JP2907938B2 - Cosmetic base - Google Patents

Description

Description: TECHNICAL FIELD The present invention relates to a cosmetic base containing an acylated keratin peptide having a cysteic acid residue in the peptide chain or a salt thereof.

[Conventional technology]

BACKGROUND ART It has been known that a keratin peptide obtained by hydrolyzing keratin is useful as a compounding agent for hair cosmetics and skin cosmetics. This is because the keratin peptide has a chemical structure similar to that of hair, and is adsorbed on the hair by its amino group or carboxyl group to protect the hair and soften the hair, and to make the hair smooth, Gives moisture, luster, etc., to the skin, gives moist feeling, moist, smoothness, luster, etc., and is a derivative of keratin, a natural protein, with less irritation to skin and mucous membranes, This is because the security is high.

The present inventors have repeated studies to impart more useful properties to the keratin peptide without impairing the properties of the keratin peptide as described above. The present invention has developed an acylated keratin peptide having a surface activity that is not available in keratin peptides, and has already filed a patent application (JP-A-59-101499).

[Problems to be solved by the invention]

However, for those involved in cosmetic research,
There is a demand to further enhance the usefulness of the acylated keratin peptide while maintaining the properties of the acylated keratin peptide, and to blend it into hair cosmetics and skin cosmetics to obtain higher quality cosmetics.

[Means for solving the problem]

The present invention provides a method for oxidizing a keratin peptide obtained by hydrolyzing keratin, or acylating a keratin-oxidized peptide obtained by hydrolyzing a keratin oxide obtained by oxidizing keratin; An acylated product of a keratin oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (1) or a salt thereof is obtained to meet the above demand.

General formula (I): (Wherein, R ₁ is an alkyl group having 7 to 21 carbon atoms, 7 to 21 carbon atoms)
A hydrocarbon group alkenyl group or alicyclic structure, R ₂
Is the side chain of the constituent amino acids of the keratin peptide. M ₁ and M ₂ are hydrogen, an alkali metal such as lithium, sodium, potassium, ammonium or monoethanolamine, diethanolamine, triethanolamine, 2-
Amino-2-methyl propane, 2-amino-2-methyl-1,3 is an onium of an organic amine, such as propanediol, M ₁ and M ₂ may be the also well or different in the same. m and n are from 0 to 24, a is from 1 to 2.5, and m +
n + a is 2 to 25) The acylated product of the keratin oxidized peptide represented by the above general formula (I) or a salt thereof is contained in the peptide chain. Since the compound has a sulfonic acid residue represented by the formula (I), the acylated product of keratin peptide or a salt thereof (hereinafter, an acylated product of keratin peptide of the prior application or a salt thereof) described in JP-A-59-101449 Has stronger washing power and emulsifying power, and exhibits good surface activity even under acidic conditions.

That is, when the acylated keratin peptide represented by the general formula (I) of the present invention or its salt is compared with the acylated keratin peptide of the prior invention or its salt, the acylated keratin peptide of the prior invention is obtained. Alternatively, the salt thereof is a carboxylic acid type anion activator having a surfactant activity by acylating a carboxyl group at a peptide terminal, whereas the keratin oxidation represented by the general formula (I) of the present invention is used. Since the acylated peptide or a salt thereof has a cysteic acid residue in the peptide chain based on the oxidation of the keratin peptide or keratin, in addition to the surfactant activity by acylating the carboxyl group at the peptide terminal, the cysteic acid residue The keratin peptide of the invention of the prior application, because the group acts as a sulfonic acid type anion activator in which the group is a strong acid Compared to acylated or a salt thereof, a stronger cleaning power and a emulsifying power, also exhibit good surface activity in pH5~6 following acidic pH region.

In addition, the acylated keratin peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) of the present invention or its salt is similar to the keratin peptide acylated product of the prior application or its salt, Protects hair, softens hair, gives hair smoothness, moisture, luster, etc., improves hair combability, and gives skin a moist feeling, moisturizing, smoothness, gloss, etc. It has the property of giving. Naturally, since it is derived from keratin, which is a natural protein, it has low irritation to skin and mucous membranes and is excellent in safety.

As described above, the acylation of the keratin oxidized peptide represented by the general formula (I) or a salt thereof hydrolyzes the keratin oxidized peptide obtained by oxidizing the keratin peptide or the keratin oxide obtained by oxidizing the keratin. The resulting keratin-oxidized peptide is obtained by acylating the keratin-oxidized peptide, and may be obtained together with a peptide having no cysteic acid residue in the peptide chain due to a reduction in molecular weight due to hydrolysis.

That is, all keratins have cystine, and when cystine is oxidized, it becomes cysteic acid. When wool is used as a keratin source and it is completely oxidized, it is calculated to be about one cysteine per 10 amino acids. Since it has an acid residue, the molecular weight is reduced by hydrolysis, the average molecular weight is about 1,200 or less, and the number of amino acids in a keratin oxidized peptide having a number of 10 or less, some of which does not have a cysteic acid residue in the peptide chain, When it is acylated,
Some peptides do not have a cysteic acid residue in the peptide chain. As a result, an acylated product having a cysteic acid residue in the peptide chain or a salt thereof and an acylated product having no cysteic acid residue in the peptide chain or a salt thereof are obtained in a mixed state.

However, such an acylated keratin peptide having no cysteic acid residue in the peptide chain or a salt thereof also has reduced detergency and emulsifying power as compared with those having a cysteic acid residue. It acts on the skin in the same way as the acylated keratin peptide of the invention of the prior application or a salt thereof, and imparts desirable properties to hair and skin. It is not necessary to isolate those having a residue, and they can be used as a cosmetic base in a state where those having no cysteic acid residue are mixed in the peptide chain.

In obtaining an acylated product of the keratin-oxidized peptide represented by the general formula (I) or a salt thereof, examples of the starting material keratin include animal hair such as wool, hair, feathers, and the like.
Blades, hooves, claws, horns and the like are used.

The hydrolysis of keratin to obtain keratin peptides is carried out with acids, alkalis or enzymes.

In acid hydrolysis, hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid,
Inorganic acids such as hydrobromic acid and organic acids such as acetic acid and formic acid are used.

For alkali hydrolysis, sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, lithium carbonate and the like are used.

In the case of hydrolysis by an enzyme, an acidic proteolytic enzyme such as pepsin, proctase A and proctase B, a neutral proteolytic enzyme such as papain, bromelain, thermolysin, trypsin, pronase and chymotrypsin are used. Bacterial neutral or alkaline proteases such as subtilisin and staphylococcal protease can also be used.
When the enzyme is used, the enzyme can be used in the form of cells containing the bacterial proteolytic enzyme, or membranes or granules on which the enzyme or the cell containing the enzyme are immobilized. In addition, hydrolysis with an acid and hydrolysis with an enzyme can be used in combination, such as hydrolysis with an enzyme after partial hydrolysis with an acid.

Details of the hydrolysis of keratin to obtain a keratin peptide are, for example, as follows.

(1) Hydrolysis by Acid As described above, the acid includes inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid and hydrobromic acid, and organic acids such as acetic acid and formic acid. Further, a mixture of hydrochloric acid and acetic acid may be used. These are generally 5 to 85% (hereinafter referred to as "%" indicating the concentration,
Those without a standard indication are used in a concentration of (% by weight), but it is desirable that the hydrolysis reaction is always at pH 4 or less. The reaction temperature is preferably from 40 to 100 ° C, but can be raised to 160 ° C under pressure.
The reaction time is preferably 2 to 24 hours. The reaction product is neutralized with an alkali such as sodium hydroxide, potassium hydroxide, sodium carbonate, ammonia, etc., and can be used as it is, but the reaction product or the neutralized product is subjected to gel filtration, ion exchange resin, ultrafiltration, dialysis, It can also be used after purification by electrodialysis or the like.

(2) Hydrolysis by alkali As the alkali, an inorganic alkali such as sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, and lithium carbonate is used as described above. These are generally 1-20%
Is appropriate. If the alkali is used more than necessary, the hue of the peptide solution becomes brown to black, which is not preferable. The reaction is preferably carried out at a temperature of room temperature to 100 ° C. for 30 minutes to 24 hours. Care must be taken not to raise the temperature excessively or to lengthen the reaction time. Hydrolysis with alkali has the advantage that the keratin hydrolyzate elutes with the progress of the reaction, and the progress of the reaction is visible. The reaction may be terminated when the reaction mixture becomes a homogeneous solution. After the reaction, it is preferable to neutralize with the above-mentioned acid, or purify by gel filtration, ion exchange resin, ultrafiltration, dialysis, electrodialysis and the like.

(3) Enzymatic hydrolysis As described above, the enzymes include acid proteases such as pepsin, proctase A and proctase B,
Neutral or alkaline proteases such as papain, bromelain, thermolysin, trypsin, pronase and chymotrypsin are used. Bacterial proteolytic enzymes such as subtilisin and staphylococcal protease can also be used. The pH at the time of hydrolysis is preferably adjusted to a range of pH 1 to 4 for acidic protease such as pepsin, and to a range of pH 4 to 10 for neutral or alkaline protease such as papain. In general, it is convenient to appropriately adjust the pH with a buffer such as an acetic acid / sodium acetate buffer or a phosphate buffer, or by adding an acid or an alkali. The reaction temperature is preferably from 30 to 45 ° C, and the reaction time is generally from 3 to 45 ° C.
24 hours is appropriate.

In the hydrolysis reaction using an enzyme, the molecular weight of the keratin peptide is greatly affected by the amount of the enzyme used, the reaction temperature, and the reaction time. Therefore, in order to obtain a keratin peptide having a target molecular weight, for each of the conditions of the amount of the enzyme used, the reaction temperature, and the reaction time, the molecular weight distribution of the obtained keratin peptide is examined by a gel furnace method, and the optimum conditions are determined. Is preferred.

Keratin peptides obtained by enzymatic hydrolysis are very suitable for use in cosmetics because they have a narrower molecular weight distribution and less free amino acids than keratin peptides obtained by acid or alkali hydrolysis. It is.

As the keratin peptide obtained by hydrolysis with an acid, alkali or enzyme as described above, m in Formula (I) is 0 to 24, n is 0 to 24, and a is 1-2.
5. It is appropriate that n + m + a is 2 to 25 (this m
+ N + a of 2 to 25 corresponds to an average molecular weight of about 200 to about 3,000 of the peptide).

That is, when the above-mentioned m + n + a is smaller than 2, the amino acid portion is increased, the detergency and the emulsifying power of the acylated product are reduced, and the irritation and permeability to the skin are also increased. This is because the water solubility is reduced. The keratin peptides obtained by hydrolysis of keratin are obtained in the form of a mixture having different molecular weights, so that the above m, n and a are represented by average values.

R ₂ in the general formula (I) is a side chain of a constituent amino acid of the keratin peptide. As the amino acid, for example, alanine, glycine, valine, leucine,
Examples include isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, lysine, asparagine, aspartic acid, glutamine, glutamic acid, cystine, cysteine, cysteic acid, tryptophan, and the like.

An example of the composition ratio of these amino acids is shown in Table 1. In addition, asparagine and glutamine are not shown in Table 1 because they were converted to aspartic acid and glutamic acid, respectively, during the hydrolysis carried out prior to analysis (completely hydrolyzed with 6N hydrochloric acid in a conventional manner). is there. In other words, aspartic acid and glutamic acid in Table 1 include those present as aspamine and glutamine in the keratin peptides. In addition, since cystine has two amino groups and two carboxyl groups, the composition ratio in Table 1 is shown as half cystine.

As oxidizing agents for oxidizing keratin peptides,
Those that oxidize the disulfide bond of cystine as selectively and strongly as possible are preferred, for example, hydrogen peroxide,
Sodium bromate, potassium bromate, sodium perborate, peracetic acid, formic acid, and the like are used. In particular, hydrogen peroxide is most suitable for oxidizing keratin peptides because of its good selectivity and easy post-treatment after oxidation. Oxidation of this keratin peptide is carried out, for example, at pH 3
~ 10, room temperature ~ 70 ° C, for 1 ~ 48 hours.

In addition, when keratin is oxidized and then hydrolyzed, keratin oxidation is performed in substantially the same manner as in the case of the above-described keratin peptide oxidation, and keratin oxide hydrolysis is also performed in the keratin hydrolysis. It is performed in much the same way as in the case.

The most common method for acylating the keratin-oxidized peptide obtained as described above includes the Schotten-Baumann reaction.

This reaction is a reaction in which an acid chloride derivative of a higher fatty acid to be condensed is added to an aqueous solution of a keratin oxidized peptide with stirring under alkaline conditions of pH 8 to 10. According to this reaction, hydrochloric acid is generated as a by-product, and the pH decreases.Therefore, it is necessary to maintain the pH at 8 to 10 by adding an alkali such as sodium hydroxide or potassium hydroxide while adding acid chloride. . The reaction time is 1 to 6 hours, and the reaction temperature is 0 to 60 ° C, preferably 20 to 50 ° C.

As the higher fatty acid side component, acid halides of higher fatty acids such as Br and I can be used in addition to the above acid chlorides. However, acid chloride is the most common.

In addition to the commonly used fatty acids having 7 to 21 carbon atoms, in addition to the method using the above-mentioned acid halide, keratin oxidized peptides and higher fatty acids or lower alcohol esters such as methyl esters and ethyl esters under high temperature and high pressure of 150 to 200 ° C. Can be employed, and dehydration condensation or dealcoholization condensation can be employed. However, since the method is a high temperature treatment, the product is colored and is not always preferable.

Furthermore, using the reagents used for peptide synthesis,
For example, a method in which a higher fatty acid is converted into a carboxyl group-active derivative such as N-oxysuccinimide ester or N-phthalimide ester and then reacted with a keratin oxidized peptide can be adopted. The sex is not high.

In any case, the obtained acylated product is preferably released into an aqueous solution of a strong acid such as hydrochloric acid or sulfuric acid, and the free material is collected as a floating precipitate, washed and purified, and then left free or in the free state. It is dissolved in water or a solvent such as alcohol or propylene glycol to form a solution of the desired concentration (10 to 60%, especially 20 to 40%), or dried to a powder. Served for use.

The hydrocarbon moiety in the acyl group of the higher fatty acid used in the acylation of the keratin oxidized peptide has 7 to 7 carbon atoms as shown by R ₁ in the general formula (I).
An alkyl group having 21 carbon atoms, an alkenyl group having 7 to 21 carbon atoms (the alkyl group or the alkenyl group may be linear or branched), or an alicyclic hydrocarbon group; Specific examples thereof in the state of, for example, caprylic acid, capric acid, lauric acid, myristic acid, palmitic acid, stearic acid, arachinic acid, behenic acid, isopalmitic acid, isomyristic acid, isostearic acid, undecylenic acid, Oleic acid, myristoleic acid, elaidic acid, erucic acid, linoleic acid, linoleic acid, arachidonic acid, coconut oil fatty acid, bovine fatty acid, resin acid (abietic acid) and the like.

As the acylated product of the keratin oxidized peptide or the salt thereof obtained as described above, cysteic acid is used in an amount of 5 to 18%.
It is preferable that the content is included in the range of mol%. When the amount of cysteic acid is less than 5 mol%, the surface activity and solubility under acidic conditions decrease, and when the amount of cysteic acid exceeds 18 mol%, the surface activity and emulsification improve. But,
At the same time, the skin irritation becomes stronger, and the inherent characteristics of low irritation and high safety are impaired.

If the residual amount of cystine in the acylated keratin peptide or its salt is large, the pH stability decreases and a low cloud point cannot be obtained, so oxidation should be carried out so that the residual amount of cystine is reduced as much as possible. Preferably, the content of half cystine is set to 2 mol% or less.

Since the acylated keratin peptide represented by the general formula (I) of the present invention or a salt thereof has a cysteic acid residue in the peptide chain, the keratin oxidized peptide is more washed than the conventional acylated keratin peptide or the salt thereof. Strong emulsifying power, good emulsification stability, and exhibits good surface activity even at acidic pH. The acylated keratin oxidized peptide represented by the general formula (I) of the present invention or a salt thereof protects the hair, softens the hair, imparts smoothness, moisture and luster to the hair, and combs the hair. To be good. And it gives the skin a moist feeling, moisture, smoothness, luster and the like. Moreover, it is safe with little irritation to the skin and mucous membranes.

An acylated keratin-oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or a salt thereof is used in place of a conventional cosmetic compound or in combination with a conventional cosmetic compound. It is blended in various cosmetics. However, an acylated keratin oxidized peptide having a cysteic acid residue in the peptide chain represented by the above general formula (I) or a keratin peptide serving as a base for a salt thereof is obtained in a state of a mixture of different molecular weights. Include those having a low molecular weight and no cysteic acid residue. Therefore, when formulated into cosmetics, keratin-oxidized peptides having a cysteic acid residue in the peptide chain represented by the above general formula (I) The acylated product or a salt thereof is used in a state of a mixture with an acylated product of a keratin oxidized peptide having no cysteic acid residue in the peptide chain or a salt thereof.

An acylated product of a keratin-oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or a salt thereof, and an acylated product of a keratin-oxidized peptide having no cysteic acid residue in the peptide chain or a salt thereof Examples of cosmetics in which a mixture of the following are blended include shampoo, hair rinse, split ends coat, first agent for permanent wave, second agent for permanent wave, hair cream, aerosol type foam, hair conditioner, set lotion, hair color , Hair Bleach, Hair Treatment, Hair Treatment Rinse, Liquid Hair Styling (Lotion), Hair Pack, Hair Tonic, Hair Restoration, Hair Restoration Hair Cosmetics, Lotion, After Shave Lotion, Shaving Foam, Burnishing Cream, Cream Various cosmetics such as ging cream, emollient cream, cold cream, moisture cream, hand cream, face cream, etc., hair remover, face pack, milky lotion, body shampoo, various soaps, makeup products, sunscreen products, etc. it can. It is preferable that the compounding amount is about 0.1 to 20% in terms of pure content in the cosmetic composition.

Further, in the cosmetic, an acylated product of a keratin oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or a salt thereof and an acylated keratin oxidized peptide having no cysteic acid residue in the peptide chain Examples of the components that can be used in combination with the mixture with the compound or a salt thereof include alkyl sulfates such as ammonium lauryl sulfate, ethanolamine lauryl sulfate, sodium lauryl sulfate, and triethanolamine lauryl sulfate; and polyoxyethylene (2EO) laurilute sulfate. Triethanolamine (EO is ethylene oxide, the value before EO indicates the number of moles of ethylene oxide added), polyoxyethylene (3EO) alkyl (a mixture of one or more of 11 to 15 carbon atoms, ) Polyoxyethylene such as sodium ether sulfate Alkyl ether sulfates,
Alkylbenzene sulfonates such as sodium laurylbenzenesulfonate and triethanolamine laurylbenzenesulfonate; polyoxyethylene alkyl ether acetates such as sodium polyoxyethylene (3EO) tridecyl ether acetate; coconut oil fatty acid sarcosine sodium; lauroyl sarcosine tri Ethanolamine, sodium lauroylmethyl-β-alanine, sodium lauroyl-L-glutamate, lauroyl-L
-Triethanolamine glutamate, coconut oil fatty acid-
N-acyl amino acid salts such as sodium L-glutamate, coconut oil fatty acid-triethanolamine L-glutamate, sodium coconut fatty acid methyltaurine, sodium lauroylmethyltaurine, sodium ether sulfate alkanesulfonate, hydrogenated coconut fatty acid sodium glycerin sulfate, Disodium undecylenoylamidosulfosuccinate, sodium octylphenoxydiethoxyethylsulfonate, disodium amideamidosulfosuccinate, dioctylsodium sulfosuccinate, disodium lauryl sulfosuccinate, polyoxyethylene alkyl (C12-15) ether Phosphoric acid (8-10EO) sodium polyoxyethylene oleyl ether phosphate, sodium polyoxyethylene cetyl ether phosphate, polio Shi ethylenesulfonyl-lauryl disodium succinate, sodium polyoxyethylene lauryl ether phosphate, sodium lauryl sulfoacetate,
Anionic surfactants such as sodium tetradecene sulfonate, distearyl dimethyl ammonium chloride, dipolyoxyethylene oleyl methyl ammonium chloride,
Cationic surfactants such as stearyldimethylbenzylammonium chloride, stearyltrimethylammonium chloride, cetyltrimethylammonium chloride, tri (polyoxyethylene) stearylammonium chloride, polyoxypropylenemethyldiethylammonium chloride, myristyldimethylbenzylammonium chloride, lauryltrimethylammonium chloride Agent, 2-alkyl-N-carboxymethyl-N-hydroxyethylimidazolinium betaine, sodium undecylhydroxyethylimidazolium betaine, undecyl-N-hydroxyethyl-N-carboxymethylimidazolinium betaine,
Stearyl dihydroxyethyl betaine, stearyl dimethylamino acetate betaine, coconut oil alkyl betaine,
Palm oil fatty acid amidopropyl betaine, coconut oil alkyl N-carboxyethyl-N-hydroxyethylimidazolinium betaine sodium, coconut oil alkyl N-carboxyethoxyethyl-N-carboxyethylimidazolinium disodium hydroxide, coconut alkyl N
Amphoteric surfactants such as -carboxymethoxyethyl-N-carboxymethylimidazolinium disodium lauryl sulfate, N-coconut fatty acid acyl L-arginine ethyl / DL-pyrrolidone carboxylate, polyoxyethylene alkyl (having 12 to 12 carbon atoms) 14) Ether (7EO), polyoxyethylene octyl phenyl ether, polyoxyethylene oleyl ether, polyoxyethylene glyceryl oleate, polyoxyethylene stearyl ether,
Polyoxyethylene cetyl ether, polyoxyethylene cetyl stearyl diether, polyoxyethylene sorbitol lanolin (40EO), polyoxyethylene nonyl phenyl ether, polyoxyethylene polyoxypropylene cetyl ether, polyoxyethylene polyoxypropylene decyl tetradecyl ether Nonionic surfactants such as polyoxyethylene lanolin, polyoxyethylene lanolin alcohol, and polyoxypropylene stearyl ether; cations such as cationized cellulose, cationized hydroxyethylcellulose, poly (diallyldimethylammonium chloride), polyvinylpyridine and polyethyleneimine Synthetic polymer such as amphoteric polymer, amphoteric polymer, anionic polymer, diethanolate isostearate Luamide, undecylenic acid monoethanolamide, oleic acid diethanolamide, bovine fatty acid monoethanolamide, hardened bovine fatty acid diethanolamide, stearic acid diethanolamide, stearic acid diethylaminoethylamide, stearic acid monoethanolamide, myristic acid diethanolamide, coconut fatty acid Thickeners such as ethanolamide, coconut oil fatty acid diethanolamide, lauric acid isopropanolamide, lauric acid ethanolamide, lauric acid diethanolamide, lanolin fatty acid diethanolamide, waxes, paraffins, fatty acid esters, glycerides, oils and fats such as animal and vegetable oils, Animal and plant extracts, polysaccharides or derivatives thereof, linear or cyclic methylpolysiloxane, methylphenylpolysiloxane, diphenyl Silicon oil such as tyl polysiloxane polyethylene glycol copolymer, dimethyl polysiloxane polypropylene copolymer, amino-modified silicone oil, quaternary ammonium-modified silicone oil, propylene glycol, 1,3-butylene glycol, ethylene glycol, glycerin, polyethylene Wetting agents such as glycol, lower alcohols such as ethanol, methanol, propyl alcohol and isopropyl alcohol, L-aspartic acid, sodium L-aspartate, DL-alanine, L-arginine, glycine, L-glutamic acid, L-cysteine, L
-Amino acids such as threonine.

An acylated product of a keratin-oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or a salt thereof, and an acylated product of a keratin-oxidized peptide having no cysteic acid residue in the peptide chain or A mixture with a salt thereof is usually used to obtain an acylated product of a keratin oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or a salt thereof when obtaining a salt thereof. It is obtained in a state where an acylated keratin-oxidized peptide having no group or a salt thereof is mixed. That is, the average molecular weight of the keratin peptide is about 1,20
When the average molecular weight of the keratin peptide is smaller than 0, the ratio of the acylated keratin-oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or the salt thereof is high. The ratio of acylated keratin peptide having no cysteic acid residue in the peptide chain or its salt increases.
However, if it can be obtained only by an acylated product of a keratin oxidation peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or a salt thereof, keratin oxidation without a cysteic acid residue in the peptide chain can be obtained. An acylated peptide or a salt thereof may be mixed.

〔Example〕

Next, the present invention will be described more specifically with reference to examples. However, the present invention is not limited only to the examples. Prior to Examples, Production Examples of keratin oxidized peptides are shown as Reference Examples.

Reference Example 1 In a three-necked flask, 450 g of 35% hydrochloric acid was added to 500 g of wool,
Hydrolysis was carried out at 80 ° C. with stirring for 18 hours. After hydrolysis,
The reaction mixture was filtered, and the filtrate was neutralized with 1,400 ml of a weakly basic anion exchange resin Diaion WA20 (trade name, manufactured by Mitsubishi Kasei Co., Ltd.), and then concentrated and filtered to remove the ion exchange resin, and the concentration was 40%. A keratin peptide aqueous solution was obtained.

The molecular weight of the keratin peptide thus obtained was measured by gel filtration, and was found to have an average molecular weight of 400. When the amount of cystine in the obtained keratin peptide was measured by an amino acid automatic analyzer [JLC-300, manufactured by JEOL Ltd.], the amount of cystine was 8.7 mol% of all amino acids.

For 200 g of a 40% aqueous solution of the obtained keratin peptide,
20 g of a 35% hydrogen peroxide solution was added to adjust the pH to 7, followed by treatment at room temperature for 3 days for oxidation. After oxidation, a 20% aqueous sodium hydroxide solution was added to adjust the pH to 9, and the mixture was stirred at 40 ° C. for 3 hours to decompose the remaining hydrogen peroxide solution, and then the concentration was adjusted to obtain a 40% keratin oxide peptide aqueous solution. Was.

The average molecular weight of the keratin-oxidized peptide thus obtained is 300, the amount of cysteic acid in the obtained keratin-oxidized peptide is 8.5 mol%, and the amount of cystine is
0.2 mol%. The measurement of the average molecular weight is based on the gel filtration method, and the measurement of the cysteic acid amount and the cystine amount is based on the amino acid analysis, and the same applies to the following.

Reference Example 2 800 g of 32% hydrochloric acid was added to 500 g of crushed wool, and the mixture was stirred at 25 ° C. for 72 hours to perform hydrolysis. After hydrolysis, add 20
% Sodium hydroxide aqueous solution was added to adjust the pH to 5. Add 0.5 g of protein hydrolase papain to this reaction solution,
Hydrolysis was performed for 24 hours while stirring at 42 ° C. During the hydrolysis, add a 20% aqueous sodium hydroxide solution to adjust the pH of the reaction solution.
Was kept at 5. After hydrolysis with papain, the reaction mixture is
Heating at 1 ° C. for 1 hour inactivated papain. 20 in the reaction solution
After adding sodium hydroxide solution to adjust the pH to 6, the mixture was filtered, and the filtrate was subjected to electrodialysis using an electrodialyzer described below, desalted, and the concentration was adjusted to obtain an aqueous solution of a keratin peptide having a concentration of 25%. The electrodialyzer used was as follows.

Model: DO-Cb (manufactured by Teijin Engineering Co., Ltd.) Membrane name: Ceremion CMV and AMV (manufactured by Asahi Glass Co., Ltd.) Membrane dimensions: 18 cm × 12 cm Number of built-in films: 10 vs. voltage: 30 V Anolyte: sodium sulfate aqueous solution (anhydrous Catholyte: sodium sulfate aqueous solution (about 5% as anhydrous sodium sulfate) The average molecular weight of the keratin peptide thus obtained is 1,200, and the amount of cystine in the keratin peptide is 7.2 mol in all amino acids. %Met.

For 200 g of a 25% aqueous solution of the obtained keratin peptide,
10 g of a 35% hydrogen peroxide solution was added, and the mixture was oxidized and the concentration was adjusted in the same manner as in Reference Example 1 to obtain a 40% keratin oxidized peptide aqueous solution.

The average molecular weight of the obtained keratin oxidized peptide is 700
The amount of cysteic acid was 6.0 mol% and the amount of cystine was 1.1 mol%.

Reference Example 3 750 g of 30% hydrochloric acid was added to 500 g of crushed wool, and the mixture was stirred at 20 ° C. for 72 hours to perform hydrolysis. After hydrolysis, ammonia gas was neutralized to pH 7 by passing ammonia gas through the reaction solution while cooling and stirring the reaction solution. Next, the reaction solution was filtered, desalted by the same electrodialysis as in Reference Example 2, and concentrated to obtain a 30% keratin peptide aqueous solution.

The average molecular weight of the keratin peptide thus obtained was 3,800, and the amount of cystine in the keratin peptide was 12.2 mol% of all amino acids.

For 200 g of a 30% aqueous solution of the obtained keratin peptide,
10 g of 35% aqueous hydrogen peroxide was added, and the mixture was oxidized and the concentration was adjusted in the same manner as in Reference Example 1 to obtain a 30% keratin oxidized peptide aqueous solution.

The average molecular weight of the keratin-oxidized peptide thus obtained was 2,000, the amount of cysteic acid was 12.0 mol%, and the amount of cystine was 0.2 mol%.

Example 1 147 g of myristic acid chloride (0.9 equivalents of keratin oxidized peptide) was added dropwise to 500 g of the 40% aqueous solution of keratin oxidized peptide obtained in Reference Example 1 over 2 hours while stirring at 45 ° C at a constant temperature. During this time, the pH was maintained at 9 by appropriately adding a 20% aqueous sodium hydroxide solution. After stirring at 45 ° C. for 1 hour, the temperature was raised to 50 ° C. and stirred for 1 hour to complete the reaction.

The reaction mixture is released into a 5% aqueous sulfuric acid solution 5 and the resulting acylated product is suspended in a free form (the carboxylic acid of the peptide is not a salt -COOH), and then washed with water.
After washing with water, the mixture was neutralized by adding a 30% aqueous potassium hydroxide solution to obtain 1,020 g of a 30% aqueous solution of a potassium salt of a condensate of a keratin oxidized peptide and myristic acid. The yield was 85%.

In addition, confirmation of the obtained product was performed as follows.

Amino nitrogen was determined by a Van Slake method on a 30% aqueous solution of the obtained product, and was found to be 0.094 mg / g. Reference Example 1 used as raw material
The 40% aqueous solution of keratin-oxidized peptide obtained in 1) was 18.5 mg / g of amino nitrogen, and it was found that most of the amino groups in the product were acylated.

Then, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after replacing with nitrogen gas, the test tube was sealed and kept at 110 ° C for 2 hours.
Hydrolysis was performed for 4 hours. After opening and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated and extracted with an aqueous layer and an ether layer using a separating funnel. The aqueous layer was used as a sample and subjected to amino acid analysis. As a result, it was found that the composition had almost the same composition as the keratin oxidized peptide obtained in Reference Example 1 used as a raw material. The ether layer was subjected to methyl esterification using N-methyl-N-nityroso-p-toluenesulfonamide according to a conventional method, and then subjected to gas chromatography. It turned out to be exactly the same as the methyl ester of the acid.

Based on the above results, Reference Example 1 in which the product was used as a raw material
It was confirmed to be a potassium salt of a condensate of myristic acid at the amino group of the keratin-oxidized peptide obtained in the above. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

The analysis conditions of the gas chromatography of Example 1 and the analysis conditions of the gas chromatography of Examples 2 to 8 to be described later are collectively shown as follows.

Column: DEGS (diethylene glycol succinate) + H
₃ PO ₄ (10: 1), inner diameter 3 mm x length 2 m (Examples 1 to 7 and its raw material) Silicon SE30, inner diameter 3 mm x 2 mm (Example 8 and its raw material) Gas: nitrogen (50 ml / min) Detection: Flame ionization detection method The temperature is shown in each figure. The number of each peak in the figure indicates the peak detection time (minute).

Example 2 Instead of myristic acid chloride in Example 1, coconut oil fatty acid (a mixed fatty acid having 8 to 18 carbon atoms) chloride was used.
0 g (1.0 equivalent of keratin-oxidized peptide) and triethanolamine of coconut oil fatty acid condensate of keratin-oxidized peptide having a concentration of 30% in the same manner as in Example 1 except that triethanolamine was used instead of potassium hydroxide. An amine salt aqueous solution (1,140 g) was obtained. The yield was 90%.

In addition, confirmation of the obtained product was performed as follows.

When an amino nitrogen was determined by a Fan-Slake method for a 30% aqueous solution of the obtained product, 0.054 mg /
g. The 40% aqueous solution of keratin oxidized peptide obtained in Reference Example 1 used as a raw material was 18.5 mg of amino nitrogen.
/ g, and it was found that the amino group was almost acylated in the product.

Then, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after replacing with nitrogen gas, the test tube was sealed and kept at 110 ° C for 2 hours.
Hydrolysis was performed for 4 hours. After opening and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated and extracted with an aqueous layer and an ether layer using a separating funnel. The aqueous layer was used as a sample and subjected to amino acid analysis. As a result, it was found that the composition had almost the same composition as the keratin oxidized peptide obtained in Reference Example 1 used as a raw material. The ether layer was subjected to methyl esterification using N-methyl-N-nitroso-p-toluenesulfonamide in a conventional manner, and then subjected to gas chromatography. It turned out to be of exactly the same composition as the methyl ester of the fatty acid.

Based on the above results, Reference Example 1 in which the product was used as a raw material
Was confirmed to be a triethanolamine salt of a condensate of coconut oil fatty acid (mixed fatty acid having 8 to 18 carbon atoms) in the amino group of the keratin-oxidized peptide obtained in the above. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 3 73 g of palmitic acid chloride (0.95 equivalents of keratin oxidized peptide) was added dropwise to 500 g of the 40% aqueous solution of keratin oxidized peptide obtained in Reference Example 2 over 2 hours while stirring at a constant temperature of 40 ° C. During that time, the pH was maintained at 9 by appropriately adding a 20% aqueous sodium hydroxide solution. After further stirring at 40 ° C. for 1 hour, the temperature was raised to 45 ° C., and stirring was continued for 1 hour to complete the reaction.

The reaction mixture is released into a 5% aqueous sulfuric acid solution 5 to suspend the produced acylated product. After the suspended product is washed with water, it is neutralized by adding 30% aqueous ammonia, and the ammonium salt of a palmitic acid condensate of a keratin oxidized peptide is neutralized. 828 g of a 30% aqueous solution was obtained. The yield was 98%.

In addition, confirmation of the obtained product was performed as follows.

The amino nitrogen of the suspended product (dry residue: 36.87%) of the obtained product before neutralization with ammonia was determined to be 0.083 mg / g by amino-nitrogen by the Van Slake method. The reason why amino nitrogen was measured before neutralization with ammonia water was that the amino group of ammonia was measured after neutralization, so that it could not be used as a sample for measuring amino nitrogen. The 40% aqueous solution of the keratin-oxidized peptide obtained in Reference Example 2 used as a raw material was 7.8 mg / g of amino nitrogen, and it was found that most of the amino groups were acylated in the product.

Then, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after replacing with nitrogen gas, the test tube was sealed and kept at 110 ° C for 2 hours.
Hydrolysis was performed for 4 hours. After opening and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated and extracted with an aqueous layer and an ether layer using a separating funnel. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the keratin-oxidized peptide obtained in Reference Example 2 used as a raw material. When the ether layer was subjected to methyl esterification using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method,
Gas chromatography revealed that the raw material was exactly the same as the methyl ester of palmitic acid, which was treated and methylesterified in the same manner.

From the above results, Reference Example 2 in which the product was used as a raw material
It was confirmed that it was an ammonium salt of a condensate of palmitic acid at the amino group of the keratin-oxidized peptide obtained in the above. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 4 15.2 g of undecylenic chloride (1.0 equivalent of keratin oxidized peptide) was added dropwise to 500 g of the 30% aqueous solution of keratin oxidized peptide obtained in Reference Example 3 over 2 hours while stirring at a constant temperature of 30 ° C. During this time, the pH was maintained at 9 by appropriately adding a 20% aqueous sodium hydroxide solution. After stirring at 30 ° C. for 1 hour, the temperature was raised to 40 ° C. and stirred for 1 hour to complete the reaction.

The reaction mixture is released into a 5% aqueous sulfuric acid solution 5 and the resulting acylated product is suspended in a free form (the carboxylic acid of the peptide is not a salt -COOH), and then washed with water.
After washing with water, the mixture was neutralized by adding a 30% aqueous potassium hydroxide solution to obtain 558 g of a 30% aqueous solution of a potassium salt of undecylenic acid condensate of keratin oxidized peptide. The yield was 97%.

In addition, confirmation of the obtained product was performed as follows.

Amino nitrogen was determined by a Fan-Slake method for a 30% aqueous solution of the obtained product.
g. The 30% aqueous solution of the keratin oxidized peptide obtained in Reference Example 3 used as a raw material was 2.1 mg of amino nitrogen /
g, and it was found that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 4N methanesulfonic acid was added thereto, and after replacing with nitrogen gas, the test tube was sealed and hydrolyzed at 110 ° C. for 12 hours. The container was opened, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separating funnel, and extracted. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the keratin oxidized peptide obtained in Reference Example 3 used as a raw material. The ether layer was washed with N-methyl-N
-Nitroso-p-toluenesulfonamide was subjected to methyl esterification and then subjected to gas chromatography, which was found to be exactly the same as the untreated methyl ester of undecylenic acid, which was similarly treated and methylesterified. found.

Based on the above results, Reference Example 3 in which the product was used as a raw material
It was confirmed to be a potassium salt of a condensate of undecylenic acid in the amino group of the keratin-oxidized peptide obtained in the above. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 5 180 g of isostearic acid chloride (0.9 equivalent of keratin oxidized peptide) was added to 500 g of the 40% aqueous solution of keratin oxidized peptide obtained in Reference Example 1 while stirring at 45 ° C. under constant temperature.
It was dropped over time. During this time, the pH was maintained at 9 by appropriately adding a 20% aqueous sodium hydroxide solution. After stirring at 45 ° C. for 1 hour, the temperature was raised to 50 ° C., and stirring was continued for 1 hour to complete the reaction.

The reaction mixture was released into a 5% aqueous sulfuric acid solution 5, the acylated product was suspended in free form, and the suspended product was washed with water and neutralized with 2-amino-2-methyl-1,3-propanediol. , Ethyl alcohol, and the 2-amino-
1,460 g of a 25% aqueous solution of 2-methyl-1,3-propanediol salt in ethyl alcohol was obtained. The concentration of ethyl alcohol is 50%. The yield was 87%.

In addition, confirmation of the obtained product was performed as follows.

Float (neutral residue 4) of the obtained product before neutralization with 2-amino-2-methyl-1,3-propanediol
6.31%), the amino nitrogen was determined by the Van Slake method and found to be 0.043 mg / g. In addition, 2
The amino nitrogen was measured before neutralization with -amino-2-methyl-1,3-propanediol because 2-amino-2-methyl-1,3-propanediol was used after neutralization. This is because the amino group of the above cannot be used as a sample for measuring amino nitrogen. The 40% aqueous solution of the keratin oxidized peptide obtained in Reference Example 1 used as a raw material was 18.5 mg / g of amino nitrogen, and it was found that most of the amino groups were acylated in the product.

Then, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after purging with nitrogen gas, the tube was sealed, and the tube was placed at 110 ° C for 2 hours.
Hydrolysis was performed for 4 hours. After opening and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated and extracted with an aqueous layer and an ether layer using a separating funnel. The aqueous layer was used as a sample and subjected to amino acid analysis. As a result, it was found that the composition had almost the same composition as the keratin oxidized peptide obtained in Reference Example 1 used as a raw material. The ether layer was subjected to methyl esterification using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method, and then subjected to gas chromatography. Was found to be exactly the same as the methyl ester.

Based on the above results, Reference Example 1 in which the product was used as a raw material
2-amino-2-methyl-1, a condensate of isostearic acid at the amino group of the keratin-oxidized peptide obtained in
It was confirmed to be a 3-propanediol salt. The results of amino acid analysis are shown in Table 2 and the results of gas chromatography are shown in FIG.

Example 6 Instead of isostearic acid chloride in Example 5, 179 g of oleic acid chloride (of keratin oxidized peptide)
Oleic acid condensation of keratin oxidized peptide in the same manner as in Example 5 except that 0.9 equivalent) was used, sodium hydroxide was used in place of 2-amino-2-methyl-1,3-propanediol, and ethyl alcohol was used. Thing sodium salt 30
941 g of a 1% aqueous solution was obtained. The yield was 85%.

In addition, confirmation of the obtained product was performed as follows.

Amino nitrogen was determined by a Fan-Slake method for a 30% aqueous solution of the obtained product.
g. The 40% aqueous solution of keratin oxidized peptide obtained in Reference Example 1 used as a raw material was 18.5 mg of amino nitrogen.
/ g, indicating that most of the amino groups were acylated in the product.

Next, a small amount of the product was placed in a test tube, 4N methanesulfonic acid was added thereto, and after replacing with nitrogen gas, the test tube was sealed and hydrolyzed at 110 ° C. for 12 hours. The container was opened, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separating funnel, and extracted. The aqueous layer was used as a sample and subjected to amino acid analysis. As a result, it was found that the composition had almost the same composition as the keratin oxidized peptide obtained in Reference Example 1 used as a raw material. The ether layer was washed with N-methyl-N
-Nitroso-p-toluenesulfonamide was subjected to methyl esterification and then subjected to gas chromatography, and it was found that the raw material was the same as the methyl ester of oleic acid, which was similarly treated and methyl esterified. found.

Based on the above results, Reference Example 1 in which the product was used as a raw material
It was confirmed to be a sodium salt of a condensate of oleic acid at the amino group of the keratin-oxidized peptide obtained in the above. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 7 65 g of coconut oil fatty acid chloride (1.0 equivalent of keratin oxidized peptide) was added dropwise to 500 g of the 40% aqueous solution of keratin oxidized peptide obtained in Reference Example 2 over 2 hours while stirring at a constant temperature of 40 ° C. During that time, a pH of 9 was maintained by appropriately adding a 20% aqueous potassium hydroxide solution. After further stirring at 40 ° C. for 1 hour, the temperature was raised to 45 ° C., and stirring was continued for 1 hour to complete the reaction.

The reaction mixture is released into a 5% aqueous sulfuric acid solution 5 and the resulting acylated product is suspended in a free form. The suspended product is washed with water, and then dissolved by adding propylene glycol to form a cocoin oil fatty acid condensate of keratin-oxidized peptide. 960 g of a propylene glycol aqueous solution was obtained. The concentration of propylene glycol is 40%. The yield was 97%.

 Confirmation of the obtained product was performed as follows.

Amino nitrogen was determined by the van Slake method using a 25% aqueous propylene glycol solution of the obtained product, and found to be 0.034 mg / g. The 40% aqueous solution of the keratin-oxidized peptide obtained in Reference Example 2 used as a raw material was 7.8 mg / g of amino nitrogen, and it was found that most of the amino groups were acylated in the product.

Then, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after replacing with nitrogen gas, the test tube was sealed and kept at 110 ° C for 2 hours.
Hydrolysis was performed for 4 hours. After opening and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated and extracted with an aqueous layer and an ether layer using a separating funnel. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the keratin-oxidized peptide obtained in Reference Example 2 used as a raw material. The ether layer was subjected to methyl esterification using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method, and then subjected to gas chromatography. It turned out to be of exactly the same composition as the methyl ester of the fatty acid.

From the above results, Reference Example 2 in which the product was used as a raw material
It was confirmed to be a condensate of coconut oil fatty acid at the amino group of the keratin-oxidized peptide obtained in the above. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 8 The procedure of Example 1 was repeated, except that 190 g (0.9 equivalents of keratin-oxidized peptide) of resin acid (a rosin-based abietic acid as a main component) chloride was used instead of myristic acid chloride in Example 1. 804 g of an aqueous potassium salt solution of a resin acid condensate of keratin oxidized peptide having a concentration of 40% was obtained. The yield was 84%.

In addition, confirmation of the obtained product was performed as follows.

When an amino nitrogen was obtained by a van Slake method for a 40% aqueous solution of the obtained product, 0.106 mg /
g. The 40% aqueous solution of keratin oxidized peptide obtained in Reference Example 1 used as a raw material was 18.5 mg of amino nitrogen.
/ g, indicating that most of the amino groups were acylated in the product.

Then, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after replacing with nitrogen gas, the test tube was sealed and kept at 110 ° C for 2 hours.
Hydrolysis was performed for 4 hours. After opening and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated and extracted with an aqueous layer and an ether layer using a separating funnel. The aqueous layer was used as a sample and subjected to amino acid analysis. As a result, it was found that the composition had almost the same composition as the keratin oxidized peptide obtained in Reference Example 1 used as a raw material. When the ether layer was methyl-esterified using N-methyl-N-nitroso-p-toluenesulfonamide according to a conventional method, it was treated in the same manner and had the same composition as the methyl ester of the resin acid of the raw material. It turned out to be.

Based on the above results, Reference Example 1 in which the product was used as a raw material
It was confirmed that it was a potassium salt of a condensate of resin acid at the amino group of the keratin oxidized peptide obtained in the above. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Comparative Example 1 The keratin peptide in Reference Example 1 (average molecular weight 40
(0, cystine amount: 8.7 mol%) was oxidized without oxidation in the same manner as in Example 1 to obtain a potassium salt of a condensate of a keratin peptide and myristic acid. The results of amino acid analysis of this product are shown in Table 2.

Comparative Example 2 The keratin peptide (average molecular weight 1,20
(0, cystine amount: 7.2 mol%) without oxidation to give an ammonium salt of a keratin peptide condensate of palmitic acid in the same manner as in Example 3. The results of amino acid analysis of this product are shown in Table 2.

Comparative Example 3 The keratin peptide in Reference Example 4 (average molecular weight: 3,80
0, a cystine amount of 12.2 mol%) was oxidized without oxidation to obtain a potassium salt of a condensate of undecylenic acid of a keratin peptide. The results of amino acid analysis of this product are shown in Table 2.

Table 2 below summarizes the results of amino acid analysis of the acylated keratin peptide or its salt obtained in Examples 1 to 8 and the acylated keratin peptide or its salt obtained in Comparative Examples 1 to 3. Shown in

Next, application examples of the present invention will be described.

Application Example 1 A shampoo having the following composition containing the potassium salt of the myristic acid condensate of the keratin oxidized peptide obtained in Example 1 was prepared, and this was designated as Example 1 of the present invention. In addition,
If the component concentration is not added in parentheses (parenthesis) after each substance name, the compounding amount is converted to a pure component. The amounts of the components are all based on weight%. These are the same in the following.

Potassium salt of myristic acid condensate of keratin oxidized peptide of Example 1 (30%) 15.0 2-Alkyl-carboxymethyl-N-hydroxyethylimidazolium betaine (30%) 15.0 Coconut oil fatty acid sodium methyltaurine (30%) 5.0 Palm oil fatty acid diethanolamide 2.5 Cationized cellulose 0.4 Mixture of paraoxybenzoic acid ester and phenoxyethanol (Secept, Seiwa Chemical Co., Ltd.) 0.5 Olive oil 0.8 Perfume Appropriate amount Sterilized ion-exchange water Adjust to a total of 100.0 Malic acid Adjust to pH6 A shampoo having the same composition was prepared except that the same amount of the potassium salt of the myristic acid condensate of the keratin peptide obtained in Comparative Example 1 was used instead of the potassium salt of the myristic acid condensate of the keratin oxidized peptide of Example 1. This was designated as Comparative Product 1.

The shampoo of this embodiment product 1 and comparative product 1 was used by 10 female panelists, and the shampoo was easily foamed, the fineness of the foam, the detergency, the smoothness of the hair after shampooing,
The gloss and combability were compared. Table 3 shows the results. The results are shown by the number of people who answered that the product 1 was better, the number of people who answered that the comparative product 1 was better, and the number of people who said that they could not say either.

As shown in Table 3, the shampoo of Example 1 in which the potassium salt of the myristic acid condensate of the keratin peptide in Example 1 was blended, the potassium salt of the myristic acid condensate of the keratin peptide in Comparative Example 1 was blended. Compared with the shampoo of the comparative product 1, the shampoo was clearly superior in foaming, fineness of foam and detergency. In addition, the effect of improving the smoothness, gloss, combability of hair after hair washing,
Example 1 was superior, and no deterioration in properties due to oxidation was observed.

Application Example 2 A shampoo having the following composition containing an ammonium salt of a palmitic acid condensate of a keratin oxidized peptide obtained in Example 3 was prepared, and this was designated as Example 2 of the present invention.

Ammonium salt of palmitic acid condensate of keratinylated peptide of Example 3 (30%) 20.0 Sodium N-lauroyl-L-glutamate 5.0 Coconut oil fatty acid sodium methyltaurine (30%) 12.0 Diethylaminoethylamide stearate 0.4 Diethanolamide laurate 2.5 Stearyldimethylbenzylammonium chloride (25
%) 0.4 Dimethyl siloxane, methyl (polyoxyethylene) siloxane, methyl (polyoxypropylene) siloxane copolymer (silicone SH374 manufactured by Toray Silicon Co., Ltd.)
9) 0.2 octamethylcyclotetrasiloxane 0.2 pyroctone olamine 0.5 polyoxyethylene (20) nonylphenyl ether
5 Mixture of paraoxybenzoate and phenoxyethanol (Secept, Seiwa Kasei Co., Ltd.) 0.2 Caisson CG (preservative, Rohm and Haas Japan Co., Ltd.) 0.1 Aminopropylethyldimethylammonium fatty acid lanolin ethyl sulfate (Cation LQ, Sanyo Chemical Co., Ltd.) 0.5 Perfume Appropriate amount Sterilized ion-exchanged water Total 100.0 Further, instead of the ammonium salt of the keratin-oxidized peptide palmitate condensate of Example 3 in the shampoo, the ammonium salt of the keratin peptide palmitate condensate of Comparative Example 2 was used. Example 2 except that the same amount of salt was mixed
Prepare a shampoo of the same composition as in
And

The shampoos of Example 2 and Comparative 2 were used by 10 female panelists and evaluated in the same manner as in Application Example 1. Table 4 shows the results.

As shown in Table 4, the shampoo of Example 2 in which the ammonium salt of the keratin peptide condensate of palmitic acid of Example 3 was blended, the ammonium salt of the palmitic acid condensate of the keratin peptide in Comparative Example 2 was blended. Compared to the shampoo of Comparative product 2, the shampoo is easier to foam,
The fineness of the foam and the detergency were clearly excellent.

Application Example 3 A shampoo having the following composition containing a potassium salt of an undecylenic acid condensate of a keratin oxidized peptide obtained in Example 4 was prepared, and this was designated as Example product 3 of the present invention.

Potassium salt of undecylenic acid condensate of keratin oxidized peptide of Example 4 (30%) 35.0 Coconut fatty acid amidopropyldimethylaminoacetic acid betaine (30%) 1.5 Cetyltrimethylammonium chloride 0.25 Polyoxyethylene lauroyl ethanolamide disodium sulfosuccinate 4.0 Coconut fatty acid diethanolamide 1.2 Diethanolamide laurate 0.8 Diethylaminoethylamide stearate 0.2 Dimethylpolysiloxane (SH200 manufactured by Toray Silicon Co., Ltd.)
−500cs) 0.2 Polyoxyethylene (120) methyl glucosidediolate 0.5 Cationic cellulose (Leoguard ML manufactured by Lion)
P) 0.3 Ethylene glycol monostearate 0.6 Mixture of p-hydroxybenzoic acid ester and phenoxyethanol (Secept, manufactured by Seiwa Kasei Co., Ltd.) 0.5 Fragrance Appropriate amount EDTA-2Na 0.1 Sterile ion-exchanged water Total 100 Also, Example 4 in the above shampoo A shampoo having the same composition as in Example 3 was prepared except that the same amount of the potassium salt of the keratin peptide undecylenic acid condensate of Comparative Example 3 was used instead of the potassium salt of the keratin oxidized peptide undecylenic acid condensate. This was designated as Comparative Product 3.

The shampoos of Working Example 3 and Comparative Product 3 were used by 10 female panelists, and evaluated in the same manner as in Application Example 1. Table 5 shows the results.

As shown in Table 5, the shampoo of Example 3 containing the potassium salt of the undecylenic acid condensate of the keratin oxidized peptide of Example 4 was compounded with the potassium salt of the undecylenic acid condensate of the keratin peptide of Comparative Example 3. Compared to the shampoo of the comparative product 3, the shampoo was clearly superior in foaming, fineness of foam, and detergency.

Application Example 4 A hair rinse having the following composition was prepared by mixing a triethanolamine salt of a coconut fatty acid condensate of a keratin oxidized peptide obtained in Example 2, and this was used as a product 4 of the present invention.
And

Triethanolamine salt of coconut oil fatty acid condensate of keratin oxidized peptide of Example 2 (30%) 4.5 Trimethyl quaternary ammonium derived collagen polypeptide (30%) (Promois W-42Q manufactured by Seiwa Kasei Co., Ltd.) 2.0 Hexadecyl Stearate 5.5 Ethylene glycol distearate 4.5 Diethylaminoethylamide stearate 3.8 Diglycerin monoisostearate 3.5 Polyoxyethylene (20) cetyl ether 2.0 Dimethylpolysiloxane (KF96- manufactured by Shin-Etsu Silicone Co., Ltd.)
350cs) 0.1 Cetyl alcohol 1.0 Beef tallow alkyl POE (60) ether myristyl ethylene glycol (Elfacos GT282 manufactured by Lion) 0.3 N-cocoyl-L-arginine ethyl ester / pyrrolidone carboxylate (CAE manufactured by Ajinomoto Co.) 0.2 Parahydroxybenzoate -Phenoxyethanol mixture (Secept, Seiwa Kasei Co., Ltd.) 0.3 Perfume Appropriate amount Sterilized ion-exchanged water Total 100.0 Citric acid pH 5.5 Also, triethanol of coconut oil fatty acid condensate of keratin oxidized peptide of Example 2 above A hair rinse having the same composition as that of Example 4 was prepared, except that the amount of sterilized ion-exchanged water was increased without adding the amine salt.
And

The hair rinses of Example 4 and Comparative 4 were diluted 5-fold and used for hair after washing with a commercially available shampoo, and the gloss, suppleness, and combability of the hair were evaluated by 10 female panelists. . Table 6 shows the results.

As shown in Table 6, the hair rinse of Example 4 in which the toluethanol salt of the keratin oxidized peptide coconut oil fatty acid condensate of Example 2 was blended was used as the keratin oxidized peptide coconut oil fatty acid condensate of Example 2 above. As compared with the hair rinse of Comparative product 4 containing no triethanol salt, the effect of improving the luster, suppleness, and combability of the hair was excellent.

In particular, the hair rinse of Example 4 is easy to prepare the hair rinse due to the excellent emulsifying power of the triethanolamine salt of the coconut oil fatty acid condensate of the keratin oxidized peptide of Example 2, and the storage stability after the preparation. The character was excellent.

Application Example 5 A hair rinse having the following composition containing a 2-amino-2-methyl-1,3-propanediol salt of an isostearic acid condensate of a keratin-oxidized peptide obtained in Example 5 was prepared, and this was used as a hair rinse. Inventive example 5 was obtained.

2-amino-2-methyl-1,3-propanediol salt of the isostearic acid condensate of the keratin oxidized peptide of Example 5 (30%) 3.0 diisopropyl adipate 3.0 behenyl alcohol 2.0 cetyl alcohol 0.3 cetyltrimethylammonium chloride (27%) 6.7 Distearyldimethylammonium chloride (73%) 3.8 Dimethylpolysiloxane (KF96-
350cs) 0.5 Hydrolyzed collagen (30%) (Promois W-32R manufactured by Seiwa Kasei) 2.0 Propylene glycol 3.0 Mixture of parahydroxybenzoate and phenoxyethanol (Secept manufactured by Seiwa Chemical) 0.3 Perfume Appropriate amount Sterile ion-exchanged water The total amount was 100.0. In addition, 2-amino-2-methyl-1,3-propanediol salt of isostearic acid condensate of the keratin-oxidized peptide of Example 5 was not added, and sterilized ion-exchanged water was increased. Prepared a hair rinse having the same composition as that of the product 5 and used it as a comparative product 5.

The hair rinse of Example 5 and Comparative Example 5 were diluted 5-fold and used on the hair after washing with a commercially available shampoo to compare the feeling of use. As a result, the hair rinse of Example 5 was better. It was excellent in improving the gloss, suppleness and combability of hair, and was easy to prepare a hair rinse, and was excellent in storage stability after preparation.

Application Example 6 A base for styling mousse having the following composition containing the sodium salt of oleic acid condensate of keratin oxidized peptide obtained in Example 6 was prepared, and the base for styling mousse and liquefied petroleum gas (LPG) were mixed with 90%. At 10:10, the mixture was filled in a spray container to obtain a styling mousse, which was designated as Example 6 of the present invention.

Sodium salt of oleic acid condensate of keratin oxidized peptide of Example 6 (30%) 5.0 Polyoxyethylene (15) lauryl ether 0.5 99% ethanol 5.0 Polyethylene bricol (14) Oleate 1.0 Acrylic resin alkanolamine liquid Cetyltrimethylammonium chloride (29%) 0.5 Dimethylsiloxane methyl (polyoxyethylene
Polyoxypropylene) siloxane copolymer (SH3749 manufactured by Toray Silicone Co., Ltd.) 1.0 Mixture of parahydroxybenzoic acid ester and phenoxyethanol (Secept manufactured by Seiwa Chemical Co., Ltd.) 0.3 EDTA-2Na 0.1 Flavor Appropriate amount Sterilized ion-exchanged water Total 100.0 Also, a styling mousse having the same composition as that of Example 6 was prepared except that the sodium salt of oleic acid condensate of the keratin oxidized peptide of Example 6 was not added and sterile ion exchange water was increased. This was designated as Comparative Product 6.

Using the styling mousse of this embodiment product 6 and the comparative product 6 on the hair, and comparing the feeling of use of both, the styling mousse of the embodiment product 6 improves the gloss, suppleness, and combability of the hair. The effect was excellent, the styling mousse base was easily prepared, and the storage stability of the styling mousse after preparation was excellent.

Application Example 7 A cream having the following composition containing the keratin oxidized peptide coconut oil fatty acid condensate obtained in Example 7 was prepared, and this was designated as Example product 7 of the present invention.

Coconut fatty acid condensate of keratin oxidized peptide of Example 7 4.5 Emulsifier mixture (Ayakol 112 manufactured by Seiwa Kasei Co., Ltd.) 12.0 Glycerin monoisostearate 3.0 Hexadecyl isostearate 4.5 Polyoxyethylene (15) cetyl ether 2.0 Jojoba oil 1.5 Liquid paraffin 2.5 dimethylpolysiloxane (KF96-
350cs) 0.2 methylphenyl polysiloxane (Toray Silicone Co., Ltd.)
SH556) 1.5 Butyl parahydroxybenzoate 0.1 Glycerin 9.0 1,3-butylene glycol 5.0 Triethanolamine 1.0 Retinol palmitate 0.5 Butylhydroxytoluene 0.05 EDTA2-Na 0.1 Sterile ion-exchanged water Total 100.0 A cream having the same composition as that of the practical product 7 was prepared, except that the coconut oil fatty acid condensate of the peptide was not added and the amount of sterilized ion-exchanged water was increased.

Using the cream of Example 7 and the cream of Comparative product 7 by hand, and comparing the feeling of use of both, the cream of Example 7 is easier to adjust to the skin, spreads better, and gives gloss and moisture to the skin. And the cream was easily adjusted, and the adjusted cream had excellent storage stability.

Application Example 8 A liquid hairdressing composition having the following composition was prepared by mixing a potassium salt of a resin acid condensate of the keratin oxidized peptide obtained in Example 8, and this was designated as Example product 8 of the present invention.

Potassium salt of resin acid condensate of keratin oxidized peptide of Example 8 3.0 Diisobutyl adipate 0.3 Polyoxypropylene monobutyl ether 23.0 95% ethanol 63.0 O-Cimen-5-ol 0.1 Propylene glycol 3.0 Fragrance Appropriate amount Sterilized ion exchange water Total 100.0 In addition, except that the potassium salt of the resin acid condensate of the keratin oxidized peptide of Example 8 was not added and the amount of sterilized ion-exchanged water was increased, a liquid hairdressing composition having the same composition as that of Example 8 was used. This was prepared as Comparative Product 8.

The liquid hair styling products of Example 8 and Comparative Product 8 were continuously used for the hair of 10 male panelists for one week each, and the hair styling power, the gloss of the hair, and the moisture were evaluated to see which was better. Table 7 shows the results.

As shown in Table 7, the liquid hair styling product of Example 8 in which the potassium salt of the resin acid condensate of the keratin oxidized peptide of Example 8 was blended was the potassium salt of the resin acid condensate of the keratin oxidized peptide of Example 8 described above. Compared to the liquid hair styling product of Comparative product 8 containing no salt, the hair styling effect, the effect of improving the luster of hair, and the effect of improving moisture were superior.

〔The invention's effect〕

As described above, the acylated keratin oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) of the present invention or a salt thereof has a cysteic acid residue in the peptide chain. As compared with the conventional acylated keratin peptide or a salt thereof, the keratin peptide has excellent detergency, a large emulsifying power, and can exhibit good surface activity even in an acidic region.

An acylated keratin peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or a salt thereof is equivalent to or more than a conventional acylated keratin peptide or a salt thereof. Protects hair, softens hair, gives hair smoothness, moisturizing, and gloss, improves combing of hair, and imparts moist feeling, moisture, smoothness, and gloss to skin have. Naturally, because it is derived from natural proteins, it has low irritation to skin and mucous membranes,
The safety is also excellent. Therefore, an acylated keratin-oxidized peptide having a cysteic acid residue in the peptide chain represented by the above general formula (I) or a salt thereof is extremely excellent as a base for blending cosmetics.

Accordingly, an acylated product of a keratin-oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or a salt thereof, and an acylated product of a keratin-oxidized peptide having no cysteic acid residue in the peptide chain or Depending on the ratio of the acylated keratin oxidized peptide having a cysteic acid residue in the peptide chain represented by the general formula (I) or the salt thereof, the mixture with the salt thereof may be a cysteic acid residue in the peptide chain. An acylated product of a keratin oxidized peptide having no cysteic acid residue in the peptide chain and a salt thereof, and an acylated product of a conventional keratin peptide or a salt thereof on hair and skin are exhibited. Since they exhibit the above properties, they are useful as bases for compounding cosmetics.

[Brief description of the drawings]

1 to 8 are graphs showing the results of gas chromatography of the methyl esterified product of the higher fatty acid portion of the substances produced in Examples 1 to 8 of the present invention and the methyl esterified product of the higher fatty acid used as a raw material. The temperature and heating rate are as shown in each figure. The number of each peak in the figure is the detection time (min)
Is shown.

Continued on the front page (58) Fields investigated (Int. Cl. ⁶ , DB name) C07K 14/47 C07K 1/107-1/113 A61K 7/06 CA (STN) CAOLD (STN) REGISTRY (STN)

Claims (1)

(57) [Claims] 1. An acylated keratin-oxidized peptide having a cysteic acid residue in the peptide chain represented by the following general formula (I) or a salt thereof, and a keratin-oxidized peptide having no cysteic acid residue in the peptide chain: Cosmetic base comprising a mixture with an acylated product thereof or a salt thereof. General formula (I): (Wherein, R ₁ is an alkyl group having 7 to 21 carbon atoms, 7 to 21 carbon atoms)
A hydrocarbon group alkenyl group or alicyclic structure, R ₂
Is the side chain of the constituent amino acids of the keratin peptide. M ₁ and M ₂ are hydrogen, an alkali metal such as lithium, sodium, potassium, ammonium or monoethanolamine, diethanolamine, triethanolamine, 2-
Amino-2-methyl propane, 2-amino-2-methyl-1,3 is an onium of an organic amine, such as propanediol, M ₁ and M ₂ may be the also well or different in the same. m and n are from 0 to 24, a is from 1 to 2.5, and m +
n + a is 2 to 25)