such as dichloroisocyanuric complex have been mainly used. On the other hand, enzymes, fragrances, dyes and the like are unstable with respect to chlorine bleaching agents, and therefore phosphorus-containing detergents using oxygen bleaching agents instead of chlorine bleaching agents have also been provided (Japanese Patent Application Laid-Open No. 2004-242242). (Sho 60-60198 publication).

However, at the present time when most detergents are phosphorus-free detergents, phosphate-containing detergents may become a social problem from the environmental point of view. Therefore, with the spread of automatic dishwashers, there has been a strong demand for a technology that eliminates phosphorus without lowering the cleaning power for various stains.

[0005]

Means for Solving the Problems As a result of intensive studies to meet such a demand, the present inventors have found that if a specific nonionic surfactant and a specific polyoxypropylene are used in combination, the same performance as a phosphorus-containing detergent is obtained. It was found that a detergent composition having excellent detergency can be obtained, and the present invention was completed.

That is, according to the present invention, a nonionic surfactant (a) represented by the following general formula (1) and / or (2) and a polyoxy compound having an average degree of condensation of oxypropylene groups of 10 to 90 are used. Provided is a detergent composition for an automatic dishwasher, which contains propylene (b). H- (OE) _l- (OP) _m- (OE) _n -OH (1) H- (OP) _p- (OE) _q- (OP) _r -OH (2) (wherein OE is oxyethylene The group, OP, represents an oxypropylene group, and l, m, n, p, q, and r are average addition mole numbers and are each 0.2 to 50. ]

[0007]

BEST MODE FOR CARRYING OUT THE INVENTION The nonionic surfactant which is the component (a) of the present invention is represented by the above general formulas (1) and (2), and the component (a) is contained in the composition. 0.001 to 10% by weight, more preferably 0.005 to 5% by weight
Is. If the content of this component is less than 0.001% by weight, a sufficient cleaning effect cannot be obtained, and if it is more than 10% by weight, the physical properties of the enzyme will be impaired when the enzyme is added as described below. Be done.

The polyoxypropylene which is the component (b) of the present invention has an average degree of condensation of oxypropylene groups of 10 to 90, preferably 30 to 50. Those within this range have excellent detergency. The polyoxypropylene used in the present invention preferably has an average molecular weight of 600 or more and 5000 or less, and particularly preferably 2000 to 4000. In the present invention, such polyoxypropylene is added to the composition in an amount of 0.001
~ 10 wt% is preferably blended, more preferably
It is 0.005 to 5% by weight. If the compounding amount of polyoxypropylene is less than 0.001% by weight, a sufficient cleaning effect cannot be obtained, and if it is more than 10% by weight, the foaming efficiency increases and the cleaning efficiency is impaired.

Further, in the present invention, the component (a) and the component (b)
The weight ratio of the components is (a) / (b) = 1/10 to 10/1, especially 1
It is more preferably / 5 to 5/1 from the viewpoint of detergency. Furthermore, the total amount of component (a) and component (b) in the composition is 0.1
-20% by weight is preferable, and 1.0-10% by weight is particularly preferable.

It is preferable to incorporate an enzyme into the composition of the present invention. The enzyme is selected from the group consisting of amylase, protease, cellulase, lipase, pullulanase, isopullulanase, and isoamylase 1
More than one type of enzyme may be mentioned. The enzyme is present in the composition at 0.1-
It is preferable to add 10% by weight, more preferably 0.2
~ 5% by weight.

The enzyme may be blended based on the activity value. In this case, the activity of each enzyme is measured as follows.

<Lipase> The specific activity of lipase is measured on the basis of hydrolysis of triolein at a constant pH, and it is shown by the activity per 1 g of enzyme. The active unit is “LU / g”, and 1 LU is 30 using polyvinyl alcohol (PVA) as an emulsifier.
It is a value obtained by dividing the number of moles of fatty acid produced by decomposing a fatty acid ester at 0 ° C. and pH 10.5 by the time (min) required for it, that is, the amount of an enzyme producing 1 μmol (micromol) of fatty acid per minute. Specifically, pH 10.
50 mM glycine buffer solution as the buffer solution of 5, the emulsifier in 1000 ml of distilled water, and the PVA with a polymerization degree of 1700
(Manufactured by Katayama Chemical Co., Ltd.) 18 g and PVA having a degree of polymerization of 500
(Wako Pure Chemical Industries, Ltd.) A 2% PVA aqueous solution containing 2 g was prepared, and 10 g of a 2% PVA aqueous solution was used as a substrate emulsion, and 1.0 g of triolein (manufactured by SIGMA) was emulsified for 5 minutes or more with a homogenizer. I used the one. Activity was measured by Y.Kondoh using high performance liquid chromatography.
and S.Takano, Analytical Chemistry, vol.58, pp2
380-2383 (1986). The composition of the reaction solution is shown below. Lipolytic enzyme solution 1.5 ml (enzyme dissolved in 50 mM glycine buffer (pH 10.5)) Substrate emulsion 1.0 ml.

The measuring method for calculating the specific activity is shown below. Preparation of calibration curve: An injection amount of 9.02 mM 1-monoolein (1-MO, SIGMA) was plotted on the horizontal axis and a peak area was plotted on the vertical axis to prepare a calibration curve. Measurement of LU: A constant stirring force was applied to the reaction solution to which the lipolytic enzyme was added, and the mixture was reacted at 30 ° C. for 30 minutes, and then the reaction stop solution [50% ethanol (Wako Pure Chemical Industries, Ltd.), 10%
Sodium dodecyl sulfate (Wako Pure Chemical Industries, Ltd.)] 0.5m
1 was added, and the solvent was removed while purging with a nitrogen gas on a 100 ° C. water bath. 5.0m to this
l of acetone (Wako Pure Chemical Industries, Ltd.) was added, and the mixture was well stirred and filtered. Further, from the chromatographic results obtained by analyzing 30 μl of the filtrate, the respective amounts in 30 μl were obtained from the calibration curve from the peak areas of diolein (DO), monoolein (MO) and glycerin (GLY). Calculation of specific activity value: The specific activity value (P) was determined from the concentration obtained in the following formula. Total amount of fatty acid produced (μmol · micromol) = (DO amount + MO amount × 2 + GLY amount × 3) × 5000 μl / 30 μl × 10 ^-3 [Note: μl is microliter] Therefore, specific activity value P: LU / g = (total fatty acid content: μmol) /
[(Enzyme added amount: g) x (reaction time: min)] The lipase used in the present invention is supplied in the form of granules and the enzyme specific activity determined from the above is 0.1 to 1 g per 1 g.
It is preferable to mix it so as to be 10,000 LU / g.

<Cellulase> The cellulolytic enzyme (cellulase) preferably has an optimum pH of 7 or higher, or a relative activity of 50 or higher when the carboxymethyl cellulose is used as a substrate, or at a pH of 8 or higher. Alkali-active cellulolytic enzymes having an activity of not less than% are preferred. As such a cellulolytic enzyme, cellulase described in JP-A-63-264699 is preferable, and as a producing strain, Bacillus sp. Are preferred, and specifically, Bacillus sp. KSM
-635 strain (FERM BP-1485), KSM-
521 (FERM BP-1570) and KSM-52
2 (FERM BP-1512), KSM-580
(FERM BP-1511), KSM-534 (F
ERM BP-1508), KSM-539 (FER)
MBP-1509), KSM-577 (FERM)
BP-1510), KSM-588 (FERM BP)
-1513), KSM-597 (FERM BP-1)
514) and the like. A method for producing a cellulolytic enzyme from these strains is described in the above-mentioned JP-A-63-26469.
No. 9 publication can be referred to.

In the present invention, the cellulolytic enzyme is
It is supplied in the form of granules, and the CMC degrading activity per 1 g of the following enzyme is determined, and then 0.5 to 10000 U / g / g,
It is preferable that the amount is 1 to 50 U / g. The enzymatic activity of the cellulolytic enzyme is shown by the degrading activity for carboxymethyl cellulose (CMC), and the CMC degrading activity can be measured by the method shown below.

CMC (manufactured by Nippon Paper Industries Co., Ltd .: viscosity 7 to 20)
0.4 ml of 2.5% aqueous solution of cp (1%, 25 ° C., degree of substitution 0.65 to 0.75), 0.2 ml of 0.5 M glycine buffer solution (pH 9.0), and deionized water 0 .3 ml
0.1 ml of enzyme solution was added to the substrate solution consisting of
React for 0 minutes. After the reaction, the reducing sugar is quantified by the 3,5-dinitrosalicylic acid [3,5-Dinitorosalicylic acid (DNS)] method. That is, D to 1.0 ml of reaction solution
NS reagent (sodium hydroxide 1.6%, 3,5-dinitrosalicylic acid 0.5% and potassium sodium tartrate 4
1 ml of a 30% hydrate solution) and added for 5 minutes at 100 ° C
After heat-development with, and after cooling, 4.0 ml of deionized water is added for dilution, and this is colorimetrically determined at a wavelength of 535 nm. The enzyme titer is 1 unit (U) of the amount of enzyme that produces a reducing sugar corresponding to 1 μmol of glucose per minute under the above conditions.
And

<Protease> The protease activity is measured by the Anson-hemoglobin method (Anson.ML.
J. Gen. Physiol. , Vol. 22, p79
(1938)). That is,
The final concentration of urea-modified hemoglobin used as a substrate is 1
After reacting for 10 minutes at a temperature of 25 ° C. and pH 10.5 in a solution prepared to have a concentration of 4.7 mg / ml, trichloroacetic acid was added to the reaction solution so as to have a final concentration of 31.25 mg / ml. , Trichloroacetic acid soluble component is colored with a phenol reagent. The activity per 10 minutes of reaction is determined from a calibration curve in which the color development of 1 mmol of tyrosine is 1 APU, and this is measured by converting the activity per minute. Therefore, in the present invention, 1AP
U refers to the amount of alkaline protease which gives a trichloroacetic acid-soluble component having the same color development as 1 mmol of tyrosine is colored by the phenol reagent in 1 minute. In the present invention, the protease is provided in granular form,
The enzyme activity is mixed in an amount of 0.1 to 30000 APU / g. If the enzyme activity is less than 0.1 APU / g, a preferable detergency cannot be obtained, and if it exceeds 30,000 APU / g, it is not preferable in terms of the balance with other components.

<Amylase and Pullulanase> In the present invention, a starch-degrading enzyme such as amylase, isoamylase, pullulanase, and isopullulanase can be used. Here, pullulanase, isopullulanase and isoamylase are involved in the decomposition of starch like α-amylase and β-amylase, but α-amylase and β-amylase are α-amylose and α-glycans in amylopectin. -1,4 bond is cleaved, while pullulanase and isoamylase are α- of sugar chain in amylopectin.
Isopullulanase is known as an enzyme that selectively cleaves α-1,4 bonds in the vicinity of α-1,6 bonds in sugar chains, i.e., in terms of cleaving branched chains in amylopectin. Different from α-amylase and β-amylase. Further, α-amylase is an endo type that randomly cleaves internal bonds in amylose and amylopectin, whereas β-amylase is an exo type amylase that regularly cleaves from the end group.

The above starch debranching enzyme used in the present invention is obtained from various sources, but is generally derived from fungi. Suitable starch debranching enzymes are pullulanase and isolanase showing amylopectin-6-glucanohydrase activity obtained from bacteria belonging to the genus Klebsiella, bacteria belonging to the genus Bacillus, bacteria belonging to the genus Aspergillus, bacteria belonging to the genus Pseudomonas. They are pullulanase and isoamylase.

Further, the starch debranching enzyme according to the present invention may be a commercially available product. As commercially available pullulanase, "Sprentase" (registered trademark, Amano Pharmaceutical Co., Ltd.), "Promozyme 200L" (registered trademark, Novo Industry Co., Ltd.), and as isoamylase, "isoamylase" (reagent, raw Chemical Industry Co., Ltd., etc.

These starch debranching enzymes are generally supplied in the form of granules, the enzyme activity of which is about 10 ³ to 10 ⁸ units / g. In the present invention, a starch debranching enzyme which exhibits an optimum action in alkaline, particularly at pH 8 to 11, is preferable, and alkaline pullulanase is particularly preferable. The optimum working pH is
It is measured by the method described in JP-A-3-87176. As an alkaline pullulanase, Bacillus sp. KSM-AP1876 (Microtechnology Research Institute No. 10887) can be used.

Starch debranching enzyme is EYCLee and WJ W
helan, "Glycogen and Starch Debranching Enzymes in
the Enzymes "Vol.5 (PDBoyer ed.) pp192-234, Acad
It has been defined as a feature of plant-derived pullulanase (R enzyme) by emicPress, New York. An enzyme that specifically cleaves α-1,6 bond decreases its viscosity when it acts on amylopectin, resulting in iodine coloration. Is increased and the reducing power is increased. They also report that the presence of this enzyme significantly promotes the degradation by β-amylase.

Among the enzymes usable in the present invention, α
-Amylases are conventionally used as detergent enzymes, and they can be used. Suitable α-amylases include Bacillus licheniformis and Bacillus subtili
An enzyme obtained from s., and examples thereof include "Termamyl" (registered trademark, Novo Industry Co., Ltd.), "Maxamil" (registered trademark, Gist Co., Ltd.) and the like. In addition, as β-amylase, an enzyme obtained from bacteria such as Bacillus sp., Soybean, malt and the like can be used, and as a commercial product, “Amano” (registered trademark, Amano Pharmaceutical Co., Ltd.), “multitome” ”
(Registered trademark, Nagase Seikagaku Co., Ltd.) and the like. These enzymes are generally supplied in the form of granules, the enzyme activity of which is about 10 ³ to 10 ⁸ units / g. Particularly in the present invention, alkali α- having an optimum pH in alkalinity
Amylase is preferred. As the alkali α-amylase, the above-mentioned “Termamyl” can be used.

These enzymes include an enzyme (A) selected from pullulanase, isopullulanase and isoamylase,
Enzyme selected from α-amylase and β-amylase
(B), the total amount of (A) and (B) in the composition, usually 0.1 ~
20% by weight, preferably 0.1-15% by weight. In addition, starch debranching enzyme (A), α-amylase or β-
The ratio of amylase (B) is (A) / (B)
= 10/1 to 1/100, preferably 2/1 to 1/50.

When the detergent composition of the present invention is used for washing, the enzyme activity of the combined enzymes (A) and (B) in the washing solution is determined to be DNS (3,5-dinitrosalicylic acid). The detergent composition of the present invention so that the activity value by the method is 10 units / g or more (the amount of enzyme that produces 1 μmol glucose per minute is 1 unit (U)), preferably 100 units / g or more. Is better to use.

The method of measuring the enzyme activity by the DNS method is shown below. This method measures the activity of a combination of enzymes (A) and (B). (1) Substrate: 0.5% by weight potato-derived soluble starch (reagent, Sigma) solution (2) Preparation of substrate solution 1.0 g of potato-derived soluble starch is dissolved in 100 ml of ion-exchanged water. (3) Preparation of sample Add 0.5 ml of the substrate solution to the test tube and put 100 mM Glycine-
Add 0.4 ml of NaOH buffer solution (pH = 10.0) and 0.1 ml of appropriately diluted enzyme solution, and incubate in a constant temperature bath at 50 ° C for 15 minutes.
After completion of the reaction, 1 ml of a DNS solution is added, color is developed in boiling water for exactly 5 minutes, and immediately after color development, the mixture is put in an ice water bath and cooled. After cooling, add 4 ml of deionized water, mix well,
Promptly measure the absorbance at 535 nm. (4) Prepare 0.5 ml of the substrate solution in a blank test tube, and put 100 mM Glycine-
0.4 ml of a NaOH buffer solution (pH = 10.0) and 1 ml of a DNS solution are added thereto, and the color is developed in boiling water for exactly 5 minutes. Immediately after the color development, it is put in an ice-water bath and cooled. After cooling, add 4 ml of deionized water, mix well, and immediately measure the absorbance at 535 nm. (5) Preparation of calibration curve Put 0.5 ml of the substrate solution into a test tube and put 100 mM Glycine-
Add 0.4 ml of NaOH buffer (pH = 10.0), and add 0.1 ml of glucose solution for calibration curve so that the concentration of glucose will be 250-1500 µmol / l. 1 ml of a DNS solution was added thereto, and the color was developed in boiling water for exactly 5 minutes. After cooling, add 4 ml of deionized water,
Mix well and measure the absorbance at 535 nm immediately. The glucose concentration is plotted on the abscissa and the absorbance is plotted on the ordinate to obtain the slope, and the conversion factor (F) is calculated as follows. F = 1 / (slope) × 1/15 × 1 / 0.1 (6) Calculation of activity The enzyme activity is calculated by the following formula. Activity (U / L) = δ absorbance x F x dilution ratio δ absorbance = (absorbance of sample)-(blank absorbance) (7) Preparation of DNS reagent (1 L) 16 g of sodium hydroxide is dissolved in 200 ml of deionized water. To do. To this, 5 g of DNS is gradually added and dissolved.
After the DNS is completely dissolved, 300 g of sodium potassium tartrate is added. After completely dissolving, make up to 100 ml with deionized water.

Further, it is preferable to add a Ca (calcium) scavenger to the composition of the present invention. Examples of Ca scavengers include hydroxymono- or polyvalent carboxylic acids or salts thereof, aminocarboxylic acids having an iminodiacetic acid structure or salts thereof, silicic acid compounds, aluminosilicate compounds, polyacrylic acid salts, acrylic acid / maleic acid copolymers. And at least one Ca scavenger selected from the group consisting of salts of copolymers of maleic acid and olefins. Here, examples of the hydroxy mono- or polycarboxylic acid (salt) include oxalic acid, malonic acid, succinic acid, citric acid, malic acid, glutaric acid, and salts thereof. Examples of the aminocarboxylic acid (salt) having an iminodiacetic acid structure include ethylenediaminetetraacetic acid, nitrilotriacetic acid, and salts thereof. Further, hexametaphosphoric acid, aminotri (methylenesulfonic acid), or the like can be added. The Ca scavenger is preferably incorporated in the composition in an amount of 5 to 85% by weight, more preferably 5 to 20% by weight.

A bleaching agent can be added to the composition of the present invention. Examples of the bleaching agent include oxygen bleaching agents. Examples of the oxygen-based bleaching agent include organic hydrochloric acid such as magnesium monoperoxyphthalate or its salt, alkali metal perborate (monohydrate or tetrahydrate), percarbonate and persilicate. Peroxides that generate hydrogen peroxide in aqueous solution are mentioned. Of these hydrogen peroxide adducts, preferred are sodium perborate and sodium percarbonate. The bleaching agent is preferably used in combination with a bleaching activator which reacts with hydrogen peroxide in water to generate an organic peracid. Tetraacetylethylenediamine (TAED), tetraacetylglycoluril (TAGU), glucose pentaacetic acid (GPA) and xylose tetraacetic acid (XTA) are commonly used as bleach activators. The bleach / bleach activator is used in a weight ratio of 8/1 to 1/1. When the bleaching agent is blended, the blending amount is 0.1 to 20% by weight, preferably 1 to 10% by weight in the composition. When the content of the bleaching agent is less than 0.1% by weight, the bleaching effect is weak, and when it is more than 20% by weight, other components such as enzymes are inhibited. When a bleach activator is added, its amount is 0.1 to 30% by weight, preferably 1 to 15% by weight, particularly preferably 2 to 10% by weight in the composition. If the content of the bleach activator is less than 0.1% by weight, no improvement in the cleaning effect is observed, and if it exceeds 30% by weight, no further effect is obtained and it tends to be economically disadvantageous. It is in.

The composition of the present invention may contain an alkaline agent or a surfactant other than the nonionic surfactant represented by the general formula (I).

Examples of the alkaline agent include sodium hydrogen carbonate, sodium carbonate, borax, sodium silicate and the like. Since sodium silicate has an effect of preventing metal corrosion, it is desirable to use it together with other alkaline agents.
In particular, sodium hydrogen carbonate and sodium silicate (SiO ₂ / Na
O ratio is 1/1 to 4/1, preferably 2/1 to 2.5 / 1)
Weight ratio of 35 / 1-2 / 1, or sodium and sodium silicate carbonate (SiO ₂ / Na ₂ O ratio of 1 / 1-4 / 1, preferably 2/1 to 2.5 / 1) weight ratio of 35 Most preferably, it is used in combination of / 1-2 / 1. In the present invention, the blending amount of the alkaline agent is preferably 5 to 85% by weight, more preferably 20 to 70% by weight. 0.05-1% by weight of alkaline agent
It is desirable to adjust the concentration of the detergent solution to pH 9.0-11.0 before use.

Examples of the surfactants used in the present invention other than the nonionic surfactants represented by the general formulas (1) and / or (2) include general surfactants. Ionic surfactants are preferred.

The nonionic surfactant is not particularly limited, but polyoxyethylene monoalkyl or monoalkenyl ethers, polyoxyethylene alkylphenyl ethers, polyoxypropylene monoalkyl or monoalkenyl ethers, polyoxybutylene. Monoalkyl or monoalkenyl ethers, alkylene oxide-added monoalkyl or monoalkenyl group-containing nonionic surfactant mixtures, sucrose fatty acid esters,
One or more selected from aliphatic alkanolamides, fatty acid glycerin monoesters, amine oxides, ethylene oxide condensation type surfactants and alkyl glycosides are preferable. More specific examples of such a nonionic surfactant include the following (1) to (10).

(1) Polyoxyethylene monoalkyl or monoalkenyl ethers, wherein the alkyl group or alkenyl group has an average carbon number of 10 to 20, and the ethylene oxide addition mole number is 1 to 30 moles on average. some stuff.

(2) Polyoxyethylene alkyl phenyl ethers having an alkyl group having an average carbon number of 6 to 12
And the average number of moles of ethylene oxide added is 1 to
What is 25 moles.

(3) Polyoxypropylene monoalkyl or monoalkenyl ethers, wherein the alkyl group or alkenyl group has an average carbon number of 10 to 20, and the propylene oxide addition mole number is 1 to 20 moles on average. some stuff.

(4) Polyoxybutylene monoalkyl or monoalkenyl ethers, wherein the alkyl group or alkenyl group has an average carbon number of 10 to 20, and the butylene oxide addition mole number is 1 to 20 moles on average. some stuff.

(5) Having an alkyl group or an alkenyl group only at one end, ethylene oxide and propylene oxide (molar ratio: 0.1 / 9.9 to 9.9 / 0.1) or ethylene oxide and butylene oxide (molar ratio: 0.1 / 9.
9 to 9.9 /0.1) is added to the nonionic surfactant mixture, wherein the alkyl group or the alkenyl group has an average carbon number of 10 to 20, and the average number of moles of alkylene oxide added per molecule is What is 1 to 30 mol.

(6) A higher fatty acid alkanolamide represented by the following general formula (A) or an alkylene oxide adduct thereof.

[0039]

[Chemical 1]

[Wherein, R ³ is an alkyl group or an alkenyl group having 10 to 20 carbon atoms, R ⁴ and R ⁵ are the same or different and are H or CH ₃ , p is a number of 1 to 3, and q is Is a number from 0 to 3. (7) Sucrose fatty acid esters having a fatty acid moiety with an average carbon number of 10 to 20.

(8) Fatty acid glycerin monoesters having an average carbon number of the fatty acid portion of 10 to 20.

(9) Amine oxides. For example, carbon number 1
Alkyl or alkenyl amine oxides having up to 24 straight or branched chain alkyl or alkenyl groups are mentioned. More preferable amine oxides include alkylamine oxides represented by the following general formula (B).

[0043]

[Chemical 2]

In the above general formula (B), R ⁶ has 8 carbon atoms.
Although it is an alkyl group or an alkenyl group having 24 carbon atoms, an alkyl group having 12 to 18 carbon atoms is particularly preferable. R ⁷ and R ⁸ have 1 to 1 carbon atoms
Although it is an alkyl group having 3 carbon atoms, a methyl group having 1 carbon atom is particularly preferable.

(10) Alkyl polysaccharides. For example, an alkyl polysaccharide represented by the following general formula (C). R ⁹ (OR ¹⁰ ) _x G _y (C) [wherein, R ⁹ represents a linear or branched alkyl group having 8 to 18 carbon atoms, an alkenyl group, or an alkylphenyl group, and R ¹⁰ represents the number of carbon atoms. It represents an alkylene group of 2 to 4 and G is a residue derived from a reducing sugar having 5 to 6 carbon atoms. x
(Average value) is 0 to 5, and y (average value) is 1 to 5. The average value of x in the general formula (C) is 0 to 5, and the water solubility and crystallinity of the present cleaning composition can be adjusted by changing this value. That is, the larger the value of x, the higher the water solubility and the lower the crystallinity. The value of x is preferably 0 to 2, particularly preferably 0.
Is. On the other hand, y is
That is, when a sugar chain of two or more sugars is used as a hydrophilic group, the sugar chain has a bond mode of 1-2, 1-3, 1-4, 1-6 bond, and further α-, β-pyranoside bond or furanoside. It is possible to include binding and any mixture having these mixed binding modalities. The average value of y in the general formula (C) is 1 to 5, preferably 1 to 1.5, more preferably
It is 1.1 to 1.4. The measured value of y is based on the proton NMR method. Further, R ⁹ in the formula is preferably an alkyl group having 10 to 14 carbon atoms from the viewpoint of solubility and detergency. Further, R ¹⁰ is preferably an alkylene group having 2 to 3 carbon atoms from the viewpoint of water solubility. Furthermore, the structure of G is determined by the raw material of monosaccharides or disaccharides or more. As the raw material of G, monosaccharides include glucose, fructose, galactose, xylose, mannose, lyxose, arabinose, and a mixture thereof. Examples of disaccharides and above include maltose, xylobiose, isomaltose, cellobiose, gentibiose, lactose, sucrose,
Examples thereof include nigerose, turanose, raffinose, gentianose, melezitose, and mixtures thereof. Among these, preferred raw materials are glucose and fructose as monosaccharides, and maltose and sucrose as disaccharides and above because of their availability and cost. Of these, glucose is particularly preferable from the viewpoint of easy availability. Furthermore, 1 mol adduct of pentaerythritol isostearyl glycidyl ether, 1 mol adduct of sorbitol isostearyl glycidyl ether, 1 mol adduct of mannitol 2-octyldodecyl glycidyl ether, 1 mol of methylglucoside isostearyl glycidyl ether. Molar adduct, 1 molar adduct of diglycerin / isostearyl glycidyl ether,
Nonionic surfactants having at least one long-chain branched alkyl group or alkenyl group and at least three hydroxyl groups in one molecule such as phytantriol can be mentioned.

Among these nonionic surfactants (1)
, (5), (6), (9) and (10) are preferable, and further (5),
(9) and (10) are particularly preferable.

In the present invention, the content of the other surfactant is 0.0010 to 10% by weight, preferably 1 to 10% by weight. When the content of the surfactant is less than 1% by weight, a sufficient cleaning effect cannot be obtained, and when the content of the surfactant is more than 10% by weight, the degree of freedom of the composition is narrowed, which is not preferable.

To the detergent composition for an automatic dishwashing machine of the present invention, 0.1 to 5% by weight of a fatty acid having a hydrocarbon chain length of about 8 to 18 is added to prevent corrosion of copper. It is also effective to add triazole or the like.

The automatic dishwashing detergent composition of the present invention can generally be prepared in the form of a dry powdered product. That is, it can also be prepared by dry mixing the powdery or granular components according to conventional manufacturing techniques and then spraying a liquid component (such as a nonionic surfactant) onto the mixture.
It is not particularly limited.

The cleaning agent for an automatic dishwasher of the present invention is
As described above, by using a surfactant as an essential component without using a strong alkali, it has sufficient detergency, and is mainly used in household automatic dishwashers where it is difficult to use a strong alkali. Used against.

[0051]

As described above, the cleaning agent for an automatic dishwashing machine of the present invention is the basic performance of the cleaning agent for an automatic dishwashing machine such as oil,
It is a highly practical detergent for automatic dishwashers which has sufficient detergency for starch and at the same time does not contain tripolyphosphate and has the ability to remove dye stains deposited on dishes, that is, bleaching performance.

[0052]

EXAMPLES The present invention will be described in more detail with reference to examples, but the present invention is not limited to these examples. In the following examples, "%" means "% by weight".

Examples 1 to 8 and Comparative Examples 1 to 4 The compositions shown in Table 1 below were prepared and washed under the following washing conditions.
The following detergency test was conducted and evaluated. The results are shown in Table 1.

<Washing conditions> Washing machine used: fully automatic dishwasher (model of Matsushita Electric Co., Ltd.)
NP-820) A cleaning solution is sprayed from a rotating nozzle to wash dishes placed on the upper surface of the spray track. Washing temperature: Gradually raise the temperature from 5 ° C to 55 ° C. Washing water; Water detergent concentration of hardness 3.5 ° DH; 0.2% Washing time; Washing 20 minutes-20 minutes rinse Circulating water volume during washing: Approximately 2.5 liters.

<Evaluation of Detergency> [Measuring Method of Detergency of Cooked Rice] (Preparation of Contaminated Dish) Soft cooked cooked rice is left at room temperature for 30 minutes, and 3 g is spread on a magnetic dish having a diameter of 25 cm and applied. Then, 6 sheets that had been air-dried at room temperature for one day were washed.

(Evaluation Method of Detergency of Cooked Rice Stain) The area of the blue portion (P) of the residue of cooked rice on the dish after washing was determined by the photograph determination by the color reaction of iodine, and each area was determined from the initial contaminated area (S). The dish cleaning rate was calculated by the following formula. Furthermore,
The cleaning rates of the 6 dishes were averaged to obtain the average cleaning rate (%). Cleaning rate of one plate (%) = [(SP) / S] × 100

[0057]

[Equation 1]

[Method for Measuring Complex Detergent Detergency] (Preparation of Contamination Dish) 10 g of margarine (“Neosoft” manufactured by Snow Brand Co., Ltd.) was added to 100 g of white sauce (canned product of Heinz), and heated to 60 ° C. and mixed well. It is treated as a composite stain. 5 g of the above composite stain is applied to each magnetic dish having a diameter of 25 cm, and baked at 120 ° C. for 15 minutes. This was left to stand for one day and then washed. (Washing test and detergency evaluation method) Five contaminated dishes were placed in a washing machine and washed under the above washing conditions. The dishes after washing were judged one by one according to the following criteria, and the washing evaluation point was calculated by the following formula. Completely washed 5 points Slightly soiled residue 4 points A small amount of soiled residue is observed Approximately 1/4 of the 3 point dish has soiled residue Approximately 1/2 of the 2 point dish has soiled residue Residual residue 1 point No washing at all 0 point Cleaning evaluation point = [sum of evaluation points of each contaminated dish] x 4

[0059]

[Table 1]

(Note) * 1: Pluronic L61 (manufactured by Asahi Denka Co., Ltd.) * 2: Compound represented by the general formula (2) (p = 5, q = 35, r
= 5) * 3: Polypropylene glycol, average molecular weight about 3000, average condensation degree about 50 (diol type, Wako Pure Chemical Industries, Ltd.) * 4: Polypropylene glycol, average molecular weight about 1000, average condensation degree about 17 (diol type, sum) Koujunyaku Co., Ltd.) * 5: Termamyl 60T (Novo Nordisk Bio Industry Co., Ltd.) * 6: Sabinase 12.0T (Novo Nordisk Bio Industry Co., Ltd.) * 7: Softanol EP7085 (Nippon Shokubai Co., Ltd.) * 8 : TAED (tetraacetylethylenediamine)

Continuation of front page (51) Int.Cl. ⁷ identification code FI C11D 3/386 C11D 3/386 3/395 3/395 10/02 10/02 (56) References JP-A-60-18591 (JP, A) ) JP-A-4-72397 (JP, A) JP-A-4-72398 (JP, A) Special Table 7-505669 (JP, A) (58) Fields investigated (Int.Cl. ⁷ , DB name) C11D 1/00-19/00

Claims (14)

(57) [Claims] 1. A nonionic surfactant (a) represented by the following general formula (1) and / or (2) in an amount of 0.001 to 10% by weight and an average degree of condensation of oxypropylene groups of 17 to 90. A detergent composition for an automatic dishwasher, which comprises 0.001 to 10% by weight of oxypropylene (b). H- (OE) l- (OP) m- (OE) n-OH (1) H- (OP) p- (OE) q- (OP) r-OH (2) (wherein OE is oxyethylene The group, OP, represents an oxypropylene group, and l, m, n, p, q, and r are average addition mole numbers and are each 0.2 to 50. ] 2. The weight ratio of component (a) to component (b) is (a) /
The cleaning composition for an automatic dishwasher according to claim 1, wherein (b) = 1/10 to 10/1. 3. The cleaning composition for an automatic dishwasher according to claim 1 or 2, which contains the component (a) and the component (b) in a total amount of 0.1 to 20% by weight. 4. The method according to claim 1, which contains an enzyme.
A cleaning composition for an automatic dishwasher according to the item. 5. An enzyme containing 0.1 to 10% by weight.
A detergent composition for an automatic dishwasher as described. 6. The washing for an automatic dishwasher according to claim 4 or 5, wherein the enzyme is one or more kinds of enzymes selected from the group consisting of amylase, protease, cellulase, lipase, pullulanase, isopropylulanase, and isoamylase. Agent composition. 7. The cleaning composition for an automatic dishwasher according to claim 1, which contains a Ca scavenger. 8. The cleaning composition for an automatic dishwasher according to claim 7, which contains a Ca scavenger in an amount of 5 to 85% by weight. 9. A Ca scavenger is a hydroxymono- or polyvalent carboxylic acid or its salt, an aminocarboxylic acid having an iminodiacetic acid structure or its salt, a silicic acid compound, an aluminosilicate compound, a polyacrylic acid salt, acrylic acid / maleic acid. The detergent composition for an automatic dishwasher according to claim 7 or 8, which is one or more Ca scavengers selected from the group consisting of salts of acid copolymers and salts of copolymers of maleic acid and olefins. 10. The detergent composition for an automatic dishwasher according to claim 1, which contains 0.1 to 20% by weight of a bleaching agent. 11. The detergent composition for an automatic dishwasher according to claim 10, wherein the bleaching agent is one or two bleaching agents selected from sodium percarbonate and sodium perborate. 12. The detergent composition for an automatic dishwasher according to claim 10, which contains 0.1 to 30% by weight of a bleach activator which reacts with hydrogen peroxide in water to generate an organic peracid. 13. The detergent composition for an automatic dishwasher according to claim 1, which contains 0.1 to 30% by weight of an alkaline agent. 14. The detergent composition for an automatic dishwasher according to claim 1, which contains a surfactant other than the component (a).