JPS6169716A - First agent for permanent wave - Google Patents

Abstract

PURPOSE:The titled first agent having a low bad smell, high stability, providing the hair with neither damage nor a feeling of physical disorder, obtained by blending thiomalic acid of a reducing agent with a specific animal protein hydrolyzate, and its derivative. CONSTITUTION:2-12wt% thiomalic acid shown by the formula I is blended with 0.1-5wt% at least one of an animal protein hydrolyzate shown by the formula II (R1 is side chain of amino acid constituting animal protein hydrolyzate; n is 3-20 integer), formula III (R2 is 8-20C long-chain alkyl, or alkenyl; M is H, Na, ammonium, etc.) or formula IV, and its derivative. Thiomalic acid has a low bad smell, improved safety, and reducing action, but provides the hair with damage and a feeling of physical disorder. The agent can prevents the damage and feeling of physical disorder by blending thiomalic acid with the compound shown by the formula II-formula IV.

Description

DETAILED DESCRIPTION OF THE INVENTION [Industrial Field of Application] The present invention relates to a novel first agent for permanent waving that can impart excellent waving effects without damaging the hair or scalp.

[Conventional technology]

Conventional permanent waving agents are made by adding basic substances such as ammonia, monoethanolamine, and triethanolamine to an aqueous solution containing a reducing agent such as thioglycolic acid and cysteine as the main ingredient to adjust the pH to 8 to 10. The first agent is an aqueous solution of an oxidizing agent such as sodium acetate or hydrogen peroxide as the second agent.

The mechanism of waving hair with this permanent waving agent is to fix the hair to a rod, curl it, and use the first agent to reductively cleave the disulfide bonds of nostine contained in the keratin protein in the hair. The purpose is to generate mercapto groups using the second agent, and oxidize the mercapto groups using the second agent to generate new disulfide bonds in the hair, thereby fixing the waves.

However, in permanent waving using such conventional agents, it has been recognized that hair is damaged depending on the degree of waving effect. but,
(The oxidation with the second agent does not necessarily completely restore the disulfide bond and regenerate the nostin, and some of the mercapto groups generated from the nostin by the treatment with the first agent are excessive due to the second agent.) It undergoes oxidation or reacts with the mercapto group of thioglycolic acid or cysteine remaining in the hair to form a disulfide bond.Mainly due to these side reactions, a part of the keratin protein is separated by /8, The remaining portion of the hair also undergoes physical and chemical changes, which not only gives the hair a strange and dry feel (but also causes significant damage to the hair).

Therefore, the present inventors have conducted various studies in order to prevent hair damage and discomfort caused by permanent wave treatment, and have found that animal protein hydrolysates or derivatives thereof are used in combination with reducing agents such as thioglycolic acid and cysteine. Therefore, we developed a first agent for permanent waving that can provide excellent waving effects without damaging the hair or scalp, and have already filed a patent application for this (for example, Japanese Patent Application No. 100240/1982).

[Problem that the invention seeks to solve]

However, thioglycolic acid, cysteine, and the like have unpleasant odors and are easily oxidized, so they pose problems in handling and storage, and cannot be said to be fully satisfactory.

[Means for solving problems]

In order to solve the above-mentioned problems, the inventors of the present invention have made an effort to solve the above-mentioned problems. :r,
As a result of repeated research, thiomalic acid was used as a reducing agent for the first agent for permanent waves, and this thiomalic acid was used to produce animal protein hydrolysates and derivatives thereof shown in the following [1] to [3] ■ General formula 〇 ) H-+NH-CH-CO? rOH(+) (wherein R1 is the amino acid (Rule 11) constituting the animal protein hydrolyzate
4 and n is an integer from 3 to 2o)■ General formula (■) (wherein, R1 and n have the same meanings as above, and R1 is animal protein It is the side chain of the amino acid that makes up the hydrolyzate,
n is an integer from 3 to 20. R2 is a long-chain alkyl group or alkenyl group having 8 to 20 carbon atoms, and M is hydrogen, an alkali metal such as sodium or potassium, ammonium, or monoethanolamine, jetanolamine, triethanolamine, 2-amino-2- Methyl-1,3
- an anhydride of an animal protein hydrolyzate or a salt thereof represented by the formula (I [l) H3 (wherein R1 and n have the same meanings as above) , R1 is the side chain of an amino acid constituting the animal protein hydrolyzate,
n is an integer from 3 to 20), the above-mentioned problems are solved and It was discovered that a first agent for permanent waving that can give an excellent waving effect without damaging the hair or scalp can be obtained, and the present invention was completed.

The thiomalic acid used in the present invention is shown by the following structural formula, and many of the mercapto compounds used as the main ingredient of the first agent for permanent waving, including HOOC-CH2-CH-COOH H thioglycolic acid, have a bad odor. However, thiomalic acid has a melting point of 15
It is a white crystalline powder with a temperature of 0 to 155°C (in the case of 61 bodies),
It has little odor and has excellent stability. In addition, since 61 units of this thiomalic acid are industrially mass-produced,
Usually d7! Six bodies, one body, or a mixture of six bodies and two bodies may be used.

Thiomalic acid, like thioglycolic acid and nosteine, has a reducing effect and cuts the disulfide bonds in the hair, but in doing so, it causes damage and discomfort to the hair, similar to the conventionally used thioglycolic acid. give a feeling. Therefore, in the present invention, the above-mentioned animal protein hydrolyzate or animal protein hydrolyzate derivative is used in combination with this thiomalic acid,
While utilizing the excellent reducing effect of thiomalic acid to give hair permanent waves, the above-mentioned animal protein hydrolyzate or animal protein hydrolyzate derivative can be used to prevent hair damage and discomfort caused by the use of thiomalic acid. It is to prevent it.

When the first agent for permanent waving of the present invention is applied to hair, the hair is reduced by thiomalic acid and by the action of the alkali or protein denaturant such as urea or lithium bromide contained in the first agent. The disulfide bonds of cystine are broken and the tissue swells. At this time, the animal protein hydrolyzate or its derivatives penetrate into the hair and are absorbed into the hair tissue. The animal protein hydrolyzate or its derivatives absorbed into the body have a polypeptide structure similar to the keratin protein of hair, so they contain acidic amino acids such as glutamic acid and aspartic acid, and arginine, lysine, and histidine, which both have. Bonds are formed with the hair tissue through ionic bonds between side chains with basic amino acids, hydrogen bonds between peptide chains, and van der Waalska bonds between side chains of water-based amino acids. It will not be washed away easily. The animal protein hydrolyzate or its derivative absorbed into the hair in this way strengthens the hair, and also prevents hair damage caused by permanent waving. As a result, the hair treated with this permanent wave first agent has the natural luster of the hair, and of course also has a waving effect.
It is also characterized by excellent retention properties. Chemically, when hair is permanently waved, some of the cysteine in the hair tissue produced by reduction becomes cystic acid, so when amino acid analysis of the hair tissue is performed, cystine decreases and cystic acid increases. is recognized. This decrease in cystine and increase in cystic acid in the hair & Il weave indicates the degree of hair damage, but when the first agent of the present invention is used for permanent waving, compared to using only a reducing agent alone. As a result, cystine decreases less and cystic acid increases less. In particular, keratin protein containing cystine as its constituent amino acid is used as a raw material for the animal protein hydrolyzate or its derivatives to be blended into the first agent for permanent waves of the present invention, and cystine is chemically decomposed as a hydrolysis method. When a keratin hydrolyzate or a derivative thereof is obtained using a hydrolysis method using an acid or an enzyme that can be hydrolyzed without oxidation, and is added to the first agent, the hydrolyzate or derivative thereof contains After the cystine contained in the hair is reduced in the same way as the cystine in the hair, disulfide bonds are formed with each other by the subsequent action of the second agent, so that it is absorbed into the hair & TLSH, and the reduction of cystine in the hair due to permanent treatment and cystic acid. It has an excellent effect of preventing the increase in

When preparing the first agent, the thiomalic acid can be used after being dissolved in a solvent such as water, alcohol, or ether, if necessary. Furthermore, like conventionally used thioglycolic acid, thiomalic acid can also be used in the form of its ammonium salt, sodium salt, potassium salt, etc., and the use of these thiomalic acid salts is also within the scope of the present invention. It is included in

The animal protein hydrolyzate used in the present invention is obtained by hydrolyzing animal proteins such as collagen, keratin, and silk with acid, alkali, or enzyme, and its derivatives are obtained as described above. It is derived by performing various reactions on animal protein hydrolysates. The preparation methods thereof will be explained below.

1. Animal protein hydrolyzate Animal protein hydrolyzate is obtained by hydrolyzing animal proteins such as collagen, keratin, and silk protein using acid, alkali, or proteolytic enzyme. During hydrolysis, acids, alkalis,
Alternatively, by appropriately selecting the amount of 141 g, reaction temperature, and reaction time, the value of n of the obtained animal protein hydrolyzate can be adjusted to 3 to 20, that is, the molecular weight is approximately 300 to approximately 2.0.
00 preferred.

Raw animal proteins include collagen, keratin,
Examples include silk protein, elastin, actin, and myosin. All of these are extremely thick animal proteins, and unlike vegetable proteins, they do not suffer from impurities such as carbohydrates and lipids, and can be obtained in large quantities.

The animal protein hydrolysates derived from these raw materials have the property of adsorbing to hair, and are useful as safe cosmetic raw materials derived from natural products to prevent hair damage, restore hair damage, and improve skin ffi. It is used to prevent denaturation of skin proteins caused by surfactants.

Raw materials such as collagen include animal skin, animal skin, bone, etc., and it is convenient to use gelatin, which is an extract of these collagens. Gelatin has shapes such as powder, plate, and granules, but all of them dissolve easily in hot water.
There are also few impurities.

Examples of raw material keratin include animal hair, hair, feathers,
Examples include nails, horns, hooves, scales, etc., but especially wool, hair,
Feathers are preferred. These keratins can be subjected to hydrolysis as they are, but if necessary, they may be cut or crushed into appropriate sizes, or pretreated such as washing, degreasing, and high-temperature pressure treatment. .

The raw material -H protein is silkworm cocoon.
, duvet thread, string cloth, etc., but since no particular processing is required, it is economically advantageous to use silkworm cocoons, cotton-like or coarse thread-like materials before spinning. As with keratin, which is the same fibrous protein, it may be cut or crushed into appropriate sizes, washed, or subjected to high-temperature pressure treatment depending on the four requirements. , halogenated alkali metal salts or alkaline earth metal salts can be dissolved into highly concentrated aqueous droplets of 40% by weight or more,
It is also possible to dissolve it in a liquid and perform hydrolysis on the dissolved liquid.

In addition, elastin, a protein that exists in the skin along with collagen and is known to give skin elasticity, and muscle proteins actin and myosin can also be used.

Acid hydrolysis, alkaline hydrolysis, and enzymatic hydrolysis of animal proteins are carried out as follows.

Examples of the hydrolyzing acid by ill rll include non-TA acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, and hydrochloric acid, and organic acids such as acetic acid and formic acid. Alternatively, a mixture of hydrochloric acid and acetic acid may be used.
These are generally used at a concentration of 5 to 85ii1%, but it is desirable to ensure that the hydrolysis reaction is always at pH 4 or below. The reaction temperature is preferably 40 to 100°C, but under pressure 1
The temperature can be raised to 60°C. The suitable reaction time is 2 to 24 hours. The reactant can be neutralized with an alkali such as sodium hydroxide, calcium hydroxide, or sodium carbonate and used as is, but the reactant or neutral gel filtration of the compound,
It can also be used after being purified by ion exchange resin, ultrafiltration, dialysis, electrodialysis, etc.

(2) Hydrolysis with alkali Examples of alkali include sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate,
Inorganic alkalis such as potassium carbonate and lithium carbonate are used. A concentration of 1 to 20% by weight is generally suitable for these. If more alkali is used than necessary, the hue of the hydrolyzate solution will turn brown to black, so it is preferable to carry out the undesirable 0 reaction at a temperature of room temperature to 100°C for 30 minutes to 24 hours, and avoid raising the temperature more than necessary. Be careful not to overdo it or prolong the reaction time! After the necessary reaction, it is preferable to neutralize with the above-mentioned acid or purify by gel filtration, ion exchange resin, ultrafiltration, dialysis, electrodialysis, etc.

(3) As enzymatic hydrolases, acidic proteolytic enzymes such as pepsin, protase A, and protase B, and neutral proteolytic enzymes such as papain, promelain, molysin, trypsin, pronase, and chymotrypsin are used. Ru. Furthermore, neutral proteolytic proteins such as subtilin and staphylococcal protease can also be used. During hydrolysis, it is preferable to adjust the pH to a range of 1 to 4 for acidic proteins such as pepsin, and to a range of 4 to 10 for neutral proteolytic enzymes such as papain. pH is generally determined by acetic acid/sodium acetate buffer, phosphate@
Appropriately it! can be prepared using buffer solutions such as street solution, or by adding acids, alkalis, etc. The reaction temperature is preferably 30 to 45°C, and the reaction time is generally 3 to 24 hours.

In a hydrolysis reaction using an enzyme, the molecular weight of the hydrolyzate is greatly influenced by the amount of si used, reaction temperature, and reaction time. Therefore, in order to obtain an animal protein hydrolyzate with the desired molecular weight, the molecular weight distribution of the obtained hydrolyzate should be examined using the gel permeability method under various conditions such as the amount of enzyme used, reaction temperature, and reaction time. , it is necessary to empirically determine the Mt passing conditions.

Enzyme-based hydrolysates have a narrower molecular weight distribution and produce less free amino acids than acid- or alkali-based hydrolysates, so they are very suitable for use in cosmetic formulations.

The average molecular weight of the hydrolyzate obtained by these hydrolysis reactions is preferably 300 or more and 2,000 or less. This is because the adsorption ability of animal protein hydrolysates to hair is determined by its molecular weight, and the molecular weight is 300 to 2,000. 6
This is because those with a molecular weight of about 0.000 are the easiest to adsorb, dissolve in water, and are easy to handle, while those with a molecular weight of more than 2.000 have low adsorption to hair and are difficult to handle.

In addition, in the general formulas (+) to (m), the side chain is R1
Amino acids represented by are alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, lysine, aspartic acid,
asparagine, glutamic acid, glutamine, insulin,
stenoic acid, tryptophan, hydroquinoproline,
Examples include hydroxylysine. And, to give an example of the composition ratio (based on mol%) of these amino acids, the first
As shown in the table.

29 Physical properties Acylated product of protein hydrolyzate or its salt The most common method for unbinding the animal protein hydrolyzate obtained as described above is the Schotten-Baumann reaction (Schotten-Baumann reaction).
Mann reaction).

In this reaction, an acid chloride derivative of a higher fatty acid to be condensed is added to an aqueous solution of an animal protein hydrolyzate (8 to 10
It is a reaction in which the substance is added under alkaline conditions with stirring.
According to this reaction, as shown in the following equation, hydrochloric acid is produced and the pH decreases, so it is necessary to maintain the pH at 8 to 1o by adding an alkali such as sodium hydroxide or potassium hydroxide while adding acid chloride. a. The essential reaction time is 1 to 6 hours, and the reaction temperature is 0 to 60°C, preferably 20 to 40°C.

As the higher fatty acid side component, in addition to the above-mentioned acid chlorides, acid halides of higher fatty acids such as Br and 1 can be used. However, acid chlorides are the most common.

In addition, for commonly used fatty acids having 8 to 20 carbon atoms, in addition to the above-mentioned method using acid halides, it is possible to use animal protein hydrolysates and higher fatty acids or their methyl esters, ethyl esters, etc. at high temperatures of 150 to 200°C and under high pressure. A method in which a lower alcohol ester is treated and subjected to dehydration condensation or dealcoholization condensation can also be adopted, but since this method involves high temperature treatment, the product becomes colored and is not necessarily preferable.

Furthermore, it is also possible to use reagents used for peptide synthesis to convert higher fatty acids into carboxyl-activated derivatives such as N-oxysuccinimide ester and N-phthalimide ester, and then react them with animal protein hydrolyzate. However, in addition to being expensive, the reaction with acid halides does not have high reactivity.

In any case, the obtained acylated product is preferably released into an aqueous solution of a strong acid such as hydrochloric acid or ft acid, and the liberated product is collected as suspended sediment, which is purified by washing with water.
Either as it is or in the form of a neutralized salt, it can be dissolved in water or a solvent such as Flucol or propylene glycol to a desired depth (10 to 60% (wt%, the same applies hereinafter),
In particular, the progress and completion of the reaction of 20-409A), which is made into a solution or dried into a powder, is carried out using the Van 5lyke method to prepare amino acids in animal protein hydrolysates. Confirmed by measuring nitrogen content.

3 Quaternary trimethylammonium derivative of animal protein hydrolyzate Quaternary trimethylammonium derivative of animal protein hydrolyzate represented by general formula (m)
The class trimethylammonium derivative can be obtained by reacting the animal protein hydrolyzate obtained as described above with 3-chloro-2-hydroxypropyltrimethylammonium chloride.

3-chloro-2-hydroquinepropyltrimethylammonium chloride (hereinafter referred to as CTA) used in the above reaction
) is known as Existing Chemistry 1!1121-181, and water F4 liquid with a concentration of about 50% is commercially available and can be easily obtained.

The above reaction is carried out by dropping an aqueous solution of CTA into an aqueous solution of animal protein hydrolyzate and bringing the animal protein hydrolyzate and CTA into contact with each other in water. In particular, it is desirable to maintain the pH within the reaction system at a pH of 9 to 11. Therefore, during the 0 reaction, in which an alkaline aqueous solution such as sodium hydroxide or potassium hydroxide is added dropwise into the reaction solution as necessary, the pH within the reaction system should be maintained as above. In order for the amino groups of the animal protein hydrolyzate to react with CTA, it is preferable to keep the pH within the alkaline range of 8 or higher, and if the pH exceeds 12, CTA and animal protein hydrolyzate will react with each other. One reaction, which causes hydrolysis, proceeds even at room temperature, but the higher the temperature, the faster the reaction. However, when the pH is high and the temperature is high, the hydrolysis of animal protein hydrolysates and CTA is promoted, and only low molecular weight products can be obtained. If the concentration of aqueous protein hydrolyzate is high, the viscosity will increase and it will be difficult to achieve a uniform reaction, so it is preferable to make an aqueous solution with a concentration of about 30 to 50%.
A 0% aqueous solution may be used as is.

Adding CTA to animal protein hydrolyzate takes 30 minutes to 6 minutes.
When CTA is added dropwise, the reaction shown in the following formula proceeds, which preferably completes within a few hours, resulting in H3 H-+NH-CH-CO? Toe-H3 ■ Since hydrochloric acid is generated and the pH of the reaction solution decreases, it is preferable to drop the alkali simultaneously with the addition of CTA and stir to maintain the pH in the solution at a pH suitable for the reaction. After dropping the CTA, stirring is continued for about 2 to 6 hours, preferably for a period of at least 30 minutes, and
It is preferable to maintain the H at 9 to 11 and to complete the reaction by leaving the head for one day and night, or by heating it to about 60°C.The progress and completion of the reaction is carried out in the hydrolyzate using the Fanslake method. W is recognized by measuring the amino nitrogen of.

In the first agent for permanent waving of the present invention, the concentration of thiomalic acid is preferably in the range of 2 to 12%, and the animal protein hydrolyzate represented by general formulas (1) to (I), its acylated product, or its salt , or its quaternary trimethylammonium derivative is preferably in the range of 0.1 to 5% as a total concentration when used alone or in combination, and the remainder is water and the first agent for this type of permanent wave. Ammonia, which is usually added to
Monoethanolamine, jetanolamine, triethanolamine, alkalis such as sodium hydroxide and potassium hydroxide, carbonates such as ammonium carbonate, sodium carbonate, and sodium bicarbonate, and other anionic, cationic, nonionic, and amphoteric types. Substances include surfactants, emulsifiers, penetrants, hair nourishing agents, chelating agents, colorants, and fragrances. Note that animal protein hydrolysates, their acylated products, their salts, or their quaternary trimethylammonium derivatives are usually obtained in the form of aqueous solutions, but in this specification, all amounts are shown as solid content. ing.

In the first agent for permanent waving of the present invention, the concentration of thiomalic acid is set at 2 to 12% because if the concentration of thiomalic acid is less than 2%, a sufficient waving effect cannot be obtained.
Furthermore, if the concentration of thiomalic acid exceeds 12%, it may damage the hair and strongly irritate the eyes, scalp, and skin. The concentration of the animal protein hydrolyzate or its derivative represented by the general formula (+) to (ml) is set to 0.1 to 5% because the concentration of the animal protein hydrolyzate or its derivative is 0.1% to 5%. This is because if the amount is less than 1%, the effect of protecting the hair will not be sufficiently exhibited, and if it is more than 11%, there is a risk that the hair will have an unpleasant feeling such as a sticky feeling.

〔Example〕

Next, the first agent for permanent waving of the present invention will be explained with reference to reference examples and examples.

Reference example 1 Reference example IA for production of animal protein hydrolyzate
14 Examples of Production of Collagen Hydrolyzate IA-1 (rj11
Hydrolysis) Add 700 g of water to 300 g of powdered gelatin, melt while heating, add 60 g of salt at 70°C, and P! After hydrolysis was carried out for 1 hour with stirring, the reaction mixture was passed through the iI! The solution was diluted to 21% with water and neutralized by passing it through a 290 ml resin tower containing a weakly basic anion exchange resin Diaion WA20 (trade name, Mitsubishi Chemical Industries, Ltd.). After concentrating this under reduced pressure, i! ! The concentration is 40
% collagen hydrolyzate aqueous solution was obtained.

The molecular weight of the thus obtained collagen hydrolyzate was measured by a gel filtration method and found to be an average molecular weight of 900.

Reference Example 18-2 (Flukali Hydrolysis PR) While heating 700 g of 6% sodium hydroxide aqueous solution, 50 g of plate gelatin was added.
After 1 hour of hydrolysis with stirring at 80°C, the reaction mixture was filtered, the filtrate was diluted to 21% with water, and the weakly acidic cation exchange resin Amberlite IRC was dissolved.
-50 (trade name, Organo C Co., Ltd.)) was neutralized by passing it through a resin column at 500 mA. After concentrating this under reduced pressure, i! ! As a result, an aqueous solution of collagen hydrolyzate with a concentration of 35% was obtained. The molecular weight of the thus obtained collagen hydrolyzate was measured by a gel filtration method and found to be an average molecular weight of 500.

Reference Example IA-3 (Enzymatic Hydrolysis) Add 650 g of water to 350 g of granular gelatin, heat to 50°C to melt the gelatin, add 20 mg of neutral proteolytic enzyme papain, and add 350 g of water while stirring at 50°C. After hydrolysis for an hour, the reaction mixture was filtered and
A 5% collagen hydrolyzate aqueous solution was obtained. The molecular weight of the collagen hydrolyzate thus obtained was measured by gel filtration and found to be the average molecular weight! It was 1,700.

Reference example IB Production of keratin hydrolyzate Reference example IB-1
(Acid hydrolysis) = 450 g of 35% hydrochloric acid to 500 g of wool in 70 flasks
was added and hydrolysis was carried out under stirring at 80°C for 16 hours.

After hydrolysis, the reaction mixture was filtered and 1 [! Pour the solution into a weakly basic anion exchange resin Diaion WA20 (mentioned above) 1.
After neutralizing with 400 ml, the solution was concentrated and filtered to remove the ion exchange resin to obtain an aqueous solution of keratin hydrolyzate with a concentration of 40%. The molecular weight of the keratin hydrolyzate thus obtained was measured by gel filtration and found to be an average molecular weight of 800.

Reference example IB-2 (alkaline hydrolysis) 500 g of pig hair, 100 g of sodium hydroxide, and 3 kg of water
was added and left to stand at 40°C for 24 hours to perform hydrolysis, then the reaction mixture was filtered and the filtrate was mixed with 6 acid cation exchange resin Amberlite IRc-50 (mentioned above) 600rr+
7! It was neutralized by After concentrating this, the ion exchange resin was removed by force to obtain an aqueous solution of keratin hydrolyzate with a concentration of 40%. The molecular weight of the keratin hydrolyzate thus obtained was measured by gel filtration and found to have an average molecular weight of 1.200.

Reference Example IB-3 (enzymatic hydrolysis) 500 g of feathers was heated at 10 kg/cj at 200°C in a high-pressure container.
After being treated with superheated steam for 30 minutes, the feathers were discharged into the atmosphere to obtain porous puffed feathers. Add 3 kg of water to this,
30 g of papain was added and hydrolysis was carried out at 40° C. for 24 hours. After hydrolysis, the reaction mixture was filtered, and the filtrate was concentrated under reduced pressure to obtain a keratin hydrolyzate with a concentration of 40%. The molecular weight of the keratin hydrolyzate thus obtained was measured by gel filtration and found to be an average molecular weight of 600.

Reference Example IC Silk-covered white matter hydrolyzate Reference Example IC-1 (alkaline hydrolysis N) 21Pour 1.5 f of 2N sodium hydroxide into a beaker,
To this, add as much as possible of dried silkworm cocoon (pre-washed to remove silkworm feces and dirt), heat to 80℃, and dissolve the cocoon by hydrolysis while stirring. Then, add the remaining cocoon. After adding the whole cocoon for 30 minutes, keep at 80℃ for another 1 hour.
The reaction product, which had been hydrolyzed, was diluted by adding 11 parts of water, and then filtered under reduced pressure. 1
1! Exchange the solution with weakly acidic cations vA resin Amberlite IR
C-50 (mentioned above) was neutralized by passing it through a 1,300 ml resin tower, concentrated under reduced pressure, filtered,
An aqueous solution of silk protein hydrolyzate at 111 degrees and 30% was obtained.

The molecular weight of the silk protein hydrolyzate thus obtained was measured by gel filtration and found to be an average molecular weight of 500.

Reference Example IC-2 (Acid Hydrolysis) Commercially available 55% lithium bromide water f4 liquid 1. After adding 200 g of unspun silk fiber to Okg at 50° C. and dissolving it, the f4 liquid was diluted to 2.0 kg with ion-exchanged water. This liquid was heated to 80° C. and stirred in a 21-inch flask, and 25 g of concentrated hydrochloric acid was added thereto for 2 hours of hydrolysis. After neutralizing by adding 48 g of cooled I&20% aqueous sodium hydroxide solution, the mixture was filtered under reduced pressure. f! ? Electrodialysis was carried out to obtain a total protein hydrolyzate aqueous solution having a concentration of 35% by desalting, concentration under reduced pressure and filtration. The molecular weight of the total protein hydrolyzate thus obtained was measured by gel filtration and found to have an average molecular weight of 1,800.

Reference Example IC-3 (enzymatic hydrolysis) 300 g of a+ silkworm cocoon was placed in a high-pressure container to weigh 10 kg.
/cd, treated with superheated steam at 200°C for 1 hour to swell, and then placed in a container of 21 and 0. IN sodium acetate mild solution (pH 6) Ig was added, the temperature was raised to 40°C, and 2hg of papain, a neutral proteolytic enzyme, was added.

After filtration of the 0 reaction compound that was hydrolyzed at 40°C for 12 hours to remove undecomposed residues, the filtrate was concentrated under reduced pressure to a concentration of 3.
An aqueous solution of 0% total protein hydrolyzate was obtained. The molecular weight of the total protein hydrolyzate thus obtained was measured by gel filtration and found to have an average molecular weight of 1.050.

Reference Example 2 Production of acylated animal protein hydrolyzate or salt thereof Reference Example 2A Production of acylated collagen hydrolyzate or salt thereof Reference Example 2A-1 Acylated product of collagen hydrolyzate with myristic acid Reference Example IA 40 of the collagen hydrolyzate obtained in -1
% aqueous solution with stirring at a constant temperature of 35℃.
.

1.0 equivalents of the decomposed product) was added dropwise over 2 hours. Meanwhile, add 20% aqueous sodium hydroxide solution to pH 9,
It was kept at 5. After stirring at 35°C for 1 hour, the temperature was raised to 40°C and the reaction was completed by stirring for 1 hour.
The generated acylated product is suspended in a free form (the carboxylic acid of the peptide part of the acylated product is not a salt, but in the form of 1000H), then washed with water, and propylene glycol is added to dissolve it, resulting in collagen hydrolysis. 710 g of a 30% propylene glycol-water solution 11 of an acylated product with myristic acid was obtained. Note that the concentration of propylene glycol was 40%. The yield was 88%.

Regarding the 30% propylene glycol-aqueous solution of the obtained product, aminodeaftinol was measured by the Van Slake method and found to be 0.008 +ag/g. The 40% aqueous solution of the collagen hydrolyzate obtained in Reference Example LA-1 used as a raw material contained 15.5 amino-tinogens.
It was found that most of the amine groups in the product were acylated.

Reference Example 2A-2 2-Amino-2-methyl-1,3-propanediol salt of the collagen hydrolyzate obtained in Reference Example IA-2.
Using 500 g of % aqueous solution, stearic acid chloride 1 was used instead of myristic acid chloride in Reference Example 2A-1.
The product was washed with water in the same manner as in Reference Example 2A-1 except that 06 g (1.0 equivalent of collagen hydrolyzate) was used, and then 2-amino-2-methyl-1,3-propanediol was added. was added to neutralize the mixture to obtain 670 g of an aqueous solution of 2-methyl-1,3-propanediol salt of collagen hydrolyzate acylated with stearic acid at a concentration of 30%. The yield was 85%.

Amino nitrogen was measured using the Fanslake method in a 30% aqueous solution of the obtained product and found to be 0.017.
mg/g. Reference example IA- used as raw material
The 35% aqueous solution of collagen hydrolyzate obtained in step 2 contained 19.60 mg/g of aminodeaf nitrogen, indicating that most of the amino groups in the product were anolated.

Reference Example 2-3 Natrilam salt of acylated product of collagen hydrolyzate with lauric acid Reference Example 35 of collagen hydrolyzate obtained in IA-3
Using 500 g of % aqueous solution, lauric acid chloride 23 was used instead of myristic acid chloride in Reference Example 2A-1.
The product was washed with water in the same manner as in Reference Example 2A-1 except that 1.0 g (1.0 equivalent of collagen hydrolyzate) was used, and then a 30% aqueous sodium hydroxide solution was added to neutralize the product to a concentration of 30. % of the sodium salt of the acylated collagen hydrolyzate with lauric acid was obtained. Yield is 9
It was 6%.

Amino nitrogen was measured in a 30% aqueous solution of the obtained product by the Van Slake method, and it was found to be 0.01.
It was 0 mg/g. Reference example IA used as raw material
The 35% aqueous solution of collagen hydrolyzate obtained in -3 had an amino nitrogen content of 5.76 mg/g, indicating that most of the amino groups in the product were acylated.

Reference Example 2B Production of acylated product of keratin hydrolyzate or its salt Reference Example 2B-1 Triphenolamine salt of hepacylated product of keratin hydrolyzate with coconut fatty acid Reference Example 2B-1 Keratin hydrolyzate obtained in Reference Example IB-1 40% of
Add 55 g of coconut fatty acid (mixed fatty acids having 8 to 18 carbon atoms) chloride (
(1.0 equivalent of keratin hydrolyzate) was added dropwise over 2 hours. 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 was discharged from the reaction vessel into a 5% aqueous sulfuric acid solution 51, and the generated acylated product was suspended in a free form, washed with water, and neutralized by adding triethanolamine to obtain keratin with a concentration of 30%. Triethanolamine salt aqueous solution of hydrolyzed product acylated with coconut fatty acid 840
I got g. The yield was 97%.

Amino nitrogen was measured using the Fanslake method for the 30% water f4f& of the obtained product, and it was found to be 0.
It was 017 erg/g. The 40% aqueous solution of the keratin hydrolyzate obtained in Reference Example IB-1 used as a raw material contained 7.270 mg/g of amino-tinogen,
It was found that most of the 7-mino groups in the product were acylated.

Reference Example 2B-2 Monoethanolamine salt of acylated product of keratin hydrolyzate with caprylic acid Reference Example 140% of the keratin hydrolyzate obtained in B-2
Using 500 g of aqueous solution, 32 g of caprylic acid chloride was substituted for coconut fatty acid chloride in Reference Example 2B-1.
(1.0 equivalent of keratin hydrolyzate) was used in the same manner as Reference Example 2B-1 except that monoethanolamine was used instead of triethanolamine. 890 g of a 30% aqueous solution of ethanolamine salt was obtained. The yield was 98%.

Amino chinogen was measured by the Van Slake method on the suspended matter (dry residue: 37.20%) of the obtained product before neutralization with monoethanolamine, and it was found that 0.
．． It was 0.41 wag/g. The reason why amino nitrogen was measured on the sample before neutralization with monoethanolamine was because after neutralization, the amino group of monoethanolamine was measured, so it could not be used as a measurement sample for amino nitrogen. be. Reference example IB- used as raw material
The 40% aqueous solution of keratin hydrolyzate obtained in step 2 contained 4.729 mg/g of amino thiosine, indicating that most of the amino groups in the product were acylated.

Reference Example 2B-3 Acylation of keratin hydrolyzate with coconut fatty acid 73 g of coconut fatty acid chloride (keratin hydrolyzate) was added to 500 g of a 40% aqueous solution of the keratin hydrolyzate obtained in Reference Example IB-3 with stirring at a constant temperature of 30°C. 1.0 equivalent) was added dropwise over 2 hours. During that time, the pH was maintained at 9 by appropriately adding 20% potassium hydroxide solution F4. Another 30℃
After stirring for 1 hour, the temperature was raised to 40°C and stirring was continued for 1 hour to complete the reaction.

The reaction mixture was discharged from the reaction vessel into 5% sulfuric acid aqueous F4 solution 51, the generated acylated product was suspended in free form, the suspended matter was washed with water, and propylene glycol was added to dissolve it to obtain a ζkeratin hydrolyzate. 960 g of 25% propylene glycol-aqueous solution of acylated product with coconut fatty acids
I got it. Note that the concentration of propylene glycol was 40%. The yield was 96%.

When aminomyotinoline was measured by the Van Slake method in a 25% propylene glycol-aqueous solution of the obtained product, it was found to be 0.007 mg/l! Met. The 40% aqueous solution of the keratin hydrolyzate obtained in Reference Example IB-3 used as a raw material contained 9.220 amino thiosine.
mg/g, indicating that most of the 7-mino groups in the product were acylated.

Reference Example 2C Preparation of acylated product of pure protein hydrolyzate or its salt Reference Example 2C-1 Pure amount Potassium salt of acylated product with lauric acid of white matter hydrolysis Reference Example Pure protein hydrolyzate obtained in IC-1 30%
65.5 g of lauric acid chloride (1.0 g of pure protein hydrolyzate) was added to 500 g of aqueous solution and stirred at a constant temperature of 30℃.
equivalent amount) was added dropwise over 2 hours. During that time, the pH was maintained at 9 by appropriately adding a 20% aqueous sodium hydroxide solution. Another 1 hour at 30℃! ! After stirring for 11 minutes, the temperature was raised to 40°C and stirring was continued for 1 hour to complete the reaction.

The reaction mixture was discharged from the reaction vessel into a 5% aqueous sulfuric acid solution E51, and the produced acylated product was suspended in the shape of an amusement park.
The suspended matter was washed with water and then neutralized with a 30% aqueous potassium solution to obtain 232 g of a potassium salt aqueous solution of an acylated product of pure protein hydrolyzate with lauric acid having a concentration of 30%. The yield was 90%.

When the amino muscle nitrogen of a 30% aqueous solution of the obtained product was measured by the Fanslake method, it was found to be 0.009.
It was mg/g. Reference example IC- used as raw material
The 30% aqueous solution of pure protein hydrolyzate obtained in step 1 contained 16.8 mg/g of amino nitrogen, indicating that most of the amino groups in the product were anolated.

Reference Example 2C-2 Calirum salt of acylated product of pure protein hydrolyzate with undecylenic acid In place of the pure protein hydrolyzate obtained in Reference Example IC- in Reference Example 2C-1] Using 500 g of a 35% aqueous solution of pure protein hydrolyzate, undecylenic acid chloride 2 was added instead of lauric acid chloride.
0 g (1.0 equivalent of pure protein hydrolyzate) was used in the same manner as in Reference Example 2C-1, and 610 g of a potassium salt aqueous solution of acylated product of pure protein hydrolyzate with undecylenic acid at a concentration of 30% was prepared. Obtained. The yield was 93%.

Amino nitrogen was measured using the Fanslake method in a 30% aqueous solution of the obtained product and found to be 0.017.
It was mg/g. Reference example IC- used as raw material
The 35% aqueous solution of pure protein hydrolyzate obtained in step 2 contained 5.4 mg/g of amino nitrogen, indicating that most of the amino groups in the product were acylated.

Reference Example 2C-3 Triethanolamine salt of acylated product of pure protein hydrolyzate with isostearic acid In Reference Example 2C-1, instead of the pure protein hydrolyzate obtained in Reference Example IC-1, Reference Example IC-3 was used. Using 500 g of the obtained 30% aqueous solution of pure protein hydrolyzate, 43.2 g of isostearic acid chloride (1.0 equivalent of IM protein hydrolyzate) was added instead of lauric acid chloride.
A triethanolamine salt aqueous solution of an acylated product with isostearic acid of a pure protein hydrolyzate at a concentration of 30% was prepared in the same manner as in Reference Example 2C-1 except that triethanolamine was used instead of the 30% potassium hydroxide aqueous solution. 5
60 g was obtained, the yield was 92%.

Amino nitrogen was measured using the Fupnslake method in a 30% aqueous solution of the obtained product, and it was found to be 0.010.
It was mg/g. Reference example IC- used as raw material
The 30% aqueous solution of pure protein hydrolyzate obtained in step 3 had an amino nitrogen content of 9.33 g/g, indicating that most of the amino groups in the product were acylated.

Reference Example 3 Production of quaternary trimethylammonium derivative of animal protein hydrolyzate Reference Example 38 Production of quaternary trimethylammonium derivative of collagen hydrolyzate Reference Example 3A-1 Obtained in Reference Example 18-1 Collagen hydrolyzate 40
% aqueous solution 700 g (average molecular f1900 of collagen hydrolyzate, total 1310 mmol of amino acid)
was placed in a reaction vessel, and 103 g of the solution (equivalent to 0.9 g of collagen hydrolyzate) was added dropwise to CTA7 with a concentration of 51% over 30 minutes while stirring at 35°C.
% sodium hydroxide aqueous solution was added dropwise to adjust the pH of the reaction solution.
was maintained at 10.0. After dropping CTA, adjust the pH to 1.
Stirring was continued for 2 hours while maintaining the temperature at 0.0, and then after being left for 24 hours, the amino nitrogen was measured. The total amount of amino nitrogen was 42 mmol, and 84% of the amino nitrogen had reacted. Was. Next, add 1 of the weakly acidic cation exchange resin Amberlite IRc-50 (mentioned above) to the reaction solution.
70 ml was added, neutralized to pH 6.5, sodium ions in the reaction solution and slightly remaining unreacted CTA were adsorbed onto the ion exchange resin, and then the ion exchange resin was removed to obtain collagen with a concentration of 30%. An aqueous F6 liquid of a quaternary trimethylammonium derivative as a hydrolyzate was obtained.

When the obtained aqueous solution was subjected to a characteristic reaction for quaternary ammonium salt, a white precipitate was produced with sodium tetraphenylboronate, and a red precipitate was produced with Dragendreux reagent, which showed a positive result.

Furthermore, in order to confirm that the collagen hydrolyzate and CTA were bonded, the obtained aqueous solution was used to perform gel evacuation, and the above-mentioned characteristic reaction was performed for each molecular weight fraction. All of the fractions had a positive quaternary ammonium salt reaction, confirming that the collagen hydrolyzate and CTA were bound together.

Reference Example 3A-2 Collagen hydrolyzate obtained in Reference Example IA-2 35
% aqueous solution 1b (average molecular weight of collagen hydrolyzate 50
0, total amount of amino nitrogen (697 mmol) into a reaction vessel, and while stirring, add 228 g of solution (0.85 equivalent of collagen hydrolyzate) to CTA7 with a concentration of 49%.
was added dropwise over a period of 30 minutes, and during this time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain the pH of the reaction solution at 9.5. After the completion of dropping CTA, stirring was continued for 5 hours while maintaining the pH at 9.5, and then after being left for 24 hours, the amino nitrogen was measured, and the total amount of amino nitrogen was 147 mmol. Amino nitrogen 79
% was also reacting. Next, the reaction solution was mixed with a strongly acidic cation exchange resin Diaion 5K-IB (trade name, Mitsubishi Chemical Industries, Ltd.).
Co., Ltd.), the solution was passed through a 320 ml resin tower, neutralized to pH 6.9, sodium ions in the reaction solution and slightly remaining unreacted CTA were adsorbed onto the ion exchange resin, and then the ion exchange resin was After removal, an aqueous solution of a quaternary trimethylammonium derivative of collagen hydrolyzate having a concentration of 30% was obtained.

The resulting aqueous solution was subjected to a quaternary ammonium salt reaction in the same manner as in Reference Example 3A-1, and all results were positive.

In addition, using the obtained aqueous solution, gel separation was carried out in the same manner as in Reference Example 3A-1, and each molecular weight fraction was subjected to a quaternary ammonium salt reaction. As a result, each fraction was positive, and collagen hydrolysis W1 confirmed that the substance and CTA were bonded.

Reference Example 3A-3 Collagen hydrolyzate obtained in Reference Example IA-3 35
% aqueous solution (average molecular weight of collagen hydrolyzate 1,700, total amount of amino nitrogen 140 mmol) was placed in a reaction vessel, and while stirring at 30°C, 63.1 g of CTA aqueous solution with a concentration of 49% (collagen hydrolyzate 1.0 equivalent of the decomposition product) was added dropwise over 1 hour, and during that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain p)] of the reaction solution at 11.0. After finishing dropping CTA,
Stirring was continued for 3 hours while maintaining the pH at 11.0, and then the amino nitrogen was measured after being left for 24 hours. The total amount of amino nitrogen was 14 mmol, which was 90% of the amino nitrogen. was reacting. Next, add a weakly acidic cation exchange resin Amberlite Natsu RC-50 (
Add 120 mA (previously mentioned), and add sodium ions in the reaction solution and only 1? The remaining unreacted CTA was adsorbed onto an ion exchange resin, and then the ion exchange resin was removed to obtain an aqueous solution of a quaternary trimethylammonium derivative of collagen hydrolyzate with a concentration of 30%.

The resulting aqueous solution was subjected to a quaternary ammonium salt type reaction in the same manner as in Reference Example 3A-1, and all results were positive.

In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 3A-1, and a quaternary ammonium salt type reaction was performed on each molecular weight fraction. It was confirmed that it was bound to CTA.

Reference Example 3B Production of quaternary trimethylammonium derivative of keratin hydrolyzate Reference Example 3B-1 40% of keratin hydrolyzate obtained in Reference Example IB-1
Add 900 g of water f4i1 (average molecular weight of keratin hydrolyzate 800, total amount of amino myotinyl 430 mmol) to a reaction vessel, and add CTA with a concentration of 49% while stirring.
148 g of an aqueous solution (equivalent to 0.1 g of keratin hydrolyzate) was added dropwise over 30 minutes, and during that time, a 20% aqueous sodium hydroxide solution was added dropwise to adjust the pH of the reaction solution to 1O90.
maintained. After the completion of dropping CTA, stirring was continued for 2 hours while maintaining the pH at 10.0, and then after being left for 24 hours, amino nitrogen was measured, and the total amount of amino nitrogen was 52 mmol. 88 of nitrogen
% were responding. Next, 220 m of 6-acidic cation exchange resin Amberlite IRc-50 (mentioned above) was added to the reaction solution.
1 was added to neutralize the pH to 6.5, the sodium ions in the reaction solution and the slight remaining unreacted CTA were adsorbed onto the ion exchange resin, and then the ion exchange PA resin was removed to give a solution with a concentration of 30%. An aqueous solution of a quaternary trimethylammonium derivative of keratin hydrolyzate was obtained.

Regarding the obtained aqueous solution, the fourth
A type reaction with a class ammonium salt was performed, and all results were positive.

In addition, when the obtained aqueous solution was gel-filtered in the same manner as in Reference Example 3A-1 and a quaternary ammonium salt type reaction was performed on each molecular weight fraction, each fraction was positive, indicating that it was a keratin hydrolyzate. It was confirmed that it was bound to CTA.

Reference Example 3B-2 40% of the keratin hydrolyzate obtained in Reference Example IB-2
900 g of water iF (average molecular weight of keratin hydrolyzate 1,200, total amount of aminomyonitrogen 272 mmol) was placed in a reaction vessel, and while stirring, CT at a concentration of 49% was added.
A aqueous solution 88.7g (keratin hydrolyzate 0°85
(equivalent amount) was added dropwise over 30 minutes, and during that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to adjust the pH of the reaction solution to 10.
．． It was kept at 5. After dropping CTA, adjust the pH to 10.5.
Stirring was continued for 2 hours while maintaining the temperature, and then after being left for 24 hours, the amino nitrogen was measured.
78% of them responded. Next, strongly acidic cation exchange resin Diamond 5K-IB (mentioned above) 200 was added to the reaction solution.
ml, neutralized to pH 6.9, adsorbed sodium ions in the reaction solution and a slight amount of unreacted CTA to the ion exchange resin, then removed the ion exchange resin and adjusted to a concentration of 30%. An aqueous solution of a quaternary trimethylammonium derivative of keratin hydrolyzate was obtained.

The resulting aqueous solution was subjected to a quaternary ammonium salt type reaction in the same manner as in Reference Example 3A-1, and all results were positive.

In addition, using the obtained aqueous solution, gel i-filtration was performed in the same manner as in Reference Example 3A-1, and a quaternary ammonium salt type reaction was performed on each molecular weight fraction. It was found that [1] and CTA are combined.

Reference Example 3B-3 40% of the keratin hydrolyzate obtained in Reference Example IB-3
700 g of aqueous solution (average molecular weight of keratin hydrolyzate 600, total amount of amino nitrogen 431 mmol) was placed in a reaction vessel, and while stirring, 165 g of CTA aqueous solution with a concentration of 49% (1.0 equivalent of keratin hydrolyzate) was added to the reaction vessel. ) was added dropwise over 1 hour, during which time 20% sodium hydroxide water 'IfJk was appropriately added dropwise to maintain the pH of the reaction solution at 11.0. Once the dropwise addition of CTA was completed, stirring was continued for 2 hours while maintaining the pH at 11.0, and then after being left for 24 hours, the amino nitrogen was measured, and the total amount of amino nitrogen was 40 mmol. Amino chinogen 93
% were responding. Next, add a weakly acidic cation to the reaction solution.
l! ! Resin Amberlite IRC-50 (mentioned above) 10
The sodium ions in the reaction solution and the slightly remaining unreacted CTA were adsorbed onto the ion exchange resin, and then the ion exchange resin was removed to form a fourth keratin hydrolyzate with a concentration of 30%. An aqueous solution of a grade trimethylammonium derivative was obtained.

The resulting aqueous solution was subjected to a quaternary ammonium salt reaction in the same manner as in Reference Example 3A-1, and all results were positive.

In addition, using the obtained aqueous solution, gel separation was performed in the same manner as in Reference Example 3A-1, and a quaternary ammonium salt reaction was performed on each molecular weight fraction. It was confirmed that CTA was bound to CTA.

Reference Example 3C Quaternary trimethylammonium derivative of silk protein hydrolyzate Reference Example 3C-1 30% of pure white matter hydrolyzate obtained in Reference Example IC2l
1.200 g of an aqueous solution (average molecular weight of pure white matter hydrolyzate 500, total amount of amino-suspended nitrogen 730 mmol) was placed in a reaction vessel, heated to 40°C, and while stirring, the concentration was increased to 5.
47 g of 0% CTA dissolved in water (equivalent to 0.1 g of HR protein hydrolyzate) was added dropwise over 30 minutes, and during that time
Add 0% sodium hydroxide aqueous solution dropwise to adjust the p of the reaction solution.
H was maintained at 10.0. After dropping CTA, stirring was continued for 2 hours while maintaining the pH at 10.0.
After leaving it for a while, I measured the amino acid nitrogen.
The total amount of amino nitrogen was 81 mmol, and 89% of the amino nitrogen had reacted. Next, the weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) was added to the reaction solution.
100 m 12 was added to neutralize the pH to 6.7, and the sodium ions in the reaction solution and slightly remaining unreacted CTA were adsorbed onto the ion exchange resin, and then the ion exchange resin was removed to give a concentration of 30%. An aqueous solution of a quaternary trimethylammonium derivative of the starched protein hydrolyzate was obtained.

When the resulting water f4$ was subjected to a quaternary ammonium salt reaction in the same manner as in Reference Example 3A-1, all tests were positive.

In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 3A-1, and a quaternary ammonium salt reaction was performed on each molecular weight fraction. As a result, each fraction was positive, and the pure amount of white matter hydrated It was confirmed that the decomposition product and CTA were bound together.

Reference Example 3C-2 500 g of an aqueous solution of silk protein hydrolyzate obtained in Reference Example IC-3 with a concentration of 35% (average molecular i of pure white matter hydrolyzate 11.800, total amount of amino-suspended nitrogen 95 mmol) into a reaction vessel, and while stirring, the concentration of 49% O
To CT8 aqueous solution 3, 4g (0.8 of sardine protein hydrolyzate
5 equivalents) over a period of 1 hour, and during that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to adjust the pH of the reaction solution to 1.
Stirring was continued for 2 hours while maintaining the temperature at O10, and then the amino nitrogen was measured after being left for 24 hours. The total amount of amino nitrogen was 17 mmol, and 82% of the amino nitrogen had reacted. Ta. Next, add 80% of the strongly acidic cation exchange resin Diaion 5K-IB (mentioned above) to the reaction solution.
m4 was added to neutralize the pH to 6.9, the sodium ions in the reaction solution and the slight remaining unreacted CTA were adsorbed onto the ion exchange resin, and then the ion exchange resin was removed to obtain silk with a concentration of 30%. An aqueous solution of a quaternary trimethylammonium derivative of hydrated Zhang white matter was obtained.

The resulting aqueous solution was subjected to a quaternary ammonium salt reaction in the same manner as in Reference Example 3A-1, and all results were positive.

In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 3A-1, and a quaternary ammonium salt reaction was performed on each molecular weight fraction. The combination of CTA and CTA was mixed.

Reference Example 3C-3 30% of the pure white matter hydrolyzate obtained in Reference Example IC-3
Aqueous solution 800a (average molecule of pure white matter hydrolyzate 1t1.050, total fit of amino thiosine 226
i remole) into a reaction container, and while stirring, reduce the concentration to 49.
% CTA aqueous solution (1°0 equivalent of pure raw white matter hydrolyzate) was added dropwise over 1 hour, and during that time
% sodium hydroxide aqueous solution F4 was added dropwise to adjust the p of the reaction solution.
H was maintained at 11.0. After dropping CTA, stirring was continued for 2 hours while maintaining the pH at 11.0.
After leaving it for a while, we measured the amino suspended nitrogen.
The total amount of amino nitrogen was 18 mmol, and 92% of the amino nitrogen was reacted.

Next, a weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) 150 m II was added to the reaction solution, and the sodium ions in the reaction solution and the slightly remaining unreacted CTA were adsorbed onto the ion exchange resin. The ion exchange resin was then removed to obtain an aqueous solution of a quaternary trimethylammonium derivative of pure raw white matter hydrolyzate with a concentration of 30%.

The resulting aqueous solution was subjected to a quaternary ammonium salt reaction in the same manner as in Reference Example 38-1, and all results were positive.

In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 3A-1, and a quaternary ammonium salt reaction was performed on each molecular weight fraction. It was confirmed that the substance and CTA were bound together.

Examples 1 to 27 Using the animal protein hydrolysates, acylated products or salts thereof, and quaternary trimethylammonium derivatives obtained in Reference Examples IA-1 to 3C-3, the formulations shown in Tables 2 to 4 were prepared. An agent for permanent waving was prepared. The amount of each component is indicated by the weighted section, and the same applies below.

In Tables 2 to 4, the types of animal protein hydrolysates, their acylated products or their salts, and their quaternary trimethylammonium derivatives are the same as in the seventh example number.

Comparative Example] ~6 For comparison, permanent wave jl! with the formulations shown in Tables 2 to 4 without using animal protein hydrolyzate or its derivatives. Formulation I was prepared.

Permanent waving was performed on 28 female panels using the first agent for permanent waving of Examples 1 to 27 and Comparative Examples 1 to 6 prepared as described above.
Perform a 10-point rating + 1i (the higher the score, the better) according to each item shown in Table 7, and compare the results to the 5th to 7th points.
Shown in the table. In the above permanent wave treatment, a 7% aqueous solution of sodium bromate was used as the second agent.

Amino acid analysis was also carried out on a portion of the hair that had undergone permanent waving, and cystic acid produced by the permanent waving was quantified. It should be noted that the amount of cystic acid produced is said to cause significant hair damage. The results (average values) are shown in Tables 5-7.

〔Effect of the invention〕

As explained above, the first agent for permanent waving of the present invention has little bad odor, is highly stable, and can impart excellent permanent waving without causing damage or discomfort to the hair.

Claims (1)

[Claims] (1) Contains 2 to 12% by weight of thiomalic acid, and contains at least one selected from the group consisting of animal protein hydrolysates and derivatives thereof shown in [1] to [3] below.
First agent for permanent waves characterized by containing 1 to 5% by weight [1] General formula (I) ▲There are mathematical formulas, chemical formulas, tables, etc.▼(I) (In the formula, R_1 is animal protein hydrolysis [2] General formula (II) ▲ Contains mathematical formulas, chemical formulas, tables, etc. ▼ (II ) (In the formula, R_1 and n have the same meanings as above, R_1 is the side chain of the amino acid constituting the animal protein hydrolyzate, n is an integer from 3 to 20, and R_2 has 8 carbon atoms. ~2
0 long-chain alkyl or alkenyl group, M is hydrogen, an alkali metal such as sodium or potassium, ammonium or monoethanolamine, diethanolamine, triethanolamine, 2-amino-2-methyl-
Acylated products of animal protein hydrolysates or their salts represented by (onium of organic alkanolamines such as 1,3-propanediol) [3] General formula (III) ▲ Numerical formulas, chemical formulas, tables, etc. are available ▼ ( III) An animal represented by (wherein R_1 and n have the same meanings as above, R_1 is a side chain of an amino acid constituting the animal protein hydrolyzate, and n is an integer from 3 to 20) Quaternary trimethylammonium derivative of protein hydrolyzate.