JPH11269045A - Hair-protecting agent - Google Patents

Abstract

PROBLEM TO BE SOLVED: To obtain a hair-protecting agent having excellent protecting activities for hair, capable of recovering the damaged hair, and capable of providing excellent luster, moisture, smoothness, combining or the like to the hair. SOLUTION: This hair-protecting agent contains a cystine-introduced peptide obtained by introducing cystine to a hydrolyzed peptide obtained by hydrolyzing a protein derived from a natural product such as an animal, a plant or a microorganism, or a derivative thereof by an amide bond of the amino group composed of the hydrolyzed peptide or the derivative thereof, and the carboxyl group of the cystine, in a substrate consisting of water or consisting essentially of the water. The content of the cystine-introduced peptide in the hair-protecting agent is preferably 0.1-20 wt.%.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a hair protectant, and more particularly, to an excellent hair containing a cystine-introduced peptide having enhanced cystine-based properties by introducing cystine into a hydrolyzed peptide or a derivative thereof. The present invention relates to a hair protecting agent having an action of preventing damage to hair and a function of repairing damaged hair.

[0002]

2. Description of the Related Art Various hair cosmetics such as shampoos, rinses, permanent waving agents, and hair dyes are used for hair. The use of such hair cosmetics may damage the hair.

[0003] For example, in the permanent wave treatment, a reducing agent is applied to hair to cleave disulfide bonds (SS bonds) of cystine present in keratin proteins of hair to generate mercapto groups (-SH groups). . Next, oxidation with an oxidizing agent such as sodium bromate or hydrogen peroxide regenerates the disulfide bond.At this time, in order to more effectively perform the reducing action and improve the durability of the wave, an alkali agent, For example, the reducing agent is caused to act in a high pH region by using ammonia or monoethanolamine in combination. As a result, some of the keratin protein in hair is damaged due to elution of some of its components.Particularly, part of cystine in the keratin protein undergoes a chemical change to cysteic acid and the like with an oxidizing agent that is subsequently acted on. You will not be able to return to cystine.

In the hair dyeing treatment, the hair is liable to be damaged by the bleaching treatment of the hair, the action of an alkali agent or an oxidizing agent in the oxidative hair dye, and the protein (protein) component in the hair is likely to flow out.

Further, even in daily shampoos, the sebum and constituent proteins of the hair are eluted due to the effect of the surfactant contained therein, and the hair is damaged. After drying, the hair becomes dry or rough. To give.

[0006] Therefore, in the above hair treatment process,
Protecting hair has been studied, and as a method for protecting such hair, blending of a protein hydrolyzate (hydrolyzed peptide) or a derivative thereof into cosmetics has been performed (for example, see Japanese Patent Application Laid-Open 57-165310, JP-A-59-88410, etc.), which were not sufficiently satisfactory.

That is, a protein hydrolyzate is derived from its protein origin. For example, hydrolyzed collagen easily forms a film and has a large effect of enhancing the strength of hair, and hydrolyzed silk forms a dense film on the hair to form a hair. Hydrolyzed wheat protein and hydrolyzed soy protein derived from plant proteins have the characteristics of having a strong moisturizing property and a large effect of giving a moist feeling to hair. Is a protein of a different kind from the keratin protein that is the subject of treatment, and in particular, does not contain cystine, which is contained a lot in keratin substances, or has a very low content, so its sorption power on hair is weak. Although it is possible to recover the physical strength of damaged hair by forming a film, there is a problem that chemical repair cannot be performed.

[0008] Among the protein hydrolysates, hydrolyzed keratin contains cystine, so that it has a good sorption property to hair as compared with hydrolyzed collagen and hydrolyzed silk, etc. Although excellent in recovery from damage, there is a problem that it is slightly inferior to hydrolyzed collagen, hydrolyzed silk, hydrolyzed soybean protein, etc. in terms of film forming ability and effect of imparting gloss and moisture to hair.

Therefore, a quaternary ammonium salt is introduced into a protein hydrolyzate to increase the ionicity of a trimethylammonium derivative of a protein hydrolyzate or a higher alkylammonium derivative of a protein hydrolyzate. Attempts have been made not only to prevent and repair hair damage, but also to impart the luster, moisture and good combability of protein hydrolysates (for example,
JP-A-60-243010, JP-A-4-2992
No. 1), the sorption of these quaternary ammonium derivatives to hair is due to ionic bonds, and therefore has a better sorption property to hair than the hydrolyzate before derivatization, but is similar to cystine. Is not a covalent bond due to
When incorporated in water-washable products such as shampoos, rinses and permanent waving agents, their effects could not be fully exerted.

[0010]

DISCLOSURE OF THE INVENTION The present invention solves the above-mentioned problems of the conventional hair protectants, prevents hair damage by hair cosmetics, recovers damaged hair, and improves the quality of hair. An object of the present invention is to provide a hair protectant capable of imparting gloss, moisture, smoothness (smoothness), combability, and the like.

[0011]

Means for Solving the Problems The present inventors have conducted intensive studies in order to solve the above-mentioned problems, and as a result, have obtained a hydrolysis obtained by hydrolyzing proteins derived from natural products such as animals, plants or microorganisms. An amide bond between the amino group of the hydrolyzed peptide or its derivative and the carboxyl group of cystine is attached to the peptide or its derivative, so that the cystine-introduced peptide having cystine introduced therein has excellent sorption property to hair and prevents hair damage The present inventors have found that damaged hair can be recovered and excellent luster, moisture, smoothness, combability and the like can be imparted to the hair, and the present invention has been completed based on that.

That is, a cystine-introduced peptide in which cystine is introduced into a hydrolyzate peptide or derivative containing no cystine or having a low cystine content to enhance the properties of disulfide bonds is absorbed onto the hair and protects the hair. Prevents hair damage, restores damaged hair, and exerts effects of imparting gloss, moisture, smoothness, good combability, etc., to the hair of each hydrolyzate peptide or its derivative. You can do it.

[0013]

BEST MODE FOR CARRYING OUT THE INVENTION The cystine-introduced peptide used in the present invention is a hydrolyzed peptide obtained by hydrolyzing a protein derived from a natural product such as an animal, a plant or a microorganism with an acid, an alkali, an enzyme or a combination thereof. Or a derivative thereof into which cystine has been introduced. As a protein (protein) source of the hydrolyzed peptide or its derivative,
Proteins derived from natural products, for example, collagen (including gelatin which is a denatured product thereof), silk fibroin (silk), sericin, casein, conchiolin, elastin, egg yolk proteins such as chickens, and egg-derived proteins such as egg white proteins And those derived from plants such as soybeans, wheat, beer lees, corn, rice (rice bran), potato proteins, and yeasts of the genera Saccharomyces, Candida, Endomycopsis, and so-called yeasts. Examples thereof include yeast derived from microorganisms such as yeast isolated from yeasts called beer yeast and sake yeast, mushrooms (basidiomycetes) and proteins isolated from chlorella. In addition, when keratin having a high cystine content is used, the sorption property to hair can be further enhanced by introducing cystine.

The hydrolyzed peptide used in the present invention is obtained by hydrolyzing the above protein with an acid, an alkali, an enzyme or a combination thereof, wherein the amount of the acid, alkali or enzyme used, the reaction temperature, By appropriately selecting the reaction time and the like, the degree of amino acid polymerization of the obtained hydrolyzed peptide can be changed in various ways, but in consideration of the sorption property to the hair and the film forming property, the number average molecular weight is 150 to 1000.
0, particularly preferably 200 to 5000. That is, when the number average molecular weight of the hydrolyzed peptide is larger than the above range, the sorption property and permeability to the hair may be reduced, and when the number average molecular weight of the hydrolyzed peptide is smaller than the above range, the absorption to the hair may be reduced. Although the adhesiveness and permeability are excellent, the film-forming action on the hair may be reduced, and the protective action of the hair may be reduced. When cystine is introduced, two peptide chains are bonded via cystine, and the number average molecular weight of the cystine-introduced peptide is about twice the above value.

For acid hydrolysis of proteins, for example, 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 are used. For example, inorganic alkalis such as sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, and lithium carbonate are used. For the enzymatic hydrolysis of the protein, an acidic protease such as pepsin, proctase A and proctase B, and a neutral or alkaline protease 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.

Derivatives of the hydrolyzed peptide include esters with the alcohol at the carboxyl group of the hydrolyzed peptide, for example, methyl ester, ethyl ester, propyl ester, isopropyl ester, lauryl ester, cetyl ester, 2-ethylhexyl ester. And esters with a hydrocarbon alcohol having 1 to 20 carbon atoms, such as, 2-hexyldecyl ester and stearyl ester.

In order to obtain a cystine-introduced peptide, first,
Cystine is converted to N, N'-dicarboxy-anhydrocystine. As a method for obtaining this N, N'-dicarboxy-anhydrocystine, a known method can be employed.

For example, first, a chlorocarbonate such as benzyl chlorocarbonate, methyl chlorocarbonate, or allyl chlorocarbonate is added dropwise to an alkaline aqueous solution of cystine under alkaline conditions, and an amino group of cystine is converted into a cystine as shown in the following reaction formula [I]. Protect.

[0019]

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(Wherein R is a benzyl group, an alkyl group or an allyl group)

Next, the reaction solution is acidified with a mineral acid such as hydrochloric acid or sulfuric acid, and then the reaction product is extracted with an organic solvent such as ethyl acetate, and the organic layer is washed with a saline solution and water. Removal by concentration under reduced pressure gives cystine in which the amino group is protected.

Next, the amino-protected cystine obtained above is dissolved in a dissolvable organic solvent such as ethyl acetate, and as shown in the following reaction formula [II], under a nitrogen gas atmosphere, The carboxyl group is converted to carbonyl chloride by the action of thionyl chloride (instead of thionyl chloride, phosphorus trichloride, phosphorus pentachloride, etc.), and then heat-condensed at 80 ° C. or more under reduced pressure to give N, N′-diamine. A carboxy anhydrous cystine is obtained.

[0023]

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Further, cystine is directly reacted with phosgene, phosgene dimer, phosgene trimer, etc.
N'-dicarboxy anhydrous cystine can also be synthesized.

The reaction between the hydrolyzed peptide or its derivative and N, N'-dicarboxyanhydrocystine obtained as described above proceeds as shown in the following reaction formula [III].

[0026]

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(Wherein, R ′ represents various amino acid side chains, and n represents the degree of amino acid polymerization)

First, the pH of an aqueous solution of a hydrolyzed peptide or a derivative thereof is adjusted to about 10.0 to 10.5 with an alkaline agent such as an aqueous solution of sodium hydroxide, and N, dissolved in a solvent such as ethyl acetate. N'-dicarboxy anhydrous cystine is added dropwise under ice-cooling, and at the same time, an alkaline agent such as an aqueous sodium hydroxide solution is added dropwise to adjust the pH.
Is maintained at 10.0 to 10.5.

After the completion of the dropwise addition of N, N'-dicarboxyanhydrocystine, the reaction is completed by continuing stirring for 2 to 5 hours under ice cooling. Next, a solvent incompatible with water, such as n-hexane, is added to the reaction solution for washing, and unreacted N, N'-dicarboxyanhydrocystine is transferred to the organic layer and removed. By adjusting the pH to 3 to 4 with hydrochloric acid or the like and performing decarboxylation, a cystine-introduced peptide can be obtained. In this cystine-introduced peptide, cystine is introduced into the hydrolyzed peptide or its derivative by an amide bond between the amino group of the hydrolyzed peptide or its derivative and the carboxyl group of cystine as shown in the formula [III].

The decarboxylated cystine-introduced peptide solution can be used as it is or in the form of a powder for preparing a hair protecting agent, or, if necessary, by ion exchange resin, dialysis membrane, electrodialysis, gel filtration, ultrafiltration, etc. After purification
It is used as a liquid or in the form of a powder after preparing it.

In the present invention, since the cystine-introduced peptide is characterized by forming a disulfide bond with the hair, it is preferable that the half-cystine-containing peptide contains 5 mol% or more of cystine as a half-cystine. In preparing the hair protecting agent, two or more cystine-introduced peptides having different protein sources may be used. The content of the cystine-introduced peptide in the hair protecting agent (the amount of the cystine-introduced peptide in the hair protecting agent) is preferably 0.1 to 20% by weight, particularly preferably 1 to 10% by weight. That is, when the content of the cystine-introduced peptide in the hair protecting agent is less than the above range, the hair is protected to prevent the hair from being damaged, and the hair has luster, moisture, smoothness, and good combability. There is a possibility that the properties of the peptide moiety such as imparting action may not be sufficiently exhibited, and even if the content of the cystine-introduced peptide in the hair protecting agent is more than the above range, the effect corresponding to the increase in the content In addition to the above, there is a possibility that the hair becomes sticky due to excessive adsorption of the cystine-introduced peptide to the hair.

The hair protectant of the present invention is prepared by adding the cystine-introduced peptide to water or a base containing water as a main component. The above-mentioned base containing water as a main component means that an alcohol such as ethanol (ethyl alcohol), ethylene glycol, propylene glycol, 1,3-butylene glycol or glycerin or a polyhydric alcohol is dissolved in water to dissolve a cystine-introduced peptide. The amount added is within the range that does not inhibit the addition. Usually, the amount of alcohols or polyhydric alcohols is preferably 50% by weight or less in the base.

The hair protective agent of the present invention includes various surfactants, emulsifiers, wetting agents,
Preservatives, fragrances, coloring agents, and other additives can be added as appropriate.

In addition to the cystine-introduced peptide, the components which can be added when preparing the hair protectant of the present invention include, for example, alkyl sulfates such as ammonium lauryl sulfate, sodium lauryl sulfate and triethanolamine lauryl sulfate, and polyoxyethylene (2EO). ) Lauryl ether triethanolamine sulfate (EO is ethylene oxide, the value before EO indicates the number of moles of ethylene oxide added), polyoxyethylene (3EO) alkyl (any one of 11 to 15 carbon atoms or 2 Or a mixture of more than one species) polyoxyethylene alkyl ether sulfates such as sodium ether sulfate, alkylbenzene sulfonates such as sodium laurylbenzenesulfonate and triethanolamine laurylbenzenesulfonate, polyoxyethylene ( EO) Polyoxyethylene alkyl ether acetates such as sodium tridecyl ether acetate, coconut oil fatty acid sarcosine sodium, sodium lauroylmethyl-β-alanine, sodium lauroyl-L-glutamate, coconut oil fatty acid-sodium L-glutamate, lauroylmethyltaurine N-acyl amino acid salts such as sodium, sodium ether sulfate alkane sulfonate, hydrogenated coconut oil fatty acid sodium glycerin sulfate, disodium amide amide sulfosuccinate, disodium lauryl sulfosuccinate, polyoxyethylene alkyl (12 to 15 carbon atoms) ether Phosphoric acid (8 to 10 EO), sodium polyoxyethylene cetyl ether phosphate, disodium lauryl polyoxyethylene sulfosuccinate, polyoxyethylene Anionic surfactants such as sodium renlauryl ether phosphate, undecylenoyl hydrolyzed collagen potassium, sodium laurate hydrolyzed collagen, coconut oil fatty acid hydrolyzed collagen sodium, potassium, salts such as triethanolamine, 2-alkyl-N -Carboxymethyl-N-hydroxyethylimidazolinium betaine, undecyl-N-hydroxyethylimidazolinium betaine sodium, undecyl-N-hydroxyethyl-N-carboxymethylimidazolinium betaine, stearyldihydroxyethylbetaine, stearyldimethylaminoacetic acid Betaine, coconut oil fatty acid amidopropyl betaine, coconut oil alkyl-N-carboxyethyl-N-hydroxyethylimidazolinium betaine sodium Amphoteric surfactants such as N- cocoyl -L- arginine ethyl · DL-pyrrolidone carboxylate, polyoxyethylene alkyl (carbon number 12-1
4) Ether (7EO), polyoxyethylene octylphenyl ether, polyoxyethylene oleyl ether, polyoxyethylene glyceryl oleate, polyoxyethylene stearyl ether, polyoxyethylene cetyl ether, polyoxyethylene sorbitol lanolin (40EO), poly Nonionic surfactants such as oxyethylene polyoxypropylene cetyl ether, polyoxyethylene lanolin, polyoxyethylene lanolin alcohol, stearyltrimethylammonium chloride, cetyltrimethylammonium chloride, cetostearyltrimethylammonium chloride, behenyltrimethylammonium bromide, iodide Cetyltrimethylammonium, oleylbenzyldimethylammonium chloride, oleylbis chloride (poly Kishiechiren (15 EO)] methyl ammonium, dialkyl dimethyl ammonium salts,
Mink oil chloride fatty acid amidopropyldimethylhydroxyethylammonium, alkyl pyridinium salt, chloride
cationic surfactants such as γ-gluconamidopropyldimethylhydroxyethylammonium, cationized cellulose, cationized hydroxyethylcellulose,
Cationic polymers such as poly (diallyldimethylammonium chloride), polyvinylpyrrolidone, and polyethyleneimine; synthetic polymers such as amphoteric polymers and anionic polymers; isostearic acid diethanolamide, undecylenic acid monoethanolamide, oleic acid diethanolamide, and tallow fatty acid monoethanolic acid Amide, diethanolamide stearic acid, diethylaminoethylamide stearate, coconut oil fatty acid ethanolamide, coconut oil fatty acid diethanolamide, lauric acid isopropanolamide, lauric acid ethanolamide, lauric acid diethanolamide, lanolin fatty acid diethanolamide, sodium carboxymethylcellulose, hydroxy Ethyl cellulose, carboxyvinyl polymer, carrageenan, xan Thickeners such gum, waxes, paraffins, fatty esters, glycerides, lecithin,
Squalane, oils and fats such as animal and vegetable oils such as avocado oil, animal and plant extracts, collagen, keratin, silk, casein, soybean, wheat, corn, potato, yeast, mushrooms and other hydrolyzed peptides of animal and plant and microorganism-derived proteins and Its peptide ester derivatives,
N-quaternary ammonium derivatives of hydrolyzed peptides of proteins derived from animals, plants and microorganisms, polysaccharides or derivatives thereof, coconut oil fatty acid diethanolamide,
Penetrants such as sorbitan monolaurate, polyoxyethylene nonyl phenyl ether, benzyl alcohol,
Glycyrrhizic acid, licorice derivatives such as carbenokirone disodium, allantoin, guaiazulene, anti-inflammatory agents such as α-bisabolol, higher alcohols such as behenyl alcohol, cetyl alcohol, stearyl alcohol, L-aspartic acid, DL-alanine, L-arginine , Glycine, L-glutamic acid, L
-Amino acids such as cysteine and L-threonine, linear or cyclic methylpolysiloxane, methylphenylpolysiloxane, dimethylpolysiloxane polyethylene glycol copolymer, dimethylpolysiloxane polypropylene copolymer, amino-modified silicone oil, and quaternary ammonium And silicone oils such as modified silicone oils.

The hair protectant of the present invention may be used alone (ie, alone), or the hair protectant of the present invention may be used as a shampoo, a hair rinse, a hair treatment,
It may be added to various hair cosmetics such as a hair conditioner, an agent for a permanent wave, a hair dye and a depigmenting agent.

When the hair protecting agent of the present invention is used alone,
The hair cosmetics may be used irrespective of their use, or may be used before, during, or after use of the hair cosmetics. In particular, for hair rinses, hair treatments, and hair cosmetics that protect hair such as hair conditioners and have a conditioning action on hair, once the cystine-introduced peptide is contained in water or a base containing water as a main component and used as a hair protectant. From
It may be mixed with the above-mentioned hair rinse, hair treatment, hair conditioner, or the like, or the components necessary for the hair rinse, hair treatment, hair conditioner, etc. may be water or a water-based base together with the cystine-introduced peptide. By containing
They may be prepared as a hair protectant having a conditioning action such as hair rinse, hair treatment, and hair conditioner.

[0037]

Industrial Applicability The hair protective agent of the present invention has an excellent protective effect on hair, prevents hair damage, restores damaged hair, and provides excellent gloss, moisture, and smoothness to hair. It has the effect of imparting combability and the like.

[0038]

Next, the present invention will be described more specifically with reference to examples. However, the present invention is not limited to only these examples. In the following examples,% indicating the concentration of a solution, a dispersion, or the like is% by weight unless the unit is specified. Prior to the examples, a production example of the cystine-introduced peptide used in the examples and a production of N, N'-dicarboxy-anhydrocystine used in the production of the cystine-introduced peptide are shown as reference examples. In addition, a method for measuring the tensile strength of hair and a method for measuring the content of cysteic acid in hair performed in Examples and the like will also be described prior to the Examples.

Reference Example 1 (Production Example 1 of anhydrous N, N'-dicarboxy cystine) 18 g of cystine was dissolved in 150 ml of a 1N aqueous solution of sodium hydroxide, and 38.3 g of benzyl chlorocarbonate was added with stirring under ice cooling. Dropped over minutes. During this time, the pH of the reaction solution was maintained at 9 to 10 by adding an aqueous sodium hydroxide solution. After the end of the dropping of benzyl chlorocarbonate,
Stirring was continued at room temperature for 2 hours to complete the reaction.

After completion of the reaction, the pH of the reaction solution was adjusted to 1 with dilute hydrochloric acid, and 300 ml of ethyl acetate was added to extract a reaction product. The organic layer was washed twice with 150 ml of a 2% saline solution, further washed with 75 ml of water, and then dried over 30 ml of anhydrous sodium sulfate.
g was added and the organic layer was dried. After removing anhydrous sodium sulfate by filtration, the filtrate was concentrated under reduced pressure to dryness, and the residue was recrystallized from chloroform to obtain 30 g of N, N'-dicarbobenzoxycystine.

Next, this N, N'-dicarbobenzoxycystine was dissolved in 267 ml of a benzene-dioxane mixed solution (volume ratio = 250: 17) and stirred under a nitrogen gas atmosphere. 2 ml of thionyl chloride was added dropwise over 1 hour. After completion of the dropwise addition, the temperature of the reaction
And stirred for 3 hours to complete the reaction.

After completion of the reaction, the temperature of the reaction solution was reduced to 80 under reduced pressure.
After heating and condensing for 2 hours while maintaining the temperature at ８５85 ° C., the reaction solution was washed five times with 20 ml of n-hexane, and the aqueous layer was concentrated under reduced pressure to obtain 19.3 g of N, N′-dicarboxyanhydrocystine anhydride. I got

Reference Example 2 (Production Example 2 of anhydrous N, N'-dicarboxy) 12 g of cystine was dissolved in 100 ml of a 1N aqueous sodium hydroxide solution, and 14.1 g of methyl chlorocarbonate was added to 30 ml of the solution while stirring under ice-cooling. Dropped over minutes. During this time, the pH of the reaction solution was maintained at 9 to 10 by adding an aqueous sodium hydroxide solution. After the completion of the dropwise addition of methyl chlorocarbonate, stirring was continued at room temperature for 2 hours to complete the reaction.

After the completion of the reaction, the pH of the reaction solution was adjusted to 1 with dilute hydrochloric acid, and 200 ml of ethyl acetate was added to extract a reaction product. The organic layer was washed twice with 100 ml of a 2% saline solution, further washed with 100 ml of water, and then dried over anhydrous sodium sulfate.
0 g was added and the organic layer was dried. After removing anhydrous sodium sulfate by filtration, the filtrate was concentrated under reduced pressure to dryness, and the residue was washed with n-hexane and dried under reduced pressure to obtain 10 g of cystine methyl carbonate.

Next, this methyl cystine carbonate was added to 30 m
dissolved in 1 l of ethyl acetate, stirred under a nitrogen gas atmosphere,
8.07 ml of thionyl chloride was added dropwise thereto over 1 hour. After completion of the dropwise addition, the temperature of the reaction solution was raised to 55 ° C., and stirring was continued for 4 hours to complete the reaction.

After completion of the reaction, the temperature of the reaction solution was reduced to 80 under reduced pressure.
After maintaining the temperature at ８５85 ° C. and performing heat condensation for 2 hours, the reaction solution was washed 5 times with 20 ml of n-hexane, and the aqueous layer was concentrated under reduced pressure to obtain 7.9 g of N, N′-dicarboxyanhydrocystine anhydride. I got

Production Example 1 (Example of production of cystine-introduced hydrolyzed collagen) 47 g of a 30% aqueous solution of hydrolyzed collagen having a number average molecular weight of 450 (30.5 mmol as the stoichiometric mole number obtained by measurement of amino nitrogen) ) Was adjusted to pH 10.2 with an aqueous sodium hydroxide solution, and under ice cooling, 3.1 g (10 mmol, hydrolyzed collagen) of N, N'-dicarboxyanhydrocystine prepared in Reference Example 1 was added to the solution. (0.65 eq.) Was dissolved in 50 ml of ethyl acetate, and the mixture was stirred and mixed, and the mixture was stirred and reacted for 3 hours. During this time, the pH of the reaction solution was maintained at 10.0 to 10.5 by adding an aqueous sodium hydroxide solution.

After completion of the reaction, the reaction product was washed three times with 100 ml of n-hexane to remove unreacted materials, and then concentrated sulfuric acid was added to the aqueous layer to adjust the pH to 4, followed by decarbonation under reduced pressure. And
By adjusting the concentration, 3 of cystine-introduced hydrolyzed collagen
45.1 g of a 0% aqueous solution was obtained.

A part of the cystine-introduced hydrolyzed collagen obtained as described above was completely hydrolyzed with 6N hydrochloric acid for 20 hours, and then subjected to amino acid analysis with an amino acid autoanalyzer.
Was detected. Further, when a part of the cystine-introduced hydrolyzed collagen obtained as described above was subjected to amino acid analysis without performing hydrolysis with hydrochloric acid, cystine was not detected, and all of the cystine detected above was hydrolyzed collagen. It was revealed to be binding.

Since cystine was not contained in the starting hydrolyzed collagen, it was clear that all of the cystine had been introduced into the hydrolyzed collagen by the cystine introduction method described above.

Production Example 2 (Production example of cystine-introduced hydrolyzed wheat protein) 80 g of a 30% aqueous solution of hydrolyzed wheat protein having a number average molecular weight of 700 (as the stoichiometric mole number obtained by measurement of amino nitrogen: 34. 2 mmol) was adjusted to pH 10.2 with an aqueous sodium hydroxide solution, and 4.5 g (15.4 mmol) of N, N'-dicarboxyanhydrocystine anhydride prepared in Reference Example 1 was added to this solution under ice-cooling. (0.9 equivalents to the hydrolyzed wheat protein) in 80 ml of ethyl acetate was added and mixed by stirring, and the mixture was stirred and reacted for 3 hours. During this time, the pH of the reaction solution was maintained at 10.0 to 10.5 by adding an aqueous sodium hydroxide solution.

After the completion of the reaction, the reaction product was washed four times with 100 ml of n-hexane to remove unreacted materials, and then concentrated sulfuric acid was added to the aqueous layer to adjust the pH to 4, followed by decarbonation under reduced pressure. And
The concentration was adjusted to obtain 75.5 g of a 30% aqueous solution of cystine-introduced hydrolyzed wheat protein.

A part of the cystine-introduced hydrolyzed wheat protein obtained as described above was completely hydrolyzed with 6N hydrochloric acid for 20 hours, and then subjected to amino acid analysis using an amino acid autoanalyzer. As a result, 5.9 mol% as half cystine was obtained. Was detected. When a part of the cystine-introduced hydrolyzed wheat protein obtained as described above was subjected to amino acid analysis without hydrolysis with hydrochloric acid, no cystine was detected, and all of the cystine detected above was hydrolyzed. It was found to be bound to wheat protein.

Since the hydrolyzed wheat protein as a raw material contained 0.4 mol% of cystine, it was detected at 5.9.
It was clear that 5.5 mol% of the mol% of cystine was introduced into the hydrolyzed wheat protein by the cystine introduction method described above.

Production Example 3 (Production example of hydrolyzed cystine-introduced silk) In place of hydrolyzed wheat protein, 80 g of a 30% aqueous solution of hydrolyzed silk having a number average molecular weight of 350 (stoichiometric amount obtained by measurement of amino nitrogen) 77.3 mmol as the number of moles) and 6.1 g (20.8 mmol, 0.5 equivalent to hydrolyzed silk) of N, N'-dicarboxyanhydrocystine produced in Reference Example 1 described above were added to 100 ml of acetic acid. A 30% aqueous solution of cystine-introduced hydrolyzed silk was prepared in the same manner as in Production Example 2 except that a solution dissolved in ethyl was used.
2 g were obtained.

A part of the cystine-introduced hydrolyzed silk obtained as described above was completely hydrolyzed with 6N hydrochloric acid for 20 hours, and then subjected to amino acid analysis with an amino acid autoanalyzer. As a result, 6.2 mol% of half cystine was obtained. was detected. Further, when a part of the cystine-introduced hydrolyzed silk obtained as described above was subjected to amino acid analysis without hydrolysis with hydrochloric acid, cystine was not detected, and all of the cystine detected above was hydrolyzed silk. It was revealed to be binding.

Since the raw material hydrolyzed silk contained no cystine, it was clear that all the cystine had been introduced into the hydrolyzed silk by the cystine introduction method described above.

Production Example 4 (Production example of cystine-introduced hydrolyzed soybean protein) 50 g of a 30% aqueous solution of hydrolyzed soybean protein having a number average molecular weight of 600 (18% as a stoichiometric mole number obtained by measurement of amino nitrogen). 4 mmol) was adjusted to pH 10.2 with an aqueous solution of sodium hydroxide, and 2.2 g (7.5 mmol) of N, N'-dicarboxyanhydrocystine anhydride prepared in Reference Example 2 was added to this solution under ice-cooling. , 0.8 equivalent to the hydrolyzed soybean protein) in 40 ml of ethyl acetate was added, mixed by stirring, and allowed to react with stirring for 3 hours. During this time, the pH of the reaction solution was maintained at 10.0 to 10.5 by adding an aqueous sodium hydroxide solution.

After completion of the reaction, the reaction product was washed three times with 80 ml of n-hexane to remove unreacted materials, and then concentrated sulfuric acid was added to the aqueous layer to adjust the pH to 4, followed by decarbonation under reduced pressure. And adjust the concentration to adjust the cystine-introduced hydrolyzed soy protein
42.8 g of a 0% aqueous solution was obtained.

A part of the cystine-introduced hydrolyzed soybean protein obtained as described above was completely hydrolyzed with 6N hydrochloric acid for 20 hours, and then subjected to amino acid analysis with an amino acid autoanalyzer. As a result, 6.1 mol% as half cystine was obtained. Was detected. When a part of the cystine-introduced hydrolyzed soybean protein obtained as described above was subjected to amino acid analysis without hydrolysis with hydrochloric acid, no cystine was detected, and all of the cystine detected above was hydrolyzed. It was found to be bound to soy protein.

Since the starting material hydrolyzed soybean protein contained 0.8 mol% of cystine, it was detected as 6.1.
It was clear that 5.3 mol% of the mol% cystine was introduced into the hydrolyzed soybean protein by the cystine introduction method described above.

Production Example 5 (Production Example of Cystine-Introduced Hydrolyzed Yeast Protein) In place of hydrolyzed soybean protein, 50 g of a 30% aqueous solution of hydrolyzed yeast protein having a number average molecular weight of 450 (stoichiometric amount obtained by measurement of amino nitrogen) 3 as the theoretical number of moles
0.3 mmol) and N, N 'produced in Reference Example 2 above.
-3.1 g of dicarboxy-anhydrocystine (10.5 mmol, 0.7 equivalent to hydrolyzed yeast protein)
38.4 g of a 30% aqueous solution of cystine-introduced hydrolyzed yeast protein was obtained in the same manner as in Production Example 4 except that a solution dissolved in ml of ethyl acetate was used.

A part of the cystine-introduced hydrolyzed yeast protein obtained as described above was completely hydrolyzed with 6N hydrochloric acid for 20 hours, and then subjected to amino acid analysis with an amino acid autoanalyzer. Was detected. When a part of the cystine-introduced hydrolyzed yeast protein obtained as described above was subjected to amino acid analysis without hydrolysis with hydrochloric acid, no cystine was detected, and all of the cystine detected above was hydrolyzed. It was revealed that it was bound to yeast protein.

Since the hydrolysis yeast protein as a raw material contained 0.2 mol% of cystine, it was detected at 5.3.
It was clear that 5.1 mol% of the mol% cystine was introduced into the hydrolyzed yeast protein by the cystine introduction method described above.

Production Example 6 (Production example of cystine-introduced hydrolyzed casein) Instead of hydrolyzed soybean protein, 50 g of a 30% aqueous solution of hydrolyzed casein having a number average molecular weight of 700 (stoichiometric amount obtained by measurement of amino nitrogen) 20.4 as moles
Mmol) and 2.5 g (8.5 mmol, 0.8 equivalent to hydrolyzed casein) of N, N′-dicarboxyanhydrous cystine prepared in Reference Example 2 were dissolved in 70 ml of ethyl acetate. Except for using it, 39.5 g of 30% aqueous solution of cystine-introduced hydrolyzed casein was obtained in the same manner as in Production Example 4.

A part of the cystine-introduced hydrolyzed casein obtained as described above was completely hydrolyzed with 6N hydrochloric acid for 20 hours, and then subjected to amino acid analysis with an amino acid autoanalyzer. As a result, 6.2 mol% of half cystine was obtained. was detected. Further, when a part of the cystine-introduced hydrolyzed casein obtained as described above was subjected to amino acid analysis without performing hydrolysis with hydrochloric acid, cystine was not detected.
It was revealed that all the cystine detected above were bound to hydrolyzed casein.

0.6 mol% in the hydrolyzed casein as a raw material
It was clear that 5.6 mol% of the detected 6.2 mol% cystine was introduced into the hydrolyzed casein by the cystine introduction method described above.

Production Example 7 (Production example of cystine-introduced corn protein) In place of hydrolyzed soybean protein, 50 g of a 30% aqueous solution of hydrolyzed corn protein having a number average molecular weight of 350 (stoichiometric amount obtained by measurement of amino nitrogen) The number of moles is 42.8 mmol) and 4.3 g of N, N'-dicarboxyanhydrocystine anhydride prepared in Reference Example 2 (14.
7 mmol, 0.7 equivalent to the hydrolyzed corn protein) in 80 ml of ethyl acetate was used, except that a 30% aqueous solution of cystine-introduced hydrolyzed corn protein was added in the same manner as in Production Example 4. .5
g was obtained.

A part of the cystine-introduced hydrolyzed corn protein obtained as described above was completely hydrolyzed with 6N hydrochloric acid for 20 hours, and then subjected to amino acid analysis with an amino acid autoanalyzer.
Mole% was detected. Further, a part of the cystine-introduced hydrolyzed corn protein obtained as described above,
Amino acid analysis without hydrolysis with hydrochloric acid revealed no cystine, indicating that all of the detected cystine were bound to the hydrolyzed corn protein.

Since the hydrolyzed corn protein as a raw material contained 1.4 mol% of cystine, 5.7 mol% of the detected 7.1 mol% of cystine was hydrolyzed by the cystine introduction method described above. It was clear that it had been introduced into the corn protein.

[Tensile strength test of hair] The major axis and the minor axis of the part where the tensile strength of the hair is measured (the central part of the hair of 18 cm in the example) are measured with a micrometer, and the cross-sectional area is calculated. Next, 0.5m before and after the point
At intervals of m, an adhesive tape (Scotch filament tape, manufactured by Sumitomo 3M Limited) is fixed to the hair. The part to which this tape is fixed is fixed to a clamp of a tensile tester (Rheometer manufactured by Fudo Kogyo Co., Ltd.), the strength of the hair at the time of cutting is measured, and the tension per cross-sectional area is calculated from the cross-sectional area obtained previously. The strength (kgf / mm ² ) is calculated. Measure the tensile strength of 30 hairs per sample,
An average value is determined for each sample, and the results are shown by the average value.

[Amount of cysteic acid in hair] Hair 0.01
2 g of 6N hydrochloric acid is added to the resulting mixture, and the mixture is completely hydrolyzed at 105 ° C. for 20 hours. The amount of cysteic acid (μmol / g) is determined by an automatic amino acid analyzer. The amount of cysteic acid in the hair indicates the degree of damage to the hair, and the smaller the value, the less damage to the hair.

Example 1 and Comparative Examples 1-2 A hair protectant having the composition shown in Table 1 was prepared, and hair treated with each hair protectant was subjected to permanent waving using a separately prepared permanent waving agent. , Sensory evaluation of the gloss, moisture, combability of the treated hair,
Furthermore, the tensile strength of the hair and the amount of cysteic acid in the hair were examined.

In Example 1, a cystine-introduced hydrolyzed collagen (number-average molecular weight of 1,000) having 10.64 mol% of cystine produced by the amino acid analysis was used as a cystine-introduced peptide in the amino acid analysis. In Example 1, hydrolyzed collagen having a number average molecular weight of 1,000 was used instead of cystine-introduced hydrolyzed collagen, and in Comparative Example 2, cystine-introduced hydrolyzed collagen or hydrolyzed collagen was not used at all.

In the examples and comparative examples, the amounts of the respective components are not expressed by the content in the hair protection agent after preparation but by the expression of the amount of compounding in relation to the preparation of the hair protection agent. The amount of each component in the table is based on parts by weight, and when the amount is not a solid content, the solid content concentration is indicated in parentheses after the component name. These are the same in the following examples.

[0076]

[Table 1]

In the treatment with the hair protecting agent, a hair bundle having a weight of 1 g and a length of 18 cm was prepared for each of the examples and comparative examples, and the hair bundle was treated with the hair protectors of Example 1 and Comparative Examples 1-2. After immersing in 20 g of each agent for 10 minutes and rinsing, the first permanent wave composition having the composition shown in Table 2 below is used.
It was immersed in 20 g of the agent for 15 minutes. After rinsing, it was immersed in 20 g of the second permanent wave agent for 15 minutes, rinsed, and then dried with a hair dryer.

[0078]

[Table 2]

The gloss, moisture and combability of the dried hair were evaluated by ten panelists (seven women and three men) on a 5-point scale according to the following evaluation criteria.

Evaluation Criteria 5: Very Good 4: Good 3: Somewhat Good 2: Bad 1: Very Bad

Next, each hair bundle after the sensory evaluation was subjected to a tensile strength test, and 40 hairs were measured 9 cm from the end.
Was measured, and five hairs each from the larger and smaller cross-sectional areas were excluded from the test, and the tensile strength of the remaining 30 hairs was measured. Further, a part of the hair after the permanent wave treatment was hydrolyzed with hydrochloric acid, and the amount of cysteic acid was measured. The results (average value)
Are shown in Table 3.

[0082]

[Table 3]

As shown in Table 3, the hair treated with the hair protectant of Example 1 containing the cystine-introduced hydrolyzed collagen and then subjected to the permanent wave treatment was treated with any of the gloss, moisture and combability of the treated hair. The evaluation value is higher than that of the hair subjected to permanent wave treatment after treatment with the hair protectants of Comparative Examples 1 and 2, and the tensile strength of the hair is large, the amount of cysteic acid in the hair is small, and the cystine-introduced hydrolyzed collagen is It was found to sorb well to the hair, prevent damage to the hair during permanent wave treatment, and increase the tensile strength of the hair.

On the other hand, the hair which was treated with the hair protectant of Comparative Example 1 containing hydrolyzed collagen and then subjected to permanent wave treatment also had the hair of Comparative Example 2 containing no cystine-introduced hydrolyzed collagen or hydrolyzed collagen. Compared to the hair treated with the hair protectant and subjected to permanent wave treatment, the sensory evaluation value is higher, the tensile strength of the hair is higher, the amount of cysteic acid in the hair is smaller, and the hydrolyzed collagen is slightly sorbed on the hair. Expresses,
The effect was lower than that of the hair protectant of Example 1.
From these results, it is considered that the cystine-introduced hydrolyzed collagen used in Example 1 was more sorbed to the hair by the action of the cystine.

Example 2 and Comparative Examples 3 to 4 Hair protectants having the compositions shown in Table 4 were prepared, and hair treated with each of the hair protectants was dyed with an separately prepared oxidative hair dye, and then dyed. The gloss, moisturization and combability of the treated hair were sensory evaluated, and the tensile strength of the hair and the amount of cysteic acid in the hair were examined.

In Example 2, a hydrolyzed cystine-introduced wheat protein (number-average molecular weight of 1500) having a cystine content of 5.9 mol% as a half cystine in amino acid analysis prepared in Production Example 2 was used as the cystine-introduced peptide.
In Comparative Example 3, a hydrolyzed wheat protein having a number average molecular weight of 1500 was used instead of the cystine-introduced hydrolyzed wheat protein, and in Comparative Example 4, no cystine-introduced hydrolyzed wheat protein or hydrolyzed wheat protein was used at all.

[0087]

[Table 4]

In the treatment with the hair protectant, a hair bundle having a weight of 1 g and a length of 18 cm was prepared for each of the examples and comparative examples, and the hair bundle was treated with the hair protectors of Example 2 and Comparative Examples 3 and 4. Each of them was immersed in 20 g of each agent for 15 minutes, rinsed and then dyed with a hair dye having the composition shown in Table 5 below.

[0089]

[Table 5]

In the hair dyeing treatment, the first agent and the second agent are mixed in equal amounts, and 2 g of the mixture is applied to the hair tresses treated with the respective hair protectants, left for 20 minutes, rinsed with hot water, Then, the reaction was carried out by washing with a 2% aqueous solution of polyoxyethylene nonylphenyl ether. After the hair dyeing treatment, the hair bundle was dried with a dryer, and the leveling properties after hair dyeing, the moisture of the hair, the gloss, and the combability were evaluated according to the same evaluation criteria as in Example 1. Further, each hair bundle after the sensory evaluation was subjected to a tensile strength test, and for 40 hairs, the cross-sectional area of a portion 9 cm from the end was measured, and 5 hairs each from the larger and smaller cross-sectional areas were measured. Was excluded from the test, and the tensile strength of the remaining 30 hairs was measured. Also,
A part of the hair after the permanent wave treatment was hydrolyzed with hydrochloric acid, and the amount of cysteic acid was measured. Table 6 shows the results (average values).

[0091]

[Table 6]

As shown in Table 6, the hair treated with the hair protectant of Example 2 containing the cystine-introduced hydrolyzed wheat protein and then treated with the hair protectant of Comparative Examples 3 and 4 was treated. The leveling property was much better than the hair dyed and treated. The leveling property by the hair dyeing treatment reflects the degree of damage to the hair during the hair dyeing treatment.
This shows that the hair treated with the hair protectant had the least damage by the hair dyeing treatment.

Regarding the gloss, moisture and combability of the hair after the hair dyeing treatment, the hair treated with the hair protecting agent of Example 2 and then treated with the hair protecting agent of Comparative Examples 3 and 4 The evaluation value is higher and the tensile strength of the hair is higher, the cysteic acid content in the hair is lower, and the cystine-introduced hydrolyzed wheat protein is well sorbed on the hair, It has been shown that hair damage during hair dyeing treatment is prevented and the tensile strength of hair is increased.

Examples 3 to 5 and Comparative Example 5 Hair protection agents having the compositions shown in Table 7 were prepared, and the hair was decolorized with a solution in which each hair protection agent was mixed with a separately prepared decolorizing agent. The gloss, moistness, smoothness and combability of the hair were sensory evaluated, and the tensile strength of the hair and the amount of cysteic acid in the hair were examined.

In Example 3, cystine-introduced hydrolyzed silk (number-average molecular weight 700) was used as the cystine-introduced peptide, in which the amount of cystine produced in Preparation Example 3 was 6.2 mol% as half cystine in amino acid analysis. Example 4
In Example 5, a cystine-introduced hydrolyzed soybean protein (number-average molecular weight: 1200) having 6.1 mol% of cystine produced by the amino acid analysis was used as the cystine-introduced peptide in the amino acid analysis in Example 4; As the introduced peptide, a cystine-introduced yeast protein (number-average molecular weight: 1000) having a cystine content of 5.3 mol% and a half-cystine produced by the amino acid analysis was used in Comparative Example 5; No degraded peptides were used.

[0096]

[Table 7]

In each of Examples 3 to 5 and Comparative Example 5, a hair bundle having a weight of 1 g and a length of 18 cm was prepared by combining 20 g of each of the hair treating agents of Examples 3 to 5 and Comparative Example 5 with the composition shown in Table 8 below. After being immersed in a mixed solution with 80 g of the decolorizing agent for 30 minutes, it was rinsed, dried with a drier, and evaluated by 10 panelists according to the same evaluation criteria as in Example 1. Also,
The tensile strength of the hair and the amount of cysteic acid in the hair were examined. Table 9 shows the results (average values).

[0098]

[Table 8]

[0099]

[Table 9]

As is clear from the results shown in Table 9, the hair treated with the decolorizing solution obtained by adding the hair protecting agent of Examples 3 to 5 containing the cystine-introduced hydrolyzing peptide to the decolorizing agent was as follows:
Compared to the hair treated with the decolorizing solution obtained by adding the hair protecting agent of Comparative Example 5 to the decolorizing agent, the gloss, moisture, smoothness, and combability of the hair are all higher in evaluation value and the tensile strength of the hair is higher. It has been shown that the amount of cysteic acid in the hair is low, the cystine-introduced hydrolyzed peptide sorbs well to the hair, prevents damage to the hair during the decolorization treatment, and increases the tensile strength of the hair.

Further, among the hair protectants of Examples 3 to 5 containing the cystine-introduced hydrolyzed peptide, the hair treated with the hair protectant of Example 3 containing the cystine-introduced hydrolyzed silk had gloss, comb, etc. The hydrolyzed silk forms a denser film than the hair treated with the hair protectant of the other examples, and has a good appearance, and the moisturized cystine-introduced hydrolyzed soybean protein derived from a plant protein hydrolyzate. The best hair-protecting agent of Example 4 containing liposomes is the best, and the smoothness is better for the hair-protecting agent of Example 5 containing cystine-introduced hydrolyzing yeast protein, and the properties of the hydrolyzed peptide of each raw material are well exhibited. It was found that each hydrolyzed peptide was well sorbed to the hair by the action of the introduced cystine.

Examples 6 to 7 and Comparative Example 6 A hair protectant having the composition shown in Table 10 and having a function as a hair treatment rinse was prepared, and the hair washed with a separately prepared shampoo was treated and rinsed with water. Dried with a dryer. After repeating this operation 20 times, the gloss, moistness, smoothness and combability of the hair were sensory evaluated, and the tensile strength of the hair and the amount of cysteic acid in the hair were examined.

In Example 6, cystine-introduced hydrolyzed casein (number-average molecular weight of about 1500) was used as the cystine-introduced peptide, in which the amount of cystine produced in Production Example 6 was 6.2 mol% as half cystine in amino acid analysis. In Example 7, as a cystine-introduced peptide, a cystine-introduced hydrolyzed corn protein (number-average molecular weight of about 800) containing 7.1 mol% of cystine produced in Production Example 7 and analyzed by amino acid analysis as half cystine was used as a cystine-introduced peptide. Did not use any cystine-introduced peptide or hydrolyzed peptide.

[0104]

[Table 10]

In Examples 6 to 7 and Comparative Example 6, hair bundles weighing 1 g and having a length of 18 cm were prepared for each of Examples 6 to 7 and Comparative Example 6, and washed with a shampoo having the composition shown in Table 11. Then, after rinsing with hot water, 2 g of each of the hair protectants of Examples 6 to 7 and Comparative Example 6 was applied to each hair bundle, rinsed with hot water and dried with a hair dryer. This operation was repeated 20 times for each hair bundle, and the gloss, moisture, smoothness, and combability of the treated hair were evaluated by 10 panelists according to the same evaluation criteria as in Example 1. Furthermore, the tensile strength of the hair and the amount of cysteic acid in the hair were examined. Table 12 shows the results (average values).

[0106]

[Table 11]

[0107]

[Table 12]

As is clear from the results shown in Table 12, the hair treated with the hair protectants of Examples 6 to 7 containing the cystine-introduced hydrolyzed peptide was compared with the hair treated with the hair protectant of Comparative Example 6. , Hair gloss, moisture, smoothness,
The evaluation value was high in all of the combability. In particular, the hair treated with the hair protecting agent of Example 7 containing the cystine-introduced hydrolyzed corn protein in which cystine is introduced into the hydrolyzed corn protein that forms a glossy film has excellent gloss and moist feeling (moistness). The hair treated with the hair protectant of Example 6 containing cystine-introduced hydrolyzed casein in which cystine was introduced into hydrolyzed casein having a high effect of imparting sensation had an excellent moist feeling.

Further, regarding the tensile strength and the amount of cysteic acid of the hair, the degree of damage to the hair is lower in the shampoo treatment than in the permanent wave treatment or the decolorization treatment.
Although the difference between Examples 6-7 and Comparative Example 6 is not so large, the hair treated with the hair protectant of Example 6 or 7 is still less than the hair treated with the hair protectant of Comparative Example 6. It has been shown that the tensile strength of the hair is high, the amount of cysteic acid in the hair is low, and the cystine-introduced hydrolyzed peptide sorbs well to the hair, preventing damage to the hair and increasing the tensile strength of the hair. Was. Of course, the cystine-introduced peptide did not reduce the function as a hair treatment rinse.

──────────────────────────────────────────────────続 き Continued on the front page (51) Int.Cl. ⁶ Identification code FI A61K 7/135 A61K 7/135 (72) Inventor Aie Matsukawa 1-2-14 Fukuichicho, Higashiosaka-shi, Osaka Co., Ltd. Seiwa Kaseinai

Claims (2)

[Claims] 1. A hydrolyzed peptide or a derivative thereof obtained by hydrolyzing a protein derived from a natural product such as an animal, a plant or a microorganism in water or a base containing water as a main component. Or a hair protecting agent comprising a cystine-introduced peptide into which cystine has been introduced by an amide bond between an amino group of the derivative thereof and a carboxyl group of cystine. 2. The cystine-introduced peptide content of 0.1
The hair protective agent according to claim 1, wherein the amount is from 20 to 20% by weight.