JP2007277195A - Cosmetic base and method for producing the same - Google Patents

Abstract

<P>PROBLEM TO BE SOLVED: To obtain a cosmetic base that is mixed with a hair cosmetic, provides the hair with gloss, moisture and softness and has improved combing property by heat treatment after application to the hair, has a high heat active effect and excellent storage stability and comprises a silylated hydrolyzed peptide and to provide a method for producing the same. <P>SOLUTION: The cosmetic base is obtained by hydrolyzing a silane coupling agent represented by general formula (I) (R<SP>1</SP>, R<SP>2</SP>and R<SP>3</SP>are each a 1-3C alkoxy group or a 1-3C alkyl group and at least two of R<SP>1</SP>, R<SP>2</SP>and R<SP>3</SP>are 1-3C alkoxy groups) in an aqueous solution containing a 1-3C lower monohydric alcohol and then reacting the resulting substance with an amino group containing a side-chain amino group of a hydrolyzed peptide. The concentration of the 1-3C lower monohydric alcohol is preferably 2-20 mass% in the aqueous solution and the number-average molecular weight of the hydrolyzed peptide is preferably 200-3,000. <P>COPYRIGHT: (C)2008,JPO&INPIT

Description

  The present invention relates to a cosmetic substrate comprising a silylated hydrolyzed peptide useful as a hair cosmetic substrate, such as a hair conditioner, a hair setting agent, and a permanent wave agent, and more particularly to a method for producing the same. The present invention relates to a cosmetic base material composed of a silylated hydrolyzed peptide having a high effect and imparting excellent luster and smoothness to hair when heat-treated after application to hair, and a method for producing the same.

  Conventionally, silicone oil (organosilicone compound) and polypeptide are blended into hair cosmetics, and the excellent extensibility of silicone oil, imparting gloss and luster to hair, protecting effect by imparting water repellency to hair, etc. Attempts have been made to exhibit the sorption effect on the hair of the polypeptide, the action of alleviating skin irritation, the protective action and the moisturizing action of the film.

  However, since silicone oil is inherently a hydrophobic (lipophilic) substance and polypeptide is inherently a hydrophilic substance, they are not compatible with each other. When they are used in combination, they are emulsified. Due to lack of stability and easy separation, there was a problem that the commercial value of cosmetics was easily impaired. In addition, it is difficult for the polypeptide to adhere to the portion previously contacted with the silicone oil, and conversely, the silicone oil cannot adhere to the portion previously contacted with the polypeptide, so that both characteristics can be fully exhibited. There was also a problem that it was not possible.

  Therefore, in order to solve the above problem, a protein-silicone copolymer in which silicone or a silane compound is bound to a protein hydrolyzate (hydrolyzed peptide) [for example, JP-A-5-148119 (Patent Document 1) JP 2005-520024 (Patent Document 2)] and silylated derivatives of hydrolyzed peptides [for example, JP-A-8-59424 (Patent Document 3), JP-A-8-67608 (Patent Document 4). Etc.] have been developed.

  In recent years, silicone derivatives and silylated derivatives of these hydrolyzed peptides have been proposed for use in hair cosmetics in particular. As reported in Japanese Patent Application Laid-Open No. 2000-302647 (Patent Document 5), when a hydrolyzed peptide silylated derivative is applied to the hair and heat-treated, the hydrolyzed peptide sorbs on the hair. The hydroxyl groups bonded to the silyl group of the hydrolyzed peptide that is attached to the silyl group are condensed on the hair by heating, and the excellent extensibility, which is the characteristic of silicone, imparts gloss and luster to the hair. This is because a so-called heat active effect has been found.

  By the way, as mentioned above, since silicone has poor solubility in water-based cosmetics, in order to maintain storage stability, it is necessary to make the silicone part a short chain, and also exhibits a heat active effect during use. In order to achieve this, it is necessary that the hydroxyl group bonded to the silyl group bonded to the peptide does not condense during the production, and that many hydroxyl groups are present until it is used as a cosmetic.

  However, the protein-silicone copolymers of Patent Document 1 and Patent Document 2 are not described in proportion, but the hydroxyl groups directly linked to the silyl group are condensed to form two peptide chains via the silicone chain. It is obtained as a mixture of a bonded polymer and a monomer in which a silane compound is bonded to the terminal of the peptide, and the storage stability is poor due to the presence of a high molecular polymer. In addition, the heat active effect such as glossiness and smoothness imparted by thermal condensation cannot be expected so much.

On the other hand, the silylated hydrolyzed peptides of Patent Document 3 and Patent Document 4 have one silyl group having a hydroxyl group bonded to the amino group of the peptide chain, and are stable in storage even when formulated in aqueous cosmetics. The heat active effect can be expected. However, since the reaction is controlled so as to suppress the condensation of hydroxyl groups bonded to the silyl group at the time of production, particularly in the case of using a silane coupling agent that becomes a silyl group having three hydroxyl groups that are easily condensed. The introduction rate of silyl groups was as low as about 60%, and there was a problem that the heat active effect during use was slightly inferior.
JP-A-5-148119 JP 2005-520024 Gazette JP-A-8-59424 JP-A-8-67608 JP 2000-302647 A

  Accordingly, the present invention provides a silylated hydrolyzed peptide that eliminates the above-mentioned problems, has a high heat active effect during use, and is excellent in storage stability and is useful as a hair cosmetic base and a method for producing the same. This is the issue. That is, according to the production method of the present invention, silyl is useful as a cosmetic base material that can give hair gloss, moisture, smoothness and improve combability by heat treatment after application to hair. Hydrolyzed peptides can be easily produced.

（式中、Ｒ^１、Ｒ^２、Ｒ^３は同一でも異なっていてもよく、炭素数１〜３のアルコキシ基または炭素数１〜３のアルキル基であるが、Ｒ^１、Ｒ^２、Ｒ^３のうち少なくとも２個は炭素数１〜３のアルコキシ基である）
で表されるシランカップリング剤を、炭素数１〜３の低級一価アルコールを含有する水溶液中で加水分解し、その後、加水分解ペプチドの側鎖のアミノ基を含むアミノ基に反応させることで、上記課題を解決し、使用時のヒートアクティブ効果が高く、しかも保存安定性に優れたシリル化加水分解ペプチドが製造できることを見出し、本発明の完成にいたった。 As a result of intensive studies to solve the above problems, the present inventors have found that the following general formula (1)

(In formula, R < ¹ >, R < ² >, R < ³ > may be same or different, and is a C1-C3 alkoxy group or a C1-C3 alkyl group, but R < ¹ >, R < ² >, R < ³ >. Of which at least two are alkoxy groups having 1 to 3 carbon atoms)
Is hydrolyzed in an aqueous solution containing a lower monohydric alcohol having 1 to 3 carbon atoms, and then reacted with an amino group containing an amino group on the side chain of the hydrolyzed peptide. In order to solve the above problems, it was found that a silylated hydrolyzed peptide having a high heat active effect at the time of use and excellent storage stability could be produced, and the present invention was completed.

  That is, according to the present invention, when hydrolyzing an alkoxy group directly bonded to a silicon atom of the silane coupling agent represented by the general formula (1) in water, a lower monohydric alcohol having 1 to 3 carbon atoms is contained. In this way, the solubility of the silane coupling agent and the stability in water are improved, and condensation of hydroxyl groups during hydrolysis and subsequent reaction with the hydrolyzed peptide is not only suppressed. The reactivity with the amino group is also improved. Therefore, the silylated peptide obtained by the production method of the present invention has a very high heat active effect during use.

  Moreover, the present inventors have an alcohol content of 2 in an aqueous solution containing a lower monohydric alcohol having 1 to 3 carbon atoms when hydrolyzing the silane coupling agent represented by the general formula (1). The number average molecular weight of the hydrolyzed peptide into which silyl functional groups are introduced is preferably from 20 to 20% by mass, and the introduction rate of silyl functional groups with a number average molecular weight of 200 to 3,000, the heat active effect when used as cosmetics, and cosmetics It was found that it is preferable from the viewpoint of storage stability.

  The cosmetic base material comprising the silylated hydrolyzed peptide of the present invention can improve the combing property by imparting luster, moisture and smoothness to the hair by a so-called heat active effect that is heat-treated after application to the hair. It is excellent in storage stability. Moreover, according to the manufacturing method of this invention, the silylated hydrolyzed peptide excellent in these effects can be manufactured easily.

  Hereinafter, the preferred embodiments of the present invention are more specifically divided into hydrolyzed peptide moieties, silane coupling agents, hydrolysis of silane coupling agents, production of silylated hydrolyzed peptides, and structure and properties of silylated hydrolyzed peptides. Explained.

[Hydrolyzed peptide]
The hydrolyzed peptide used in the production of the silylated hydrolyzed peptide which is the cosmetic base material of the present invention is obtained by partially hydrolyzing a naturally derived protein (protein) with acid, alkali, enzyme or a combination thereof. Protein sources include collagen (including gelatin which is a modified product thereof), keratin, silk fibroin, sericin, casein, conchiolin, elastin, chicken egg yolk protein, egg white protein Soybeans, peas, wheat, beer lees, corn, rice (rice lees), plant-derived ones such as potato proteins, yeasts of the genus Saccharomyces, Candita, and Endomycopsis -Isolated from yeast proteins, mushrooms (basidiomycetes) and chlorella isolated from yeast yeast called sake yeast Npaku include those derived from microorganisms such as.

  The hydrolyzed peptide used for silylation can be obtained by hydrolyzing the above protein with acid, alkali, enzyme or a combination thereof. At this time, the amount of acid, alkali or enzyme used, reaction temperature or reaction is used. By appropriately selecting the time, the number average molecular weight of the obtained hydrolyzed protein can be made a preferable value of 200 to 3,000. The number average molecular weight used in the present invention is a calculated value obtained by multiplying the amino acid polymerization degree obtained from the total nitrogen amount and amino nitrogen amount of the hydrolyzed peptide by the average amino acid molecular weight of each protein.

  The number average molecular weight of the hydrolyzed peptide is preferably 200 to 3,000, more preferably 250 to 2,500, from the viewpoints of sorption to hair, film-forming property, and storage stability in cosmetics. That is, when the number average molecular weight of the hydrolyzed peptide is not more than the above range, the proportion of the silyl group in the silylated hydrolyzed peptide is increased and storage stability is deteriorated. If the number average molecular weight exceeds the above range, the proportion of silyl groups in the silylated hydrolyzed peptide is small and the hair sorption and film-forming action may be deteriorated. This is because not only can the gloss and smoothness imparting properties and good extensibility of the silicones not be exhibited, but also high molecular weight peptides may associate with each other during storage to easily cause insoluble matter.

（式中、Ｒ^１、Ｒ^２、Ｒ^３は同一でも異なっていてもよく、炭素数１〜３のアルコキシ基または炭素数１〜３のアルキル基であるが、Ｒ^１、Ｒ^２、Ｒ^３のうち少なくとも２個は炭素数１〜３のアルコキシ基である）
で表されるもので、具体例としては、３−グリシドキシプロピルメチルジメトキシシラン、３−グリシドキシプロピルメチルジエトキシシラン、３−グリシドキシプロピルメチルジプロポキシシラン、３−グリシドキシプロピルエチルジメトキシシラン、３−グリシドキシプロピルエチルジエトキシシラン、３−グリシドキシプロピルエチルジプロポキシシラン、３−グリシドキシプロピルトリメトキシシラン、３−グリシドキシプロピルトリエトキシシランなどが挙げられる。 〔Silane coupling agent〕
The silane coupling agent used in the method for producing a silylated hydrolyzed peptide of the present invention is represented by the following general formula (1).

(In formula, R < ¹ >, R < ² >, R < ³ > may be same or different, and is a C1-C3 alkoxy group or a C1-C3 alkyl group, but R < ¹ >, R < ² >, R < ³ >. Of which at least two are alkoxy groups having 1 to 3 carbon atoms)
Specific examples include 3-glycidoxypropylmethyldimethoxysilane, 3-glycidoxypropylmethyldiethoxysilane, 3-glycidoxypropylmethyldipropoxysilane, and 3-glycidoxypropyl. Examples include ethyldimethoxysilane, 3-glycidoxypropylethyldiethoxysilane, 3-glycidoxypropylethyldipropoxysilane, 3-glycidoxypropyltrimethoxysilane, and 3-glycidoxypropyltriethoxysilane.

（式中、Ｒ^１は水酸基または炭素数１〜３のアルキル基である）
で表されるものに変換される。 [Hydrolysis of silane coupling agent]
The reaction between the hydrolyzed peptide and the silane coupling agent represented by the general formula (1) is performed by first using the silane coupling agent in an aqueous solution containing a lower monohydric alcohol having 1 to 3 carbon atoms at 20 to 40 ° C. By stirring for 5 to 20 minutes, the alkoxy group bonded to the silicon atom is converted into a hydroxyl group. That is, the silane coupling agent has the following general formula (2)

(Wherein R ¹ is a hydroxyl group or an alkyl group having 1 to 3 carbon atoms)
Is converted to the one represented by.

  Examples of the lower monohydric alcohol having 1 to 3 carbon atoms to be used include methanol, ethanol, propanol, and isopropanol. Since silylated hydrolyzed peptides are used in cosmetics, safety and odor From this point of view, ethanol is preferred.

  And the alcohol concentration of the aqueous solution containing a C1-C3 lower monohydric alcohol has preferable 2-20 mass%, and its 5-15 mass% is more preferable. This is because if the alcohol concentration is below the above range, the silane coupling agent in which the alkoxy group is converted to a hydroxyl group by hydrolysis may not be stably maintained, and if the alcohol concentration exceeds the above range, the next step This is because in the reaction with the hydrolyzed peptide, the hydrolyzed peptide may be aggregated or insolubilized.

  Conversion of alkoxy groups to hydroxyl groups by hydrolysis proceeds faster at higher temperatures, but 20-40 ° C is optimal because there is a risk of condensation between the hydroxyl groups. And although hydrolysis occurs on the acidic side or the basic side, the acidic side is more likely to occur, so it is preferable to adjust the aqueous solution containing the lower monohydric alcohol to pH 3.0 to 4.0. .

  The concentration of the silane coupling agent when hydrolyzing the silane coupling agent in an aqueous solution containing a lower monohydric alcohol having 1 to 3 carbon atoms is related to the number of alkoxy groups bonded to the silyl group and the alcohol concentration. Yes, it is difficult to define the numerical value, but there is a possibility that the possibility of condensation between the hydroxyl groups generated at a high concentration of the silane coupling agent is high, and it is preferable to make it about 10 to 20% by mass, In particular, 15 mass% or less is preferable in the silane coupling agent in which three hydroxyl groups are generated.

[Production of silylated hydrolyzed peptide]
A silylated hydrolyzed peptide is produced by dropping a solution containing a silane coupling agent prepared by converting an alkoxy group directly bonded to a silicon atom into a hydroxyl group as described above into a hydrolyzed peptide under stirring and bringing them into contact with each other. However, in this reaction, the hydrolyzed peptide is preferably in an aqueous solution of about 10 to 30% by mass. This is because if the concentration of the hydrolyzed peptide aqueous solution is too high, the hydroxyl groups directly bonded to the silicon atoms of the resulting silylated hydrolyzed peptide may be easily condensed.

  The dropping time of the hydroxylated silane coupling agent varies depending on the dropping amount, but it is preferably completed in about 30 minutes to 5 hours.

  Since the reaction proceeds on the basic side, it is necessary to add an alkaline solution such as sodium hydroxide or potassium hydroxide to adjust the pH of the peptide solution to 8 to 10, particularly 8.5 to 9.5. The reaction proceeds even at room temperature, but the reaction rate increases as the temperature increases. However, as the temperature increases, the concentration of the solution increases due to the volatilization of the solvent, and even if the pH is high, the possibility that the hydroxyl groups directly bonded to the silicon atoms condense increases. It is preferable to carry out at 50 ° C. In Patent Document 3 and Patent Document 4, the silylation reaction is carried out at 40 to 50 ° C. However, in the production method of the present invention, since a lower alcohol is added, a higher reaction rate is obtained at a lower temperature. can get.

  The progress and completion of the reaction can be confirmed by measuring the amount of amino nitrogen of the hydrolyzed peptide during the reaction by the van Slyke method.

  After completion of the reaction, the reaction solution is neutralized and purified as it is or by alcohol removal, ion exchange resin, dialysis membrane, electrodialysis, gel filtration, ultrafiltration, etc. However, after neutralization, condensation between hydroxyl groups tends to occur, and therefore concentration and dealcoholization are preferably performed under reduced pressure at low temperature.

[Structure and properties of silylated hydrolyzed peptides]
In order to incorporate the silylated hydrolyzed peptide into a hair cosmetic product and exhibit a heat active effect, the introduction rate of the silyl functional group and the molecular weight of the hydrolyzed peptide portion are important points. That is, in order to bring out the characteristics of the silyl functional group strongly, it is sufficient to use a hydrolyzed peptide having a small molecular weight and having an amino group in the side chain and a high amino acid content (a lot of basic amino acids). In order to emphasize the characteristics and add the nature of the silyl functional group to it, a peptide having a low amino acid content having an amino group in the side chain and having a high molecular weight may be used. However, in a low molecular weight peptide having a high amino acid content having an amino group in the side chain, if the introduction rate of the silyl functional group is extremely high, the hydrophilicity is reduced, the storage stability is deteriorated, and the original hair of the peptide is reduced. The sorption effect on the water is reduced. Conversely, when the introduction rate of the silyl functional group into the hydrolyzed peptide is too low, the heat active effect cannot be expected.

  Therefore, although the rate of introduction of the silyl functional group into the hydrolyzed peptide cannot be strictly defined, generally, the hydrolyzed peptide number average molecular weight is 200 to 600 and 60 to 75%, and the hydrolyzed peptide number average molecular weight is 600 to 600%. It is preferable that the introduction rate is 65 to 80% at 1500, the number average molecular weight of the hydrolyzed peptide is 1500 to 3000, and the introduction rate is 80% or more.

  Next, the present invention will be described more specifically with reference to examples, but the present invention is not limited to these examples. Prior to the examples, gel filtration analysis conditions used in the examples and the like will be described. Moreover, in the following examples etc., all the% which shows the density | concentration of a solution or a dispersion liquid is the mass%.

[Gel filtration analysis]
The gel filtration analysis was performed under the following conditions. The analysis results are shown in FIGS. 1 to 8 for each of the Examples and Comparative Examples. The results of the obtained silylated hydrolyzed peptides are indicated by solid lines, and the results of the raw hydrolyzed peptides are indicated by broken lines. The weight average molecular weight in the gel filtration analysis is a value calculated based on the detection position of the standard sample and the peak area of the measurement sample, and the value average molecular weight value obtained from the total nitrogen amount and amino nitrogen amount is Slightly different.

Analysis column: TSKgel G3000PWxL (7.8 mm ID × 30 cm) manufactured by Tosoh Corporation
Eluent: 0.1% trifluoroacetic acid-45% acetonitrile-water solution Elution rate: 0.3 ml / min
Detector: UV detector, 220 nm
Standard sample: Ribonuclease A (MW13,700)
Aprotinin (MW 6,500)
Insulin B chain (MW 3,496)
Bradykinin (MW 1,060)
Glutathione (MW 307)

Example 1
Hydrolyzed collagen (collagen hydrolyzate with a number average molecular weight of 1762) in 15% aqueous solution 100 g (8.51 mmol as the stoichiometric number of moles obtained by measuring the amount of amino nitrogen) was 20% hydroxylated. An aqueous sodium solution was added dropwise to adjust the pH to 9.5, and the mixture was heated to 40 ° C.

On the other hand, in General Formula (1), 2.1 g of silane coupling agent in which R ¹ is CH ₃ and R ² and R ³ are OCH ₃ (1.1 equivalent to the amount of amino nitrogen of hydrolyzed collagen) is 10 Dissolved in a 15% aqueous ethanol solution to a concentration of 15%, adjusted to pH 3.5 with dilute hydrochloric acid, and stirred at 30 ° C. for 15 minutes to hydrolyze the methoxy group (—OCH ₃ ) to a hydroxyl group. Converted.

  While stirring the above hydrolyzed collagen solution at 40 ° C., a silane coupling agent solution converted into a hydroxyl group was dropped into the solution over 1 hour. After completion of the dropwise addition, stirring was further continued at 45 ° C. for 3 hours to complete the reaction.

  After completion of the reaction, the amino nitrogen was measured to determine the introduction rate of the silyl functional group into the hydrolyzed collagen amino group. The introduction rate was 84%.

  After adjusting the pH of the reaction solution to 6.5 with dilute hydrochloric acid, dealcoholization was performed under reduced pressure and the concentration was adjusted to obtain 161 g of an aqueous solution having a reaction product (silylated hydrolyzed collagen) concentration of 10%.

  When the obtained reaction product and the raw material hydrolyzed collagen were subjected to gel filtration analysis, the weight average molecular weight according to the gel filtration analysis of the reaction product was 6,147, and the raw material hydrolyzed collagen was 4,970. The reaction product was about 1,100 larger than the raw material. However, these chromatograms are shown in FIG. 1. In the chromatogram of the reaction product shown by the solid line in FIG. 1, the component corresponding to the molecular weight more than twice that of the raw hydrolyzed collagen shown by the broken line is confirmed. No formation of a peptide polymer via a silicone chain due to condensation of hydroxyl groups was observed.

Example 2
20% of hydrolyzed wheat protein (hydrolyzed wheat protein, number average molecular weight 680) 20% aqueous solution 100 g (29.4 mmol as the stoichiometric mole obtained by measuring amino nitrogen content) An aqueous sodium hydroxide solution was added dropwise to adjust the pH to 9.5, and the mixture was heated to 40 ° C.

On the other hand, in the general formula (1), R ¹ , R ² and R ³ are all OCH ₂ CH ₃ silane coupling agent 7.4 g (0.9 equivalent to the amount of amino nitrogen of the hydrolyzed wheat peptide) Dissolve in a 10% ethanol aqueous solution to a concentration of 12%, adjust the pH to 3.5 with dilute hydrochloric acid, and continue stirring at 30 ° C. for 15 minutes to convert the OCH ₂ CH ₃ group directly bonded to the silicon atom to a hydroxyl group. Converted.

  While stirring the hydrolyzed wheat protein aqueous solution at 40 ° C., a silane coupling agent solution converted into a hydroxyl group was dropped therein over 1 hour. After completion of the dropwise addition, stirring was continued for 3 hours at 45 ° C. to complete the reaction.

  After adjusting the pH of the reaction solution to 6.5 with dilute hydrochloric acid, dealcoholization was performed under reduced pressure, and the concentration was adjusted to obtain 159 g of an aqueous solution having a reaction product (silylated hydrolyzed wheat protein) concentration of 15%. . The introduction rate of the silyl functional group was 77%.

  When gel filtration analysis of the obtained reaction product and raw material hydrolyzed wheat protein was performed, the weight average molecular weight by gel filtration analysis of the reaction product was 1,580, and the raw material hydrolyzed wheat protein was 932, The reaction product was about 650 larger than the raw material. However, those chromatograms are shown in FIG. 2. In the chromatogram of the reaction product shown by the solid line in FIG. 2, the component corresponding to the molecular weight more than twice that of the raw hydrolyzed wheat protein indicated by the broken line is It was not confirmed, and the production of a peptide polymer via a silicone chain due to condensation of hydroxyl groups was not observed.

Example 3
100 g of a 20% aqueous solution of hydrolyzed keratin (wool hydrolyzate having a number average molecular weight of 444) instead of hydrolyzed collagen (67.6 mmol as the stoichiometric mole obtained by measuring the amount of amino nitrogen) ), 16.7 g of a silane coupling agent in which R ¹ is CH ₃ and R ² and R ³ are OCH ₂ CH _{3 in} the general formula (1) (1. with respect to the amount of amino nitrogen of hydrolyzed keratin). 0 equivalents) was used in the same manner as in Example 1 to obtain 139 g of an aqueous solution having a reaction product (silylated hydrolyzed keratin) concentration of 15%. The introduction rate of the silyl functional group was 72%.

  As a result of gel filtration analysis of the obtained reaction product and raw material hydrolyzed keratin, the weight average molecular weight of the reaction product by gel filtration analysis was 1,506, and the raw material hydrolyzed keratin was 951. The product was about 550 larger than the raw material. However, those chromatograms are shown in FIG. 3. In the reaction product chromatogram shown by the solid line in FIG. 3, the components corresponding to the molecular weight more than twice that of the raw material hydrolyzed keratin shown by the broken line are confirmed. No formation of a peptide polymer via a silicone chain due to condensation of hydroxyl groups was observed.

Example 4
100 g of 20% aqueous solution of hydrolyzed soy protein (hydrolysate of soy protein, number average molecular weight 551) instead of hydrolyzed wheat protein (stoichiometric moles obtained by measurement of amino nitrogen as 36. In general formula (1), 6.9 g of a silane coupling agent in which R ¹ , R ² and R ³ are all OCH ₃ (0.8% relative to the amount of amino nitrogen of hydrolyzed soy protein) is used. Except that the equivalent amount was used, 151 g of an aqueous solution having a reaction product (silylated hydrolyzed soy protein) concentration of 15% was obtained in the same manner as in Example 2. The introduction rate of the silyl functional group was 65%.

  When the obtained reaction product and the raw material hydrolyzed soy protein were subjected to gel filtration analysis, the reaction product was subjected to gel filtration analysis with a weight average molecular weight of 2,032, and the raw material hydrolyzed soy protein was 1,440. The reaction product was about 600 larger than the raw material. However, those chromatograms are shown in FIG. 4. In the chromatogram of the reaction product shown by the solid line in FIG. 4, the components corresponding to the molecular weight more than twice that of the raw hydrolyzed soy protein shown by the broken line are It was not confirmed, and the production of a peptide polymer via a silicone chain due to condensation of hydroxyl groups was not observed.

Comparative Example 1
Using the same hydrolyzed collagen as in Example 1 and the same silane coupling agent, silylated hydrolyzed collagen was produced as follows according to the method of Patent Document 1.

Solid sodium hydroxide is added to 100 g of a 30% aqueous solution of hydrolyzed collagen to adjust the pH to 11, this solution is heated to 55 ° C., and under stirring, in formula (1), R ¹ is CH ₃ , R ² and 4.2 g of silane coupling agent with R ³ of OCH ₃ (1.1 equivalents relative to the amount of amino nitrogen of hydrolyzed collagen) was added dropwise over 1 hour, and stirring was continued at 60 ° C. for 5 hours after completion of the addition. And then left at 60 ° C. overnight.

  After completion of the reaction, the amount of amino nitrogen was measured to determine the rate of introduction of the silyl functional group into the amino group of the hydrolyzed collagen. The rate of introduction was 73%.

  The reaction solution was adjusted to pH 6 with dilute sulfuric acid and the concentration was adjusted to obtain 302 g of an aqueous solution having a reaction product (silylated hydrolyzed collagen) concentration of 10%.

  When gel filtration analysis of the obtained reaction product and raw material hydrolyzed collagen was performed, the weight average molecular weight according to gel filtration analysis of the reaction product was 36,600, and the raw material hydrolyzed collagen was 4,970. The reaction product was about 7 times larger than the raw material. FIG. 5 shows these chromatograms. In the chromatogram of the reaction product shown by the solid line in FIG. 5, a large peak corresponding to a molecular weight of five times or more of the raw hydrolyzed collagen shown by the broken line is seen. The silylated hydrolyzed collagen produced by this production method was a mixture of monomers not condensed with a polymer via a silicone chain, which is considered to be due to condensation between hydroxyl groups.

Comparative Example 2
Using the same silane coupling agent as the hydrolyzed wheat protein as in Example 2, silylated hydrolyzed wheat protein was produced in the same manner as in Comparative Example 1 as follows.

Solid sodium hydroxide was added to 100 g of a 30% aqueous solution of hydrolyzed wheat protein to adjust the pH to 11, and this solution was heated to 55 ° C. and stirred under the general formula (1), R ¹ , R ² and R ³ is OCH ₂ CH ₃ silane coupling agent 11.0 g (0.9 equivalents relative to the amount of amino nitrogen of hydrolyzed wheat protein) is added dropwise over 1 hour, and stirred at 60 ° C. for 5 hours after completion of the dropwise addition. And then left at 60 ° C. overnight.

  After completion of the reaction, the pH of the reaction solution was adjusted to 6 with dilute sulfuric acid, and the concentration was adjusted to obtain 238 g of an aqueous solution having a reaction product (silylated hydrolyzed wheat protein) concentration of 15%. The introduction rate of the silyl functional group was 71%.

  As a result of gel filtration analysis of the obtained reaction product and the hydrolyzed wheat protein of the raw material, the weight average molecular weight by the gel filtration analysis of the reaction product was 28,289, and the hydrolyzed collagen of the raw material was 932. The product was nearly 30 times larger than the raw material. FIG. 6 shows these chromatograms. In the chromatogram of the reaction product shown by the solid line in FIG. 6, a peak corresponding to a molecular weight of 10 times or more of the raw hydrolyzed collagen shown by the broken line is seen, The silylated hydrolyzed wheat protein produced by this production method was a mixture of monomers not condensed with a polymer via a silicone chain, which is considered to be due to condensation between hydroxyl groups.

Comparative Example 3
Using the same silane coupling agent as the hydrolyzed keratin as in Example 3, silylated hydrolyzed keratin was produced as follows according to the method of Patent Document 3.

  A 20% aqueous sodium hydroxide solution was added dropwise to 50 g of a 30% aqueous solution of hydrolyzed keratin to adjust the pH to 9.5, and the mixture was heated to 55 ° C.

On the other hand, in the general formula (1), 16.7 g of a silane coupling agent having R ¹ of CH ₃ and R ² and R ³ of OCH ₃ (1.0 equivalent to the amount of amino nitrogen of hydrolyzed keratin) was added to water. The solution was dissolved in a 15% aqueous solution, the pH was adjusted to 3.5 with dilute hydrochloric acid, and stirring was continued at 50 ° C. for 15 minutes to hydrolyze the methoxy group (—OCH ₃ ) and convert it to a hydroxyl group.

  While stirring the above hydrolyzed keratin solution at 55 ° C., a silane coupling agent solution converted into a hydroxyl group was dropped into the solution over 30 minutes. After completion of the dropwise addition, stirring was further continued at 55 ° C. for 5 hours to complete the reaction.

  The reaction solution is neutralized with dilute hydrochloric acid, desalted with an electrodialyzer, adjusted to pH 6.5, and concentrated to adjust the concentration of the reaction product (silylated hydrolyzed keratin). 148 g of an aqueous solution having a concentration of 15% was obtained. The rate of introduction of the silyl functional group into the amino group of the hydrolyzed keratin was 61%.

  As a result of gel filtration analysis of the obtained reaction product and raw material hydrolyzed keratin, the weight average molecular weight of the reaction product by gel filtration analysis was 1,492, the raw material hydrolyzed keratin was 951, and the reaction product The product was about 540 larger than the raw material. FIG. 7 shows these chromatograms, but in the chromatogram of the reaction product shown by the solid line in FIG. 7, no component corresponding to a molecular weight more than twice that of the raw material hydrolyzed keratin shown by the broken line is confirmed. The formation of a peptide polymer via a silicone chain due to condensation of hydroxyl groups was not observed.

Comparative Example 4
A silylated hydrolyzed peptide was produced in the same manner as in Comparative Example 3 using the same hydrolyzed soybean protein as in Example 4 and the same method as in Comparative Example 3.

  A 20% aqueous sodium hydroxide solution was added dropwise to 50 g of a 30% aqueous solution of hydrolyzed soybean protein to adjust the pH to 9.5, and the mixture was heated to 55 ° C.

On the other hand, in the general formula (1), 5.1 g of silane coupling agent in which R ¹ , R ² and R ³ are all OCH ₃ (0.8 equivalent to the amount of amino nitrogen of hydrolyzed soy protein) in water was dissolved to a 15% aqueous solution, the pH was adjusted to 3.5 with dilute hydrochloric acid, stirring continued for 15 minutes at 50 ° C., was converted to a methoxy group (-OCH ₃₎ hydrolyzing the hydroxyl group.

  While stirring the above hydrolyzed soy protein solution at 55 ° C., a silane coupling agent solution converted into a hydroxyl group was dropped into the solution over 30 minutes. After completion of the dropwise addition, stirring was further continued at 55 ° C. for 5 hours to complete the reaction.

  The reaction solution is neutralized with dilute hydrochloric acid, desalted with an electrodialyzer, adjusted to pH 6.5, and concentrated to adjust the concentration of the reaction product (silylated hydrolyzed soy protein). 99 g of a 15% aqueous solution was obtained. The rate of introduction of the silyl functional group into the amino group of the hydrolyzed soy protein was 60%.

  When the obtained reaction product and the raw material hydrolyzed soy protein were subjected to gel filtration analysis, the reaction product was subjected to gel filtration analysis and the weight average molecular weight was 1,996, and the raw material hydrolyzed soy protein was 1,440. The reaction product was about 550 larger than the raw material. FIG. 8 shows these chromatograms. In the chromatogram of the reaction product shown by the solid line in FIG. 8, a component corresponding to a molecular weight more than twice that of the raw hydrolyzed soy protein shown by the broken line is confirmed. In addition, the formation of a peptide polymer via a silicone chain due to condensation of hydroxyl groups was not observed.

[Storage stability of silylated hydrolyzed peptides]
The presence or absence of precipitates when the aqueous solutions of silylated hydrolyzed peptides obtained in Examples 1 to 4 and Comparative Examples 1 to 4 were stored at room temperature (however, 10 to 25 ° C.) for 90 days was visually examined. It was. The evaluation criteria are as follows.

Evaluation criteria +++: Very large amount of precipitate ++: Large amount of precipitate +: A slight amount of precipitate or turbidity is observed-: No precipitate is recognized

  The results are shown in Table 1. Table 1 also shows the types of peptides used in the synthesis of the silylated hydrolyzed peptides of the examples and comparative examples.

  As shown in Table 1, none of the silylated hydrolyzed peptides produced in Examples 1 to 4 produced turbidity or precipitates when stored at room temperature. On the other hand, in Comparative Examples, in Comparative Examples 1 and 2 produced by the method of Patent Document 1, precipitates were generated on the 15th day after storage. Further, in Comparative Examples 3 and 4 produced by the method of Patent Document 3, turbidity and precipitation were not generated even after storage for 90 days.

[PH stability of silylated hydrolyzed peptide]
The pH stability of the silylated hydrolyzed peptides prepared in Examples 1 to 4 and Comparative Examples 1 to 4 was examined. That is, a 10% aqueous solution of silylated hydrolyzed peptide was adjusted to pH 3, 4, 5, 7, 9, 10 with 6N hydrochloric acid or 20% sodium hydroxide, and the presence or absence of turbidity after standing at room temperature for 24 hours was checked. It was confirmed visually. The results are shown in Table 2. The evaluation criteria are the same as in the case of storage stability.

  As shown in Table 2, the silylated hydrolyzed peptides of Examples 1 to 4 did not show any turbidity at any pH, but in Comparative Examples 1 and 2, turbidity occurred at pH 3 and 4, and fine insoluble at pH 10 Things were precipitating. In Comparative Example 3, turbidity occurred at pH 3 and 4, but in Comparative Example 4, as in Example 4, no turbidity occurred at any pH.

  Next, the heat active effect of the silylated hydrolyzed peptide will be described with application examples in which the silylated hydrolyzed peptides produced in Examples 1 to 4 and Comparative Examples 1 to 4 are blended in various hair cosmetics.

Application example 1
Hair creams having the compositions shown in Table 3 were prepared, and each hair cream was applied to the hair, and then the gloss, moisture, and combing properties of the hair that had been hot-air dried with a hair dryer and the hair that had been cold-air dried with a hair dryer were evaluated. In addition, all content of each component in an implementation product and a comparison product is based on a mass part, and about content whose content is not solid content, a solid content density | concentration is shown in parenthesis after a component name. Moreover,% which shows the density | concentration of a solution or a dispersion liquid is mass.

  Treatment of the hair with the hair cream was performed as follows. That is, five hair bundles of 15 cm in length and 1 g in weight are prepared, each washed with a 2% aqueous solution of polyoxyethylene (3) sodium lauryl ether sulfate, rinsed in running tap water, and these hair bundles are Two were used for each of the product 1 and the comparative product 1, and one was used for the control product. With respect to these hair bundles, 0.5 g of the hair cream of the above-mentioned product 1 and comparative product 1 and the hair cream of the control product were applied to each hair bundle while spreading. Example Product 1 and Comparative Product 1 Each of the hair bundles was dried by applying hot air from a distance of 10 cm with a commercially available hair dryer of 1000 W. The hair bundle was dried with cold air using the same hair dryer. The temperature at the position of the hair bundle in hot air drying was 65 ° C. 30 seconds after the start of drying, and 72 ° C. at the end of drying of the hair bundle (2 minutes after the start of drying).

  Assess the ranking of the hair after drying as 10 panelists (6 women, 4 men), the control 1 as [1] and the best as [5] I let you. The average value is shown in Table 4 as an evaluation value.

  As shown in Table 4, when the hair cream containing the silylated hydrolyzed collagen produced in Example 1 was used, heat treatment was performed for any evaluation items of gloss, moisture, and combability of the hair after the treatment. When it was performed, the evaluation value was greatly increased as compared to when no heat treatment was performed (cold air drying), and it was confirmed that the silylated hydrolyzed collagen produced in Example 1 had a high heat active effect. On the other hand, the hair cream containing the silylated hydrolyzed collagen produced in Comparative Example 1 has little difference in the evaluation value between the heat-treated product and the cold-air dried product, and it can be said that there is almost no heat active effect. Even in the case of treatment, the evaluation value was almost the same as in the case of the cold air drying of the product 1.

Application example 2
After preparing hair rinses with the compositions shown in Table 5 and using each hair rinse on the washed hair, the gloss, moisture, combability and hair tension of hair that has been hot-air dried with a hair dryer and hair that has been cold-air dried with a hair dryer are adjusted. Examined.

  In the test, five hair bundles were prepared, each of the two hair bundles was treated with the hair rinse of the product 2 and the comparative product 2, one hair bundle was heated and dried with a hair dryer, and the other hair bundle was a hair. It dried with cold air with the dryer. Moreover, one hair bundle was processed with the hair rinsing of the control product, and this hair bundle was dried with cold air with a hair dryer.

  The treatment of the hair with the hair rinse was performed as follows. That is, five hair bundles having a length of 15 cm and a weight of 1 g were washed with a commercially available shampoo containing no hydrolyzed peptide or derivative thereof, and rinsed with hot water. After the hair bundle after washing, the hair rinse of the above-mentioned product 2, comparative product 2 and control product 2 was used for each hair bundle 2g, rinsed with hot water, and compared with product 2 Each hair bundle of product 2 is heated and dried with the same hair dryer as in application example 1 under the same conditions, and the hair bundle of each of the other product 2 and comparative product 2 and the control product is the same hair dryer. And dried with cold air. After repeating this shampoo washing, hair rinse treatment, and drying process 5 times, the hair gloss, moisture, and combability were evaluated by 10 panelists (6 women, 4 men) according to the same evaluation criteria as in Application Example 1. I let you. Next, 14 hairs were extracted from each hair bundle and subjected to the following hair beam evaluation test to compare the knot sizes.

[Evaluation method for hair tension]
A constant-humidity chamber with a relative humidity of 58% at room temperature with a light knot (knot) as shown in Fig. 9 at the center of a 15cm long hair, with the hair root side up and a 10g weight attached to the hair tip side. Hang in for 1 minute. Then, after removing the weight on the hair end side and suspending in the humidity chamber for 1 hour, the knot produced on the hair was photographed with a scanning electron microscope, and the size of the knot of the hair was based on the photographed image. The length (major axis) was measured with an image processing apparatus (JSM-5800LV manufactured by JEOL Ltd. was used for the scanning electron microscope, and SemAfore (trade name) manufactured by the same company was used for image processing). Measure the size of 14 hair knots per sample, exclude the results for the 4 hairs from the 2 largest to the smallest, and the 4 smallest hairs, with 10 hairs per sample. The average value was calculated | required about the result and it was set as the evaluation result. In addition, it means that there is "beam" in hair, so that the numerical value which shows an evaluation result is large (a knot is large).

  The evaluation results of hair gloss, moisture, combability and hair tension are shown in Table 6 as average values.

  As shown in Table 6, the heat-treated hair of Example 2 that was heat-dried using the hair rinse containing the silylated hydrolyzed wheat protein produced in Example 2 was used for the hair that had been air-dried using the same hair rinse. In comparison, the evaluation values of the gloss, moisture, and combability of the hair are all high, but in the case of the comparative product 2 containing the silylated hydrolyzed wheat protein produced in Comparative Example 2, There was no difference in the evaluation value of the cold-air dried hair, and there was almost no heat active effect. Moreover, in the hair rinse of Example Product 2, even when the heat treatment is performed, the evaluation value is almost the same as that in the case of cold air drying of Example Product 2. The production method of Example 2 is more suitable for the hair than the production method of Comparative Example 2. It was clear that silylated hydrolyzed wheat protein with high effect of imparting gloss, moisture and combing ability can be produced.

  In addition, the size of the knots indicating the evaluation result of the hair beam is the largest for the hair that has been heat-dried after using the hair rinse containing the silylated hydrolyzed wheat protein produced in Example 2, and the air-dried after using the same hair rinse. The hair rinse containing the silylated hydrolyzed wheat protein produced in Comparative Example 2 is 1.26 times larger than the hair dried by heating after use. The improvement of the imparting action was great. Compared to this, in Comparative product 2, there was no great difference between heat-treated hair and cold-air dried hair, and in the silylated hydrolyzed wheat protein of Comparative Example 2, no improvement in the action of applying a beam was observed.

Application example 3
A hair setting agent having the composition shown in Table 7 was prepared, and each hair setting agent was used for washed hair, and the gloss, moisture and tension of heat-treated hair and non-heat-treated hair were examined.

  In the test, five hair bundles were prepared, each of the two hair bundles was treated with the hair setting agent of Example 3 and Comparative product 3, one of the hair bundles was heated and dried with a hair dryer, and the other hair bundle was treated. Was dried with a hair dryer in cold air. Further, one hair bundle was treated with the hair setting agent of the control product 3, and this hair bundle was dried with a hair dryer in cold air.

  The treatment of the hair with the hair setting agent was performed as follows. That is, hair with a length of 20 cm is washed in advance with an aqueous solution of 2% polyoxyethylene (3) sodium lauryl ether sulfate, rinsed with water and air-dried at room temperature to produce five hair bundles composed of these 20 hairs. They were each wrapped around a rod. Two rods around which the hair was wound were used for Example 3 and Comparative Product 3, and the remaining one was used as a control product. 2 ml each of the hair setting agent of Example Product 3, Comparative Product 3 and Control Product 3 is applied to the hair bundle wound around these rods, and one rod of each of Example Product 3 and Comparative Product 3 is dried with hot air at 90 ° C. The remaining rods of Example 3 and Comparative Product 3 and the control rod were dried in a constant temperature bath at 36 ° C. Remove the hair after drying from the rod, and let 10 panelists (6 women, 4 men) evaluate the gloss and moisture of the hair according to the same evaluation criteria as in Application Example 1, and 14 hairs from each hair bundle They were extracted one by one and subjected to the same hair beam evaluation test as in Application Example 2 to compare the knot sizes. The results are shown in Table 8 as average values.

  As shown in Table 8, the hair heat-treated at 90 ° C. using the hair set containing silylated hydrolyzed keratin produced in Example 3 was dried at 36 ° C. using the same hair set. Compared to hair, both the gloss and moisture of the hair have high evaluation values, and it was clear that the effect of imparting gloss and moisture to the hair is enhanced by heat treatment. In addition, when the hair setting agent containing the silylated hydrolyzed keratin produced in Comparative Example 3 is used, the hair gloss and moisture of the heat-treated hair are improved compared to the hair dried at 36 ° C. .

  The size of the knot indicating the evaluation result of the hair beam is the largest for the hair heated using the hair setting agent containing the silylated hydrolyzed keratin produced in Example 3, and the same hair setting agent is used. It was 1.32 times that of the hair that was not heat-treated. On the other hand, when the hair setting agent containing the silylated hydrolyzed keratin produced in Comparative Example 3 was used, the heat-treated hair was 1.25 times that of the unheated hair, and the heat-treated hair The imparting effect was slightly inferior.

  From the above results, it can be said that the silylated hydrolyzed keratin produced in Comparative Example 3 also has a heat active effect, but the difference in effect due to heating is greater in Example 3 and this is the method of Example 3. In the production of the silylated hydrolyzed keratin, the introduction rate of the silyl functional group is considered to be higher than in the production of the method of Comparative Example 3.

Application example 4
Shampoos having the compositions shown in Table 9 were prepared, and the hair was washed with each shampoo, and then the hair gloss, moisture and combability when the hair was dried with hot air and when dried with cold air were evaluated.

  In the test, five hair bundles are prepared, and each of the two hair bundles is washed with the shampoos of the product 4 and the comparative product 4, one hair bundle is heated and dried with a hair dryer, and the other hair bundle is the hair. It dried with cold air with the dryer. Moreover, one hair bundle was processed with the shampoo of the control product 4, and this hair bundle was dried in cold air with a hair dryer.

  The treatment of the hair with the shampoo was performed as follows. That is, five hair bundles having a length of 15 cm and a weight of 1 g were prepared, two for each of the product 4 and the comparative product 4 and one for the control product. For each of these hair bundles, each hair bundle was washed with 0.5 g of each of the shampoos of Example Product 4, Comparative Product 4 and Control Product 4 and rinsed with hot water. Each one is heat-dried under the same conditions with the same hair dryer as the product 1 and the other hair bundle of the product 4 and the comparative product 4 and the hair bundle of the control product 4 are cooled with the same hair dryer. Dried. After repeating this shampoo washing and drying process 10 times, 10 panelists (6 women, 4 men) evaluated the gloss, moisture, and combing properties of hair according to the same evaluation criteria as in Application Example 1. . The results are shown in Table 10 as average values.

  As shown in Table 10, the hair dried by heating after washing with the shampoo containing the silylated hydrolyzed soy protein produced in Example 4 was glossy, moisturized and combed compared to the hair washed with the same shampoo and dried with cold air. It was clear that the evaluation value greatly increased in any evaluation item of street characteristics and the heat active effect was very high. On the other hand, the hair dried by heating after washing with the shampoo containing the silylated hydrolyzed soy protein produced in Comparative Example 4 also had a higher evaluation value than the hair dried by cold air, and the silyl produced in Comparative Example 4 Although it can be said that the hydrolyzed soy protein also has a heat active effect, the difference in the effect is smaller than that of the product of Example 4, which is the same as that of Comparative Example 4 in the production of the silylated hydrolyzed soy protein by the method of Example 4. This is probably because the introduction rate of the silyl functional group is higher than the production by this method.

It is a figure which shows the gel filtration chromatography of the silyl hydrolyzed collagen manufactured in Example 1, and the hydrolyzed collagen which is the raw material. It is a figure which shows the gel filtration chromatography of the silyl hydrolysis wheat protein manufactured in Example 2, and the hydrolysis wheat protein which is the raw material. It is a figure which shows the gel filtration chromatography of the silyl hydrolysis keratin manufactured in Example 3, and the hydrolysis keratin which is the raw material. It is a figure which shows the gel filtration chromatography of the silyl hydrolysis soybean protein manufactured in Example 4, and the hydrolysis soybean protein which is the raw material. It is a figure which shows the gel filtration chromatography of the silyl hydrolyzed collagen manufactured in the comparative example 1, and the hydrolyzed collagen which is the raw material. It is a figure which shows the gel filtration chromatography of the silyl hydrolysis wheat protein manufactured by the comparative example 2, and the hydrolysis wheat protein which is the raw material. It is a figure which shows the gel filtration chromatography of the silyl hydrolysis keratin manufactured in the comparative example 3, and the hydrolysis keratin which is the raw material. It is a figure which shows the gel filtration chromatography of the silyl hydrolysis soybean protein manufactured by the comparative example 4, and the hydrolysis soybean protein which is the raw material. It is a figure which shows typically the knot (knot) of the hair at the time of evaluating the beam of hair.

Claims (5)

The following general formula (1)

(In formula, R < ¹ >, R < ² >, R < ³ > may be same or different, and is a C1-C3 alkoxy group or a C1-C3 alkyl group, but R < ¹ >, R < ² >, R < ³ >. Of which at least two are alkoxy groups having 1 to 3 carbon atoms)
Obtained by hydrolyzing in a water solution containing a lower monohydric alcohol having 1 to 3 carbon atoms and then reacting with an amino group containing an amino group in the side chain of the hydrolyzed peptide. A cosmetic base material comprising the resulting silylated hydrolyzed peptide.   A cosmetic base material comprising the silylated hydrolyzed peptide according to claim 1, wherein the hydrolyzed peptide has a number average molecular weight of 200 to 3,000. The following general formula (1)

(In formula, R < ¹ >, R < ² >, R < ³ > may be same or different, and is a C1-C3 alkoxy group or a C1-C3 alkyl group, but R < ¹ >, R < ² >, R < ³ >. Of which at least two are alkoxy groups having 1 to 3 carbon atoms)
Is hydrolyzed in an aqueous solution containing a lower monohydric alcohol having 1 to 3 carbon atoms, and then reacted with an amino group containing an amino group in the side chain of the hydrolyzed peptide. A method for producing a cosmetic substrate comprising a silylated hydrolyzed peptide.   The silylated hydrolysis according to claim 3, wherein the content of the alcohol in the aqueous solution containing the lower monohydric alcohol having 1 to 3 carbon atoms used when hydrolyzing the silane coupling agent is 2 to 20% by mass. A method for producing a cosmetic base material comprising a peptide. The method for producing a cosmetic base material comprising the silylated hydrolyzed peptide according to claim 3 or 4, wherein the hydrolyzed peptide has a number average molecular weight of 200 to 3,000.

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