JPS6169714A - Shampoo composition - Google Patents

Abstract

PURPOSE:The titled composition having improved conditioning effect, treatment effect and irritation on the skin, obtained by blending an anionic surface active agent with an acylated substance of animal protein hydrolyzate and a quaternary ammonium derivative of animal protein hydrolyzate. CONSTITUTION:A shampoo agent containing an anionic surface active agent is blended with (a) an acylated substance of animal protein hydrolyzate preferably shown by the formula I (R1 is 8-20C alkyl or alkenyl; R2 is side chain of constituent amino acid of animal protein hydrolyzate; n is 3-20 integer; M is H, alkali metal, ammonium, etc.) or its salt, and (b) a quaternary ammonium derivative of animal protein hydrolyzate preferably shown by the formula II or formula III (at least one of R3-R5 are 8-20C alkyl or hydroxyalkyl, and the others are 1-3C alkyl, hydroxyalkyl, or benzyl), having the above- mentioned improved effects, and low irritation to the eyes and scalp.

Description

DETAILED DESCRIPTION OF THE INVENTION [Field of Industrial Application] The present invention relates to shampoo compositions. For more details,
The conditioning effect and treatment effect of blending an acylated product of animal protein hydrolyzate or its salt and a quaternary ammonium derivative of animal protein hydrolyzate with an anionic surfactant-containing nyanpu agent. This invention relates to a Nyanpu composition which has excellent properties and is less irritating to the eyes and scalp.

[Prior Art] Conventionally used shampoos have as their base anionic surfactants such as alkyl sulfate salts and polyoxyethylene alkyl sulfate salts, and nonionic surfactants such as polyoxyethylene alkyl ethers and fatty acid alkylolamides. surfactant or alkyl betaine,
It contains a zwitterionic surfactant such as an alkylamine oxide alone or in the form of a mixture thereof.

When hair is washed with shampoos containing these bases, sebum and other oils present on the surface of the hair are washed away excessively, making the hair feel extremely unpleasant after washing and making it difficult to pass through with combs and brushes. Become. In addition, when the hair is completely dry, it is difficult to manage, and especially in the winter when the humidity is low, static electricity is easily generated when brushing, which causes phenomena such as hair flies, and the hair gets tangled with each other. This makes it difficult for the brush to pass through, causing split ends and hair breakage.

Therefore, it has been conventional practice to add oil or the like to the shampoo base to supplement the oil content during hair washing.

[Problem that the invention seeks to solve]

However, in a shampoo formulation system, the entire system is emulsified or solubilized by surfactants, and a sufficient amount of oil is added to the scalp and hair without compromising the stability of the system. It is a shame to do so.

In addition, when a large amount of oil is added, the amount of oil adsorbed to the hair increases, but the foaming and cleaning power, which is the original function of Nyanbu, becomes extremely poor, resulting in a significant loss of commercial value.

Furthermore, if the shampoo accidentally gets into the eyes, the surfactant, especially the anionic surfactant, can strongly irritate the eyes.

[Means for solving problems]

As a result of intensive research to solve the various problems in the conventional Nyanpu compositions described above, the present inventors have found that shampoos containing anionic surfactants contain collagen, keratin, silk protein, etc. When blending an acylated product of an animal protein hydrolyzate or a salt thereof with a quaternary ammonium derivative of the animal protein hydrolyzate, it is possible to A shampoo composition that gives suppleness, smoothness, etc. to hair after washing, has excellent conditioning and treatment effects, such as good shedding properties, and is less irritating to the eyes and scalp. This discovery led to the completion of the present invention.

In the shampoo composition of the present invention, as the anionic surfactant, anionic surfactants conventionally used as bases of shampoo agents, such as straight or branched chain alkylbenzene sulfonates, straight chain or branched chain alkylbenzene sulfonates, etc. Polyoxyalkylene alkyl sulfate ester salts, alkyl sulfate ester salts, olefin sulfonates, alkanesulfonic acids, alkyl ethyne carboxylates, etc., which have a branched alkyl group and have ethylene oxide or propylene oxide added thereto, can be used. can.

In addition, counter ions for these anionic surfactants include alkali metal ions such as sodium and potassium, alkaline earth metal ions such as calcium and magnenium, ammonium ions, monoethanolamine, jetanolamine, and triethanolamine. , alkanolamines such as triisopropanolamine, and the like.

In the shampoo composition of the present invention, the acylated product of animal protein hydrolyzate or its salt to be used in combination with the anionic surfactant has the following general formula (+) (wherein R1 has 8 to 20 carbon atoms). is a long-chain alkyl group or alkenyl group, and R2 is a group III of an amino acid constituting the animal protein hydrolyzate. n is an integer of 3 to 20, M is an alkali metal such as hydrogen, sodium, or potassium; Ammonium or monoethanolamine, jetanolamine, triethanolamine, 2-amino-
Anolated products of animal protein hydrolysates or salts thereof are preferred.

In addition, the quaternary ammonium derivative of the animal protein hydrolyzate used in the 7YAMP composition of the present invention, together with the above-mentioned acylated product of the animal protein hydrolyzate or its salt, is represented by the following general formula (It). H3 (wherein, R2 and n have the same meanings as in the -M formula (1), R2 is the t(1) chain of the amino acid constituting the animal protein hydrolyzate, and n is 3 to is an integer of 20), or a quaternary trimethylammonium derivative of an animal protein hydrolyzate represented by the following general formula CII [3 (R2 and n have the same meanings as in the above general formula (+), R2 is a 0111 chain of amino acids constituting the animal protein hydrolyzate, and n is an integer from 3 to 20.R3
, R4, and R5 are long-chain alkyl groups or hydroxyalkyl groups with 8 to 20 carbon atoms, and the remainder are alkyl groups, hydroxyalkyl groups, or benzyl groups with 1 to 3 carbon atoms. Quaternary ammonium derivatives at the 7-mino group of the protein hydrolyzate are preferred.

Acylated products of animal protein hydrolysates or salts thereof, quaternary ammonium derivatives, etc. represented by the above general formulas (RI to (III)) include collagen, keratin, silk, etc.
It is derived from animal protein hydrolysates such as be done. The absorbed animal protein hydrolyzate derivative has a polypeptide structure similar to hair keratin, so it contains acidic amino acids such as glutamic acid and aspartic acid, and arginine, which both have.
Bonds are formed with the hair tissue through ionic bonds between side chains of basic amino acids such as lysine and histidine, hydrogen bonds between peptide chains, and van der Waalska between side chains of hydrophobic amino acids. The animal protein hydrolyzate derivative absorbed into the hair in this way strengthens the hair and makes it less susceptible to damage when subjected to permanent waving, for example. Acylated products of animal protein hydrolyzate as shown in general formula (1) include alkali metals such as sodium and potassium, ammonium, monoethanolamine, jetanolamine, triethanolamine, 2-amino-2- Methyl-1,3-
When used in the form of a salt of an organic alkanolamine such as propanediol, it acts as an anionic surfactant with mild surface activity, and when used in combination with the various anionic surfactants mentioned above, it can cause damage to hair. Suppresses excessive degreasing from the scalp, reducing irritation to the scalp and eyes. In addition, quaternary ammonium derivatives of animal protein hydrolysates, such as those represented by general formula (■) or (III), have a quaternary ammonium moiety induced, so collagen hydrolysates and keratin hydrolysates Compared to simple animal protein hydrolysates, it has excellent absorption into the hair and has the effect of imparting flexibility to the hair. These have excellent effects even when blended alone into shampoos, but especially when used in combination with an acylated product of animal protein hydrolyzate or a salt thereof as shown in the general formula (+), Since the acylated product of protein hydrolyzate or its salt is anionic and the quaternary ammonium derivative of animal protein hydrolyzate is cationic, animal protein hydrolyzate as shown by general formula (I) Due to the interaction between the anolide or its salt and the quaternary ammonium derivative of animal protein hydrolyzate as shown by the general formula (■) or (m), when they are combined alone, In addition to its effectiveness, it also provides an excellent texture.

That is, an acylated product of an animal protein hydrolyzate or a salt thereof as shown by the general formula (1), and a compound of the general formula ([1
) or (II), in addition to the mutual affinity of their polypeptide moieties, the quaternary ammonium derivatives of animal protein hydrolysates as shown in general formula (1) The affinity is further increased by the 7-ionic nature of the acylated product of the decomposition product or its salt and the cationic nature of the quaternary ammonium derivative of the animal protein hydrolyzate as shown by the general formula (■) or (Ill). Furthermore, since it interacts with the anionic surfactant contained in the mixture, the compatibility between the ingredients improves, and when the anionic surfactant acts on the hair and scalp, its excessive cleaning action, It alleviates the degreasing effect and prevents the hair from losing its suppleness and combability.
It also reduces irritation to the scalp and eyes.

An acylated product of an animal protein hydrolyzate or a salt thereof as shown by the general formula (1) used in the present invention, or an animal protein hydrolyzate as shown by the general formula (II) or ([+1) Quaternary ammonium derivatives are derived by performing various reactions from animal protein hydrolysates obtained by hydrolyzing animal proteins such as collagen, keratin, and silk using acids, alkalis, or enzymes. Ru. The manufacturing 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 enzyme, reaction temperature, and reaction time, the value of n of the resulting animal protein hydrolyzate can be adjusted to 3 to 20, that is, the molecular weight is approximately 300 to approximately 2,000.
can be made into a preferred one.

Raw animal proteins include collagen, keratin,
Examples include silk protein, elastin, actin, and myonon. 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.

Animal protein hydrolysates derived from these raw materials have the property of adsorbing to hair, and are also used as safe cosmetic raw materials derived from natural products to prevent hair damage, restore hair damage, moisturize the skin, and improve the interface. It is useful in preventing denaturation of skin proteins caused by active agents.

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 comes in powder, plate, and granule forms, 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, and 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.

Silk protein raw materials include silkworm cocoons,
Examples include silk thread and silk cloth, but since no particular processing is required, it is economically advantageous to use silkworm cocoons or unspun cotton-like or double-thread-like materials. Similar to keratin, which is the same fibrous protein, silk protein may be cut or crushed into appropriate sizes, washed, or subjected to high-temperature pressure treatment as necessary. Since silk proteins can be dissolved in highly concentrated aqueous solutions of 40% by weight or more of alkali metal salts or alkaline earth metal salts, it is also possible to once dissolve silk proteins in these aqueous solutions and then hydrolyze the molten solution.

In addition, elastin, which is known as a protein that exists in the skin together with collagen and gives elasticity to the skin, and actin and myonon, which are muscle proteins, can also be used.

Acid hydrolysis, alkaline hydrolysis, and enzymatic hydrolysis of υJ physical protein are performed as shown below.

Examples of hydrolysis acids using tl+ acids include inorganic acids such as hydrochloric acid, f[acid, phosphoric acid, nitric acid, and hydrobromic 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 5 to 85% by weight, but
It is desirable that the hydrolysis reaction always be at a pH of 4 or below. If more acid is used than necessary, the hue of the hydrolyzate solution will turn brown to black, which is undesirable. 1. The reaction temperature is 40 to 100°C. Preferably, 160°C under pressure
6 The reaction time is preferably 2 to 24 hours. 0 The reactant can be neutralized with an alkali such as sodium hydroxide, hydroxide, sodium carbonate, etc. and used as it is, but the reactant or neutralized The substance can also be purified and used by gel filtration, ion exchange resin, ultrafiltration, dialysis, electrodialysis, etc.

(Alkali hydrolyzed by 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 1-2011% 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. After the reaction, neutralize with the acid mentioned above, or use gel filtration, ion exchange resin,
Purification is preferably carried out by ultrafiltration, dialysis, electrodialysis, etc.

(3) As the enzymatic hydrolase, acidic proteolytic enzymes such as pepsin, protase A, and protase B, and neutral proteolytic enzymes such as papain, bromelain, thermolynone, trypnone, pronase, and chymotrybunone are used. Further, neutral proteolytic enzymes such as subtilin and staphylococcal protease can also be used. p during hydrolysis
l+ is p in the case of acidic proteolytic enzymes such as pepnon.
In the case of neutral proteolytic enzymes such as papain, it is preferable to adjust the pH to a range of 4 to 10.
pH is generally determined by acetic acid/sodium acetate, phosphoric acid
The reaction temperature is preferably 30 to 45°C, and the reaction time is generally 3 to 24 hours, which is preferably adjusted appropriately with a buffer solution such as IFK solution or by addition of acid, alkali, etc.

In enzymatic hydrolysis reactions, the molecular weight of the hydrolyzate is greatly influenced by the amount of # element 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 is examined by gel filtration under various conditions such as the amount of enzyme used, reaction temperature, and reaction time. It is necessary to determine the optimal conditions empirically.

Enzymatic hydrolysates produce less amino acids with a molecular weight distribution of <<, im than hydrolysates with acids or alkalis, and are therefore 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, are easily soluble in water, and are easy to handle, while those with a molecular weight of more than 2,000 have little adsorption to hair and are difficult to handle.

In addition, the amino acids whose side chains are represented by R in the general formula (2) include alanine, glycino, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine,
histidine, lysine, aspartic acid, asparagine,
Glutamic acid, Glutamine, Cystine, Nsteic acid,
Examples include tryptophan, hydroxyproline, and hydroquinlinone. Table 1 shows examples of the composition ratios (based on mol%) of these amino acids.

2. Acylated product of animal protein hydrolyzate or its salt The most common method for acylating the animal protein hydrolyzate obtained above is the Schotten-Baumann reaction.
Mann reaction).

This reaction is a reaction in which an acid chloride derivative of a higher fatty acid to be condensed is added to an aqueous solution of an animal protein hydrolyzate under alkaline conditions of pH 8 to 10 with stirring. According to this reaction, as shown in the following formula, OR1 R2CC1+H+NH-CH-CofTOHOR1 1l -R2-C+NH-CH-CO? Since TOH + HCl hydrochloric acid is formed and the pH decreases, it is necessary to maintain the pH at 8 to 10 by adding an alkali such as sudium hydroxide or potassium hydroxide while adding acid chloride. The reaction temperature is 0 to 60°C, preferably 20 to 40°C for 1 to 6 hours.

In addition to the above-mentioned acid chlorides, acid halides of higher fatty acids such as Br and 1 can be used as the higher fat @ side component. 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, methods such as animal protein hydrolyzate and higher fatty acids or their methyl esters, ethyl esters, etc. at high temperatures of 150 to 200°C and under high pressure are used. A method of dehydration condensation or dealcoholization condensation by treating a lower alcohol ester with a lower alcohol ester can also be adopted, but since the 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 carboquine group-activated derivatives such as N-oxysuccinimide ester or N-phthalimide ester, and then react them with animal protein hydrolysates. 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 sulfuric acid, and the liberated product is collected as a floating precipitate, which is purified by washing with water. or dissolve it in water or a solvent such as alcohol or propylene glycol to form a solution at a preferred concentration (10 to 60% (wt%, hereinafter the same), especially 20 to 40%), or The progress and completion of the reaction is confirmed by measuring the amino nitrogen in the animal protein hydrolyzate using the Van 5lyke method.

3 Quaternary trimethylammonium derivative of animal protein hydrolyzate Quaternary trimethylammonium derivative of animal protein hydrolyzate represented by the general formula (■)
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-hydroxypropyltrimethylammonium chloride (hereinafter referred to as CTA) used in the above reaction
) is known as existing chemical substance +21-181, and an aqueous solution 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 in water. 12, it is particularly desirable to maintain the pH within the reaction system at 9 to 11. Therefore, during the 0 reaction, an alkaline aqueous solution such as sodium hydroxide or potassium hydroxide is dropped into the reaction solution as necessary.
To maintain G) within the above range, it is preferable that the amino group of the animal protein hydrolyzate be on the alkaline side, at pH 8 or higher, to react with CTA, and if G)H exceeds 12, CTA and animal The reaction, which is caused by the hydrolysis of a protein hydrolyzate, 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. The higher the concentration of the protein hydrolyzate, the higher the viscosity (which makes it difficult to achieve a uniform reaction), so the concentration is 30-50%.
It is preferable to use a commercially available aqueous solution with a concentration of 50% as CTA.

Adding CTA to animal protein hydrolyzate takes 30 minutes to 6 minutes.
When CTA is added dropwise, a reaction as shown in the following formula proceeds, which is preferably completed within hours, and CH3H+NH-CH-CO? yOe - = Hydrogen chloride is generated and the pH of the reaction solution decreases, so add alkali dropwise at the same time as CTA and stir to reduce the pH in the solution.
It is preferable to maintain H at a pH suitable for the reaction, and therefore it is preferable to allow at least 30 minutes for the dropwise addition. After dropping CTA, the W temperature is continued for about 2 to 6 hours, and the pH is adjusted to 9 to 11. Preferably, the reaction is completed by keeping it for a day or two or by heating it to about 60°C.The progress and completion of the reaction can be determined by measuring the amino nitrogen in the hydrolyzate using the Van Slake method. It is confirmed by

4 Quaternary ammonium derivative of animal protein hydrolyzate The quaternary ammonium derivative of the amino group of animal protein hydrolyzate represented by the general formula CIII) can be obtained as follows.

First, a halogenated long-chain alkyl or a halogenated long-chain hydroxyalkyl such as a long-chain alkyl chloride or a long-chain hydroxyalkyl chloride having 8 to 2 carbon atoms is added to the hydrolyzate of the animal protein obtained as described above. Alkylate or hydroquine alkylate the amino groups of the protein hydrolyzate. The method of alkylation or hydroxyalkylation at this time is the CTA described in the previous section.
However, especially when using alkyl halides such as alkyl chlorides, since they are not water-soluble, the reaction mixture should be mixed with low-boiling alcohols such as methyl alcohol, ethyl alcohol, isopropyl alcohol, or acetone. The above reagent and animal protein hydrolyzate can be reacted by adding a water-soluble, low boiling point solvent such as .

In addition, alkylation or hydroquine alkylation proceeds in such a method because of dialkylation or bis-(
Hydroquine alkyl)) Therefore, in order to obtain a quaternary ammonium derivative, it is necessary to proceed to the next reaction.

When carrying out monoalkylation or mono (hydroquine alkyl)ation in the first reaction, by using about an equivalent amount of the reagent for the 7-mino group of the animal protein hydrolyzate,
In addition, when performing dialkylation or bis-(hydroxyalkyl) formation, use approximately twice the equivalent amount of the reagent. Slightly high in the range (and increases reaction time).

Furthermore, in order to induce a quaternary ammonium derivative, the reaction method differs depending on the reagent used. In other words, when producing a quaternary ammonium derivative containing a methyl group, an ethyl group, or a propyl group, a low-boiling point compound such as methyl chloride is used. When using methyl halide, ethyl halide, propyl halide, etc., add the required amount of methyl chloride, etc. and a neutralizing agent such as sodium carbonate, sodium hydrogen carbonate, potassium carbonate, potassium hydrogen carbonate, etc. in an autoclave. High temperature (60-140℃)
In the case of producing a quaternary ammonium derivative containing a hydroxyethyl group or a hydroxypropyl group, which is reacted under high pressure, substantially the same method is used when ethylene oxide or propylene oxide is used. When using a benzyl halide such as benzyl chloride to obtain a quaternary ammonium derivative containing a benzyl group, a required amount of benzyl halide such as benzyl chloride is added and the reaction is carried out at 80 to 130°C for 1 to 3 hours.

If necessary, the reaction mixture in the previous step is concentrated under reduced pressure to remove water and alcohol, and the reaction is carried out using appropriate solvent conditions. Almost the same method is used when using ethylene chlorohydrin and when using glycerol-1-chlorohydrin as a quaternary ammonium derivative containing a 2,3-dihydroxypropyl group.

In any case, to lead to quaternary ammonium derivatives,
Alkyl halides, hydroxyalkyl halides, halides such as ethylene oxide and propylene oxide, or epoxides are used, but if these reagents vaporize under the reaction conditions, the reaction should be carried out at high temperature and pressure using an autoclave or the like. If there is no risk of vaporization, the reaction is carried out at high temperature and normal pressure.The reaction temperature is 40 to 140°C, and the reaction time is 1 to 4 hours.
A suitable solvent or catalyst is used as necessary.

The shampoo composition of the present invention includes a shampoo containing an anionic surfactant, an acylated product of an animal protein hydrolyzate or a salt thereof, and a quaternary ammonium derivative of an animal protein hydrolyzate as described above. It is prepared by blending.

However, in its preparation, it does not specify the order of adding the anionic surfactant and the acylated product of animal protein hydrolyzate or its salt, or the quaternary ammonium derivative of animal protein hydrolyzate. An anionic surfactant, an anolated product of an animal protein hydrolyzate or a salt thereof, and a quaternary ammonium derivative of an animal protein hydrolyzate may be contained in the Noyanpu composition.

In the shampoo composition of the present invention, the concentration of the anionic surfactant is preferably in the range of 2 to 20%, and the concentration of the acylated product of animal protein hydrolyzate or its salt is in the range of 0.2 to 20%. Animal protein hydrolyzate No. 4
The amount of the class ammonium derivative is preferably in the range of 0.1 to 5%.

This is because if the concentration of anionic surfactant is lower than the above range, the foaming and cleaning power of the shampoo will be reduced, and if it is higher than the above range, it will be excessive in the normal usage amount and will cause strong irritation to the eyes, scalp, skin, etc. Because it will be. If the concentration of the acylated product of animal protein hydrolyzate or its salt is lower than the above range, the hair will not be supple or
Even if the effect of imparting smoothness etc. is not sufficiently exhibited and the concentration exceeds the above range, there is no particular problem in normal use, but in that case, the concentration of the anionic surfactant can be lowered to reduce the total concentration of both. It is preferable that the concentration of the quaternary ammonium derivative of the animal protein hydrolyzate is lower than the above range, and the effect of imparting suppleness, smoothness, etc. to the hair is fully exerted. On the other hand, if the amount is higher than the above range, the amount absorbed into the hair may be excessive and leave an unpleasant sensation such as tackiness on the hair. In the present invention, among surfactants, particularly anionic surfactants, are used as the shampoo base because the anionic surfactant has good compatibility with the animal protein hydrolyzate derivative and foams. This is because it has good dryness, cleansing power, and feel.

In addition to the above-mentioned three essential ingredients, the ingredients of known shampoo compositions can be added to the Nyanpu composition of the present invention.

For example, surfactants such as nonionic surfactants, amphoteric surfactants, and cationic surfactants, higher fatty acids such as yaso fatty acid jetanolamide, and stearic acid monoethanolamide may be used as long as the effects of the present invention are not impaired. Pearlizing agents such as monoethanolamide or noethanolamide, ethylene glycol monostearate, ethylene glycol distearate, animal protein hydrolysates, synthetic esters, oils such as natural animal and vegetable oils, A-layer agents, chelating agents, Preservatives, fragrances, etc. can be added.

〔Example〕

Next, the present invention will be further explained by referring to reference examples and examples.

Reference example 1 Reference example IA for production of animal protein hydrolyzate
Reference example for production of collagen hydrolyzate IA-1 (Acid hydrolysis) Add 700 g of water to 300 g of powdered gelatin, dissolve while heating, add 60 g of concentrated hydrochloric acid at 70°C, and add water for 1 hour while stirring. After the decomposition, the reaction mixture was filtered, the filtrate was diluted to 21% with water, and the solution was passed through a 290 ml resin tower containing weakly basic anion exchange resin Diaion WA20 (trade name, Mitsubishi Chemical Industries, Ltd.). Neutralized. This was concentrated under reduced pressure and filtered to obtain an aqueous solution of collagen hydrolyzate with a concentration of 40%.

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 IA-2 (alkaline hydrolysis) 500 g of plate gelatin was dissolved while heating 700 g of a 6% aqueous sodium hydroxide solution, and 1 was dissolved while stirring at 80°C.
After hydrolysis for a period of time, the reaction mixture was filtered, the filtrate was diluted with water to a volume of 5.
The solution was neutralized by passing the solution through a resin tower at 00 mA. This was concentrated under reduced pressure and filtered to obtain a 35% collagen hydrolyzate aqueous solution. 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, then add 20 g of the neutral proteolytic enzyme papain, and stir at 50°C. After 3 hours of hydrolysis, the reaction mixture was filtered to a concentration of 3.
A 5% collagen hydrolyzate aqueous solution was obtained. The molecular weight of the thus obtained collagen hydrolyzate was measured by gel filtration and found to be an average molecular weight of 700.

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

After hydrolysis, the reaction mixture was filtered and the filtrate was treated with a weakly basic anion exchange resin Diaion WA20 (described above) at 1,40
After neutralization with 0 ml of [ML, the ion exchange resin was removed to obtain a 40% aqueous solution of keratin hydrolyzate. The molecular weight of the keratin hydrolyzate thus obtained was measured by gel filtration and found to have an average molecular weight of 800.

Reference Example IB-2 (Alkaline Hydrolysis) Add 100 g of sodium hydroxide and 3 kg of water to 500 g of pig hair, leave it at 40°C for 24 hours to perform hydrolysis, filter the reaction mixture, and add weakly acidic cations to the filtrate. Replacement resin Amberlight IRc-50 (mentioned above) 600ml! It was neutralized by After concentrating this, Il! Then, the ion exchange resin was removed to obtain an aqueous 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/cd 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 40% keratin hydrolyzate. 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 Manufacture of Silk-covered White Matter Hydrolyzate Reference Example IC-1 (Flukaline Hydrolysis) 1.5 ffi of 2N sodium hydroxide was placed in a 2c beaker, and 500 g of dried silkworm cocoon was added to this (preliminarily washed silkworm (excluding feces and dirt), add as much as possible, heat to 80℃, and stir while stirring.
The cocoon was dissolved by hydrolysis, and the remaining cocoon was added. After adding the entire amount of cocoon for 30 minutes, add another 1 hour 8
After heating to 0°C and stirring to complete hydrolysis,
After diluting the reaction product by adding 11, it was filtered under reduced pressure.

The filtrate was treated with a weakly acidic cation exchange resin Amberlite IRc-
50 (supra) 1. After neutralizing the solution by passing it through a 300 ml resin tower, it was compressed under reduced pressure and filtered to obtain an aqueous solution of silky white matter hydrolyzate with a concentration of 30%. The molecular weight of the silk-covered white matter hydrolysis obtained in this way was determined by
When measured by leakage method, the average molecular weight was N500.

Reference Example IC-2 (Acid Hydrolysis) Commercially available 55% lithium bromide aqueous solution? &1. After adding 200 g of unspun silk fiber to Okg at 50°C and dissolving it, this solution was diluted to 2.0 kg with ion-exchanged water.

This liquid was heated to 80°C in a 21370 flask and li! The mixture was stirred, and 25 g of 1-hydrochloric acid was added for hydrolysis for 2 hours. After cooling, 48 g of 20% aqueous sodium hydroxide solution was added to neutralize the mixture, and then filtered under reduced pressure. The iIt solution was subjected to electrodialysis, desalted, concentrated under reduced pressure and filtered to obtain an aqueous solution of silky white matter hydrolyzate with a concentration of 35%. The molecular weight of the silk-covered white matter hydrolyzate thus obtained was measured by gel filtration and found to have an average molecular weight of 1,800.

Reference example 1cm3 (enzyme hydrolysis) 300g of washed silkworm cocoon was heated to 10kI in a high-pressure container.
r/cll, treated with superheated steam at 200°C for 1 hour to swell, and then placed in a bee force of 21 and 0. IN acetic acid
JtsuAitf+[(pH6)11. Add le, 40°C
Then, 2011 g 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% silken white matter hydrolyzate was obtained. The molecular weight of the thus obtained silken white matter hydrolyzate was measured by a gel filtration method and found to be an average molecular weight of i, oso.

Reference Example 2 Production of an acylated product of animal protein hydrolyzate or its salt Reference Example 2A Production reference of an acylated product of collagen hydrolyzate or its salt Reference IP112A-1 Acylated product of collagen hydrolyzate with myristic acid Reference Example IA- 40 of the collagen hydrolyzate obtained in 1.
% aqueous solution over 2 hours while stirring at a constant temperature of 35°C. Meanwhile, 20
% aqueous sodium hydroxide solution was appropriately added to maintain the pH at 9.5. After stirring at 35°C for 1 hour, the temperature was raised to 40°C, the reaction was completed by stirring for 1 hour, and the reaction mixture was discharged from the reaction vessel into a 5% aqueous sulfuric acid solution 51, and the produced acylated product was converted into a free form ( The carboxylic acid in the bebutide part of the acylated product is not in the form of a salt but in the form of -COOH), then washed with water, and then propylene glycol is added to dissolve the acylated product. Glycol-water soluble night 71
Obtained 0g. Note that the concentration of propylene glycol was 40%. The yield was 88%.

Regarding the 30% propylene glycol-aqueous solution of the obtained product, amino nitrogen was determined by the Van Slake method and was found to be 0.008 mg/g, which was obtained in Reference Example IA-1 used as a raw material. The 409A aqueous solution of collagen hydrolyzate has an amino nitrogen content of 15.510
mg/g, indicating that most of the amino groups in the product were acylated.

Reference Example 2 Person-2 Sodium salt of collagen hydrolyzate acylated with coconut fatty acid Reference 9111 Using 500 g of a 35% aqueous solution of the collagen hydrolyzate obtained in A-2, myristic acid chloride in Reference Example 2A-1 was added. The product was washed with water in the same manner as in Reference Example 2A-1 except that 96 g of coconut fatty acid chloride (1.0 equivalent of collagen hydrolyzate) was used instead, and then a 30% aqueous sodium hydroxide ion solution was added. Neutralized sodium salt aqueous solution of collagen hydrolyzate acylated with coconut fatty acid to a concentration of 30% 89
3g was obtained. The yield was 96%.

Amino thia s was measured by the Van Slake method on a 30% aqueous solution of the obtained product, and it was found that O,009
It was 11g/g. Reference example IA used as raw material
The 35% aqueous solution of collagen hydrolyzate obtained in -2 had an amino thiadine content of 19.60 mg/g, indicating that most of the amino groups in the product were acylated.

Reference Example 2A-3 Sodium salt of collagen hydrolyzate acylated with lauric acid Collagen hydrolyzate 35 obtained in Reference Example 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 Reference IP1128-1 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. The yield was 96%, and the amino nitrogen content of a 30% aqueous solution of the obtained product was measured by the Van Slake method, and it was found to be 0.010 B/g. The 35% aqueous solution of collagen hydrolyzate obtained in Reference Example IA-3 used as a raw material had an amino nitrogen content of 5.76 B/g, indicating that most of the amino groups in the product were acylated. found.

Reference Example 2B Production of acylated product of keratin hydrolyzate or its salt Reference Example 2B-1 2-Amino-2-methyl-1,3-propanediol salt of acylated product of keratin hydrolyzate with coconut fatty acid Reference Example IB- 40% of the keratin hydrolyzate obtained in 1.
Coconut fatty acid (mixed fatty acid with 8 to 18 carbon atoms) chloride 55F1 (
1.0 equivalent of keratin hydrolyzate (II) 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 produced acylated product was suspended in a free form, washed with water, and then 2-amino-2-methyl-1,3
- Neutralization by adding propanediol to obtain 855 g of a 2-amino-2-methyl-1,3-propanediol salt aqueous solution of keratin hydrolyzate acylated with coconut fatty acid at a concentration of 30%, yield: 94 %Met.

Amino nitrogen was measured in a 30% aqueous solution of the obtained product by the Van Slake method, and it was found to be 0.00.
It was 7 B7 g. Reference example IB- used as raw material
The 40% aqueous solution of keratin hydrolyzate obtained in step 1 contained 7.270 mg/g of amino nitrogen, indicating that most of the amino groups in the product were acylated.

Reference Example 2B-2 Monoethanolamine salt of acylated product of keratin hydrolyzate with caprylic acid 40% of the keratin hydrolyzate obtained in Reference Example IB-2
Using 500 g of aqueous solution, 32 g of caprylic acid chloride (in place of coconut fatty acid chloride in Reference Example 2B-1)
Monoethanol, an acylated product of keratin hydrolyzate with caprylic acid, was prepared in the same manner as in Reference Example 2B-1 except that monoethanolamine was used in place of triethanolamine (1.0 equivalent of keratin hydrolyzate) and monoethanolamine was used instead of triethanolamine. 11890 g of 30% water of amine salt was obtained. The yield was 98%.

When the amino nitrogen of the obtained product (dry residue 37.20%) before neutralization with monoethanolamine was measured by the Van Slake method,
It was 0.041 mg/g. The reason why the amino acid was measured 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 acid. be. Reference example IB- used as raw material
The 40% aqueous solution of keratin hydrolyzate obtained in step 2 contained 4.729 mg7 g of amino-thia a, 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 while stirring at a constant temperature of 30°C. 1.0 equivalent) to 2
It dripped over time. During this time, the pH was maintained at 9 by appropriately adding a 20% aqueous potassium hydroxide solution. 1 further at 30℃
After stirring for an hour, the temperature was raised to 40° C. and stirring was continued for L hours to complete the reaction.

The reaction mixture is discharged from the reaction container into a 5% aqueous sulfuric acid solution 51, and the generated acylated product is suspended in a free form,
After washing the f$ product with water, propylene glycol was added and dissolved to obtain 960 g of a 25% aqueous propylene glycol solution of a keratin hydrolyzate acylated with coconut fatty acid. Note that the concentration of propylene glycol is 40%. The yield was 96%. Amino nitrogen in a 25% aqueous propylene glycol solution of the obtained product was measured by the Van Slake method and found to be 0.007 mg/g. The 40% aqueous solution of keratin hydrolyzate obtained from reference 1qlB-3 used as a raw material has an amino nitrogen content of 9.220.
mg/g, indicating that most of the amino groups in the product were acylated.

Reference Example 2C Preparation of acylated product or salt thereof of silky white matter hydrolyzate Reference Example 2G-1km Potassium salt of acylated product with lauric acid of protein hydrolysis Reference l 30% of silky white matter hydrolyzate obtained in NIc-1
Stir 500 g of % aqueous solution at 30℃ for t1! 65.5 g of lauric acid chloride (1.0 equivalent of silky white matter hydrolyzate) was added dropwise over 2 hours. 20% during that time
The pH was maintained at 9 by appropriately adding an aqueous sodium hydroxide solution. After further heating at 30°C for 1 hour at ff1M', the temperature was lowered to 4°C.
The temperature was raised to 0°C and stirring was continued for 1 hour to complete the reaction.

The reaction mixture is discharged from the reaction container into a 5% aqueous sulfuric acid solution 51, and the produced acylated product is suspended in a free form,
The suspended matter was washed with water and neutralized with a 30% water 18 solution potassium aqueous solution to obtain 232 g of a potassium salt aqueous solution of the acylated product of total protein hydrolyzate with lauric acid having a concentration of 30%.

The yield was 90%.

Amino nitrogen was measured in a 30% aqueous solution of the obtained product by the Fanslake method, and it was found to be 0.009.
It was mg/g. Reference example IC- used as raw material
The 30% aqueous solution of total protein hydrolyzate obtained in step 1 contains 16% amino nitrogen. h+g/g, indicating that most of the amino groups in the product were acylated.

Reference Example 20-2 Calirum salt of acylated total protein hydrolyzate with undecylenic acid.In place of the total protein hydrolyzate obtained in Reference Example IC-1 in Reference Example 2C-1, the total protein hydrolyzate obtained in Reference Example IC-2 was used. In the same manner as Reference Example 2G-1, except that 500 g of the 359A aqueous solution of the total protein hydrolyzate was used and 20 g of undecylenic acid chloride (1.0 equivalent of the total protein hydrolyzate) was used instead of the lauric acid chloride. 610 g of a potassium salt aqueous solution of acylated total protein hydrolyzate with underunic acid having a concentration of 30% was obtained. The yield was 93%.

1. Amino chinogen was measured by the Van Slake method on a 30% aqueous solution of the product, and it was found to be 0.01.
It was 7 mg/g. Reference example IC used as raw material
The 35% water 'tG solution of total protein hydrolyzate obtained in -2 contained 5.4 +wg/g of amino nitrogen, indicating that most of the amino groups in the product were acylated. .

Reference Example 2C-3 Triethanolamine salt of anolate of total protein hydrolyzate with isostearic acid Reference Example IC-3 was used in place of the total protein hydrolyzate obtained in Reference Example 1G-1 in Reference Example 2C-1. Using 500 g of a 30% aqueous solution of the obtained total protein hydrolyzate, 43.2 g of isostearic acid chloride (1.0 equivalent of the total protein hydrolyzate) was used instead of lauric acid chloride, and 30% potassium hydroxide aqueous solution was used. Triethanolamine brine f4 solution of acylated product with isostearic acid of total protein hydrolyzate with a strength of 30% was prepared in the same manner as in Reference Example 2C-1 except that triethanolamine was used instead.
Obtained 0g. The yield was 92%.

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

Reference Example 3 Production of quaternary ammonium derivative of animal protein hydrolyzate Reference Example 3A Production of quaternary ammonium derivative of collagen hydrolyzate Reference Example 3A-1 Collagen hydrolyzate obtained in Reference Example IA-1 40 of
% aqueous solution 500 g (average molecular weight of collagen hydrolyzate 900, total 1310 t remol of aminonitrogen)
and 150 g of isopropyl alcohol were placed in a reaction vessel, and g of isopropyl alcohol containing lauryl chloride (1.0 equivalent of collagen hydrolyzate) with a concentration of 20% was added dropwise at 40°C over 1 hour, and during that time 2
Add 0% sodium hydroxide aqueous solution dropwise to adjust the p of the reaction solution.
H was maintained at 9.5. After dropping lauryl chloride, stirring was continued for 2 hours while maintaining the pH at 9.5.
After the mixture was left to stand for 24 hours, the amount of amino nitrogen was measured, and the total amount of amino nitrogen was 12 mmol, indicating that 96% of the amino nitrogen had reacted. After laurylating the collagen hydrolyzate in this way, the reaction mixture was concentrated under reduced pressure to remove water and isopyrroalcohol, and then 400 g of n-butyl alcohol was added to dissolve the product and remove insoluble matter. The remaining by-product sodium chloride and a small amount of unreacted material were filtered off. Transfer the filtrate to Mitsurocolben, and add 75.9 g of benzyl chloride to this.
(twice the equivalent of the laurylated product) and 20 g of sodium hydrogen carbonate were added, and a condenser was attached to heat and stir, and the reaction was carried out at a liquid temperature of 110° C. for 2 hours. After removing the remaining by-product sodium chloride along with insoluble materials by decantation, 400 g of ion-exchanged water was added to the n-
Butyl alcohol was azeotropically distilled off with water under reduced pressure. Furthermore, by adding a small amount of water and repeating azeotropy, n-butyl alcohol was completely removed. Dissolve the product in water and prepare an aqueous solution of chloride of lauryl dibenzylammonium derivative of collagen hydrolyzate with a concentration of 30% 112
Obtained 0g.

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

Furthermore, in order to confirm that the collagen hydrolyzate and lauryl dibenzoyl were bonded, the obtained aqueous solution was subjected to gel filtration, and the above-mentioned characteristic reaction was performed on each molecular weight fraction. Each fraction was positive for the quaternary ammonium salt reaction, confirming that the collagen hydrolyzate and lauryl dibenzoyl were bound together.

Reference Example 3A-2 Collagen hydrolyzate obtained in Reference Example IA-2 35
% aqueous solution 1 kg (average molecular weight of collagen hydrolyzate 5
00, total amount of amino nitrogen (697 mmol) was placed in a reaction vessel, and while stirring, 228 g of CTA aqueous solution with a concentration of 49% (1 i
) was added dropwise over a period of 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 9.5.
maintained. After the dropwise addition of CTA, stirring was continued for 5 hours while maintaining the pH at 9.5, and then after being left for 24 hours, amino nitrogen was measured, and the total amount of amino nitrogen was 147 mmol. Seventy-nine percent of the status ia iAs responded. Next, the reaction solution was passed through a 320 mJ resin column of strongly acidic cation exchange resin Diaion 5K-IB (trade name, Mitsubishi Chemical Industries, Ltd.), and the pH was adjusted to 6.9.
The sodium ions in the reaction solution and the slightly remaining unreacted CTA are adsorbed onto an ion exchange resin.
The ion exchange resin was then removed to obtain an aqueous solution of a quaternary trimethylammonium derivative of collagen hydrolyzate having a concentration of 3094.

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.

Further, 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 it was bound to CTA.

Reference Example 3A-3 Collagen hydrolyzate obtained in Reference Example IA-3 35
% aqueous solution 800 g, (average molecular weight of collagen hydrolyzate 1,700, total amount of amino nitrogen 140 t)
63.1 g of CTA aqueous solution (1.0 equivalent of collagen hydrolyzate) with a concentration of 49% was added dropwise to the reaction vessel over 1 hour while stirring at 30°C. The pH of the reaction solution was maintained at 11.0 by appropriately dropping an aqueous sodium oxide solution. After finishing dropping CTA, p
Stir for 3 hours while maintaining H at 11.0 1? After the mixture was left for 24 hours, the amino nitrogen was measured, and the total amount of amino thia 1A was 14 mmol.
90% of the amino nitrogen had reacted. Next, add a weakly acidic cation exchange resin Amberlite IRC-50 to the reaction solution.
(Previously mentioned) Add 120 mIt to adsorb the sodium ions in the reaction solution and the slight remaining unreacted CTA to the ion exchange resin, then remove the ion exchange resin and add collagen hydrate to a concentration of 30%. An aqueous solution of a quaternary trimethylammonium derivative as a decomposition product 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.

Further, 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 it was bound to CTA.

Reference Example 3B Production of quaternary ammonium derivative of keratin hydrolyzate Reference Example 3B-1 40% of keratin hydrolyzate obtained in Reference NIB-1
900 g of aqueous solution (average molecular weight of keratin hydrolyzate 800, total amount of amino nitrogen 430 mmol) was placed in a reaction vessel, and while stirring, 148 g of CTA aqueous solution with a concentration of 49% (0.g equivalent of keratin hydrolyzate) was added. 3
The reaction solution was added dropwise over a period of 0 minutes, and a 20% aqueous sodium hydroxide solution was appropriately added dropwise during this period to maintain the pH of the reaction solution at 10.0. After dropping CTA, stirring was continued for 2 hours while maintaining the pH at 10.0, and then left for 24 hours.
When amino nitrogen was measured, the total amount of amino nitrogen was 52 mmol, and 88% of the amino thiadine had reacted. Next, 220 mA of weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) was added to the reaction solution to neutralize it to GIH6,5, and the sodium ions in the reaction solution and the slight remaining unreacted CTA were added to the reaction solution. was adsorbed on ion-exchange heat exchange resin, and then the ion-exchange resin was removed to obtain an aqueous solution of a quaternary trimethylammonium derivative of keratin hydrolyzate with a concentration of 30%.

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

In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as Reference 1i13A-1, and a quaternary ammonium salt type reaction was performed on each molecular weight fraction. It was confirmed that they are connected.

Reference Example 3B-2 40% of the keratin hydrolyzate obtained in Reference Example IB-2
1fi900 g of water (average molecular weight of keratin hydrolyzate 1,200, total amount of amino nitrogen 272 mmol) was placed in a reaction vessel, and while stirring, CT with a concentration of 49% was added.
'A aqueous solution 88.7g (keratin hydrolyzate 0°8
5 equivalents) 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 p)l of the reaction solution at 10.5. After dropping CTA, adjust the pH to 10.
．． Stirring was continued for 2 hours while maintaining the temperature at 5.5, and then left to stand for 24 hours. When the amino nitrogen was measured, the total amount of amino nitrogen was 61 mmol, and 78% of the amino nitrogen had reacted. Ta. Next, strongly acidic cation exchange hot oil Diaion 5K-IB (mentioned above) 2 was added to the reaction solution.
00 ml was added to neutralize to pH 6.9, and sodium ions in the reaction solution and a slight amount of unreacted CT remained.
A 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 keratin 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 carried out in the same manner as in Reference Example 3A-1, and when each molecular weight fraction was subjected to a quaternary ammonium salt type reaction, each fraction was positive, indicating that keratin hydrolysis It was confirmed that the substance and CTA were bound together.

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) and 100 g of isopropyl alcohol were placed in a reaction vessel and heated at 40°C.
While stirring, 561 g of an isopropyl alcohol solution of cetyl chloride with a concentration of 20% (1.0 equivalent of keratin hydrolyzate) was added dropwise over 1 hour.
% sodium hydroxide aqueous solution dropwise as needed to adjust the pH of the reaction solution.
was maintained at 9.5. After finishing dropping cetyl chloride,
Stirring was continued for 1 hour 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 17 mmol, which was 96% of the amino nitrogen. was reacting. After cetylizing the keratin hydrolyzate in this way, the reaction mixture was evaporated under reduced pressure to remove water and isopropyl alcohol.
mj was added to dissolve the product, and by-product sodium chloride remaining as an insoluble matter and a small amount of unreacted matter were filtered off.

Next, add the acid solution, 50.2 g of methyl chloride (2.4 times equivalent of the cetyl reaction product), and 35 g of sodium hydrogen carbonate.
The mixture was heated in an autoclave at 110°C for 3 hours. After cooling, the reaction mixture was filtered and the isopropyl alcohol was removed by vacuum concentration to obtain 430 g of a viscous syrup of the chloride of the cetyldimethylammonium derivative of the product keratin hydrolyzate.

After diluting the obtained viscous syrup with water, reference example 3A-
When a quaternary ammonium salt reaction was performed in the same manner as in Example 1, all results were positive.

In addition, the water diluted solution of the obtained viscous syrup was subjected to gel filtration 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. It was confirmed that the decomposition product and cetyldimethyl were combined.

Reference Example 3C Production of quaternary ammonium derivative of total protein hydrolyzate Reference Example 3C-1 30% of total protein hydrolyzate obtained by 1η in Reference Example IC-1
% aqueous solution 1°200 g (average molecular weight of total protein hydrolyzate 500, total amount of amino nitrogen 730 mmol)
was placed in a reaction vessel, heated to 40°C, and while stirring, 247 g of 1 tL of CTA aqueous solution with a concentration of 50% (11 per 0.g of total protein hydrolyzate) was applied to the skin over 30 minutes. The pH of the reaction solution was maintained at 10.0 by appropriately dropping an aqueous sodium hydroxide solution. After the completion of dropping CTA, stirring was continued for 2 hours while maintaining the pH at 4lo, o, and then after being left for 24 hours, amino nitrogen was measured, and the total amount of amino nitrogen was 81 mmol.
89% of the amino nitrogen was reacted. Next, a weakly acidic cation exchange resin Amberlite IR (, -5
Add 100 ml of the above solution, neutralize to pH 6.7, adsorb the sodium ions in the reaction solution and the slight remaining unreacted CTA onto the ion exchange resin, and then remove the ion exchange resin. Thus, an aqueous solution of a quaternary trimethylammonium derivative of 30% total protein hydrolyzate 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. It was confirmed that the substance and CTA were bound together.

Reference Example 3C-2 500 g of the aqueous solution of the total protein hydrolyzate obtained in Reference Example IC-3 at a concentration of 35% (average molecular weight of the total protein hydrolyzate 1,800, total amount of amino nitrogen 95 mmol) was Add C at a concentration of 49% to a reaction vessel while stirring.
30.4 g of TA aqueous solution (0.4 g of Ifi protein hydrolyzate)
85 equivalents) was added dropwise over 1 hour, and during that time 20%
While maintaining the pH of the reaction solution at 10.0 by adding an appropriate amount of sodium hydroxide aqueous solution dropwise, stirring was continued for 2 hours.After standing for 24 hours, amino nitrogen was measured, and the total amount of amino nitrogen was measured. was 17 mmol, and 82% of the amino-definition reacted. Next, 80m6 of the strongly acidic cation exchange resin Diaion 5K-IB (mentioned above) was added to the reaction solution to neutralize it to pH 6.9, and the sodium ions in the reaction solution and the slightly remaining unreacted CT were added to the reaction solution.
A was adsorbed on ion exchange) H fat, and then the ion exchange resin was removed to obtain a quaternary trimethylammonium derivative aqueous solution of total protein 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 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 each molecular weight fraction was subjected to a quaternary ammonia salt reaction. As a result, each fraction was positive, indicating that total protein hydrolysis It was confirmed that the substance and CTA were bound together.

Reference Example 3C-3 30% of the total protein hydrolyzate obtained in Reference Example IC-3
500 g of an aqueous solution (average molecular weight of total protein hydrolyzate 1,050, total amount of amino chinogen 140 lmol) was placed in a reaction vessel, and while stirring at 50°C, a concentration of 20
% decyl chloride in isopropyl alcohol solution 2
47 g (2.0 equivalents of total protein hydrolyzate) was added dropwise over a period of 2 hours, and during this period, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain the pH of the reaction solution at 9.5. After dropping the decyl chloride, stirring was continued for 1 hour while maintaining the pH at 9.5, and then left to stand for 24 hours. When the amino nitrogen was measured, the total amount of amino nitrogen was less than 1 mmol. Ta. When the amount of decyl chloride and its hydrolyzate, decyl alcohol, in the above reaction solution was quantitatively determined, the total amount of both was 12 mmol, indicating that didecyl chloride was carried out with a yield of 92% or more. .

After completing the didecylation of the total protein hydrolyzate in this manner, the reaction mixture was concentrated under reduced pressure to remove water and isopropyl alcohol, and after distilling off the water, 500 mN of isopropyl alcohol was added to dissolve the product. Then, by-product sodium chloride remaining as insoluble matter and a small amount of unreacted material were filtered off, and a mixture of the filtrate, 8.5 g of methyl chloride, and 6 g of sodium hydrogen carbonate was placed in an autoclave for 11 hours.
After heating at 0° C. for 2 hours and cooling, the reaction mixture was filtered and the isopropyl alcohol was removed by vacuum concentration to obtain 210 g of a viscous syrup of didenylmethylammonium derivative of the total protein hydrolyzate of the product. .

The resulting viscous syrup was diluted with water and 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 water diluted solution of the obtained viscous tubercle, gel filtration was performed in the same manner as in Reference Example 3A-1, and each molecular weight fraction was subjected to a quaternary ammonium salt characteristic reaction, and each fraction was positive. It was confirmed that the total protein hydrolyzate and didenylmethyl were bonded.

Example 1 Sodium lauryl sulfate is 8%, Reference Examples 2A-1 to 3C
The anolated product of the animal protein hydrolyzate obtained in step-3 or its salt and the quaternary ammonium derivative of the animal protein hydrolyzate were at the concentrations shown in Table 2, EDTA was 0.1%,
A shampoo composition containing an appropriate amount of fragrance and the balance consisting of purified water was prepared, and its performance was evaluated using the method shown below. The types of animal protein hydrolyzate derivatives used in the preparation of the above Noyanpu composition are indicated by reference example numbers.

fi+ Foaming Test A foaming test was carried out using the Wilmsmann method. In other words, a plastic cylinder (diameter 6ω x
Pour 1200 ml of a 20% aqueous solution of Nyanpu composition (anionic surfactant concentration: 4.0%) into a constant temperature bath (25 degrees Celsius) with a height of 36 cm and 1 liter, and rotate the dedicated plano (2,0 OOr, A method was used in which the amount of bubbles generated was measured by foaming (p, i, 5 minutes).A commercially available product was used for the foaming test using the Willsmann method. Not only the spread, but also the stability of the foam after the rotation of the plan is stopped.
Can be determined. The measurement results regarding foam spread and foam stability are shown in Table 2. Foam spread is the total volume of foam produced by the rotation of the brush, and foam stability is the amount of foam generated by the rotation of the brush. The volume of water surface arising from the bottom of the cylinder is 1
The time taken to reach 00 ml is shown in seconds.
This indicates that the longer the time period, the better the stability of the foam. ' In addition, in this test, 0.4 g of synthetic fat having the composition shown below was added to 200 mg of the test liquid (approx.
%) and used as a substitute for natural hair stains.

Composition of synthetic fats Lanolin 20% Coconut oil 20% Paraffin oil 20% Vaseline 20% Cetyl alcohol 10% Castor oil 10% (2) Feeling when washing hair Products of the present invention (shampoo composition of Example 1 in Table 2) Two female panelists washed their hair once a day using Sample No. 1-15) and its control product (Sample No. 16 in Table 2), and compared both Noyanpu compositions according to each item shown in Table 3. I conducted a test. The amount of each nyanpu composition used was 5 g per hair wash.

Example 2 Shampoo compositions having the formulations shown in Table 4 (using sample numbers 21 to 25 and commercially available Noyanpu compositions A-C,
The degree of eye irritation was tested using the raize method.

That is, five healthy domestic rabbits (male, white) weighing 2.3 to 2.7 kg were given shampoo composition Q, jmj! The cornea, iris, and mucous membrane were observed 1 hour and 24 hours after instillation into the eyes, and the results were scored using the following assay method, and the average value for the five birds was determined.

The score obtained by multiplying the product of the obtained average values of each item for the cornea by 5, the value obtained by multiplying the average value of the iris by 5, and the value obtained by multiplying the sum of the average values of each item for the mucous membrane by 2 are combined. The results are shown in Table 5, in which the larger the total score (0), the stronger the irritation to the eyes.

Test method 1 Cornea: Opacification 0-4 Capsule area 0-4 2 Iris: Hyperemia θ-2 3 Conjunctiva: Redness 0-3 Floating I! θ~4 Secretion 0~3 [Effects of the Invention] As explained above, according to the present invention, Noyamp's original performance is excellent, and it imparts flexibility, smoothness, and good combability to the hair, A Nyanpu composition that is less irritating to the eyes and scalp has been provided.

gp;・(-↓1

Claims (4)

[Claims] (1) A shampoo containing an anionic surfactant is blended with an acylated product of animal protein hydrolyzate or its salt and a quaternary ammonium derivative of animal protein hydrolyzate. shampoo composition. (2) The acylated product of animal protein hydrolyzate or its salt has the following general formula (I) ▲ Numerical formula, chemical formula, table, etc. ▼ (I) (In the formula, R_1 is a long chain with 8 to 2 carbon atoms. It is an alkyl group or an alkenyl group, and R_2 is a side chain of an amino acid constituting the animal protein hydrolyzate. n is an integer from 3 to 20, and M is an alkali metal such as hydrogen, sodium, or potassium, ammonium, or Ethanolamine, diethanolamine, triethanolamine, 2-amino-
2. The shampoo composition according to claim 1, which is an acylated product of an animal protein hydrolyzate or a salt thereof. (3) The quaternary ammonium derivative of animal protein hydrolyzate has the following general formula (II) ▲ There are mathematical formulas, chemical formulas, tables, etc. ▼ (In the formula, R_2 and n are the same as in the above general formula (I) is a quaternary trimethylammonium derivative of animal protein hydrolyzate represented by R_2 is a side chain of an amino acid constituting the animal protein hydrolyzate, and n is an integer from 3 to 20. A shampoo composition according to claim 1 or 2. (4) The quaternary ammonium derivative of animal protein hydrolyzate has the following general formula (III) ▲There are mathematical formulas, chemical formulas, tables, etc.▼(III) (R_2 and n are the same as in the above general formula (I) R_2 is the side chain of the amino acid constituting the animal protein hydrolyzate, n is an integer from 3 to 20, R_
3. At least one of R_4 and R_5 has 8 to 20 carbon atoms
is a long-chain alkyl group or hydroxyalkyl group,
The remainder is an alkyl group, hydroxyalkyl group, or benzyl group having 1 to 3 carbon atoms. The shampoo composition described in Section 1.