JP2020132563A - Cosmetic - Google Patents
Cosmetic Download PDFInfo
- Publication number
- JP2020132563A JP2020132563A JP2019027223A JP2019027223A JP2020132563A JP 2020132563 A JP2020132563 A JP 2020132563A JP 2019027223 A JP2019027223 A JP 2019027223A JP 2019027223 A JP2019027223 A JP 2019027223A JP 2020132563 A JP2020132563 A JP 2020132563A
- Authority
- JP
- Japan
- Prior art keywords
- hair
- protein
- cosmetic
- cosmetics
- keratin
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 239000002537 cosmetic Substances 0.000 title claims abstract description 65
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 68
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 68
- XWRZKLKALVJDDS-REOHCLBHSA-N (2r)-2-(diaminomethylideneamino)-3-sulfanylpropanoic acid Chemical compound NC(N)=N[C@@H](CS)C(O)=O XWRZKLKALVJDDS-REOHCLBHSA-N 0.000 claims abstract description 16
- 150000001413 amino acids Chemical class 0.000 claims abstract description 10
- 125000002887 hydroxy group Chemical group [H]O* 0.000 claims abstract description 5
- 210000004209 hair Anatomy 0.000 claims description 96
- 102000011782 Keratins Human genes 0.000 claims description 25
- 108010076876 Keratins Proteins 0.000 claims description 25
- 239000003795 chemical substances by application Substances 0.000 claims description 21
- 238000011282 treatment Methods 0.000 claims description 10
- 239000002453 shampoo Substances 0.000 claims description 9
- 239000003086 colorant Substances 0.000 claims description 3
- 230000037308 hair color Effects 0.000 claims description 3
- 235000018102 proteins Nutrition 0.000 abstract description 65
- 235000001014 amino acid Nutrition 0.000 abstract description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 20
- 210000003491 skin Anatomy 0.000 description 17
- 238000011156 evaluation Methods 0.000 description 15
- 239000000203 mixture Substances 0.000 description 14
- 238000009472 formulation Methods 0.000 description 9
- 239000012488 sample solution Substances 0.000 description 8
- 238000000034 method Methods 0.000 description 7
- 230000003700 hair damage Effects 0.000 description 6
- 230000006870 function Effects 0.000 description 5
- 230000008439 repair process Effects 0.000 description 5
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 4
- 239000007844 bleaching agent Substances 0.000 description 4
- 239000003638 chemical reducing agent Substances 0.000 description 4
- 235000018417 cysteine Nutrition 0.000 description 4
- 230000006378 damage Effects 0.000 description 4
- 230000007062 hydrolysis Effects 0.000 description 4
- 238000006460 hydrolysis reaction Methods 0.000 description 4
- 239000006210 lotion Substances 0.000 description 4
- 239000003921 oil Substances 0.000 description 4
- 102000008186 Collagen Human genes 0.000 description 3
- 108010035532 Collagen Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 125000002091 cationic group Chemical group 0.000 description 3
- 229920001436 collagen Polymers 0.000 description 3
- 238000005520 cutting process Methods 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 229960003067 cystine Drugs 0.000 description 3
- 210000003746 feather Anatomy 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 125000003396 thiol group Chemical group [H]S* 0.000 description 3
- PMNLUUOXGOOLSP-UHFFFAOYSA-N 2-mercaptopropanoic acid Chemical compound CC(S)C(O)=O PMNLUUOXGOOLSP-UHFFFAOYSA-N 0.000 description 2
- 241000255789 Bombyx mori Species 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- 108010073771 Soybean Proteins Proteins 0.000 description 2
- 150000001298 alcohols Chemical class 0.000 description 2
- 125000000129 anionic group Chemical group 0.000 description 2
- GEHJBWKLJVFKPS-UHFFFAOYSA-N bromochloroacetic acid Chemical compound OC(=O)C(Cl)Br GEHJBWKLJVFKPS-UHFFFAOYSA-N 0.000 description 2
- 125000003739 carbamimidoyl group Chemical group C(N)(=N)* 0.000 description 2
- XVOYSCVBGLVSOL-UHFFFAOYSA-N cysteic acid Chemical compound OC(=O)C(N)CS(O)(=O)=O XVOYSCVBGLVSOL-UHFFFAOYSA-N 0.000 description 2
- 150000001945 cysteines Chemical class 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 239000006260 foam Substances 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 230000003719 hair strength Effects 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 239000000741 silica gel Substances 0.000 description 2
- 229910002027 silica gel Inorganic materials 0.000 description 2
- 235000019710 soybean protein Nutrition 0.000 description 2
- CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 2
- -1 thiol compound Chemical class 0.000 description 2
- UMGDCJDMYOKAJW-UHFFFAOYSA-N thiourea Chemical compound NC(N)=S UMGDCJDMYOKAJW-UHFFFAOYSA-N 0.000 description 2
- 239000001993 wax Substances 0.000 description 2
- 210000002268 wool Anatomy 0.000 description 2
- 241000251468 Actinopterygii Species 0.000 description 1
- 239000004215 Carbon black (E152) Substances 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 239000004909 Moisturizer Substances 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-N Sulfurous acid Chemical compound OS(O)=O LSNNMFCWUKXFEE-UHFFFAOYSA-N 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Natural products NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 239000006096 absorbing agent Substances 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000004061 bleaching Methods 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000012459 cleaning agent Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- UFULAYFCSOUIOV-UHFFFAOYSA-N cysteamine Chemical compound NCCS UFULAYFCSOUIOV-UHFFFAOYSA-N 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000002951 depilatory effect Effects 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 239000010696 ester oil Substances 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 230000003779 hair growth Effects 0.000 description 1
- 230000013632 homeostatic process Effects 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 150000002430 hydrocarbons Chemical class 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 229960003151 mercaptamine Drugs 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 239000003595 mist Substances 0.000 description 1
- 230000001333 moisturizer Effects 0.000 description 1
- 230000003020 moisturizing effect Effects 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 239000003223 protective agent Substances 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 229920002545 silicone oil Polymers 0.000 description 1
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000005846 sugar alcohols Polymers 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000003813 thin hair Effects 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Cosmetics (AREA)
Abstract
Description
本発明は化粧料に関し、更に詳しくは、適用部位への付着性に優れ、適用部位の機能・特性を改善・保護又は補修することができる化粧料に関する。 The present invention relates to a cosmetic, and more particularly to a cosmetic having excellent adhesion to an application site and capable of improving, protecting or repairing the function and characteristics of the application site.
化粧料は、単に外観を美しく整えるだけでなく、適用部位を保護するため、あるいは適用部位における機能・特性を改善又は補修するために用いられることがある。このような化粧料に含まれる成分の一つとして、タンパク質が従来から知られている。タンパク質は髪や皮膚になじみやすく、皮膚及び毛髪の保湿、感触改良、並びに肌荒れ防止に有効であることが知られている。 Cosmetics may be used not only to make the appearance beautiful, but also to protect the application site or to improve or repair the function / characteristics of the application site. Protein has been conventionally known as one of the components contained in such cosmetics. Proteins are well-adapted to hair and skin, and are known to be effective in moisturizing and improving the feel of hair and preventing rough skin.
例えば、毛髪及び皮膚を構成するタンパク質として知られているケラチンは、皮膚及び毛髪の構造を維持するために重要である。ケラチンは細く長い髪に強度、ハリ・コシ、及びしなやかさを与える。また、ケラチンは、乾燥及び様々な刺激から身体を守る皮膚にバリア機能を与える。コラーゲンは水分保持力が高く、髪及び皮膚の潤いを与え、それを維持することで生体機能及び代謝等の恒常性を与える。シルクタンパク質は、疎水性と親水性のアミノをバランスよく含み、髪及び皮膚の表面を被覆して滑り性を改善することにより、髪に指通りの良い質感、皮膚になめらかな質感を与えることが知られている。 For example, keratin, known as a protein that constitutes hair and skin, is important for maintaining the structure of skin and hair. Keratin gives long, thin hair strength, firmness, and suppleness. Keratin also provides a barrier function to the skin that protects the body from dryness and various stimuli. Collagen has a high water-retaining power, moisturizes hair and skin, and by maintaining it, gives homeostasis such as biological function and metabolism. Silk protein contains hydrophobic and hydrophilic amino acids in a well-balanced manner, and by covering the surface of hair and skin to improve slipperiness, it can give hair a smooth texture and a smooth texture. Are known.
タンパク質は、その由来及び構成するアミノ酸の組成によって様々な物性を示す。ケラチン及びシルクのように、水に不溶なタンパク質も多くある。化粧品で用いられるタンパク質の中でも特に、ケラチンを水に溶解させることは難しい。この原因として、ケラチンを構成するアミノ酸組成にはシステインが多く、このシステインが分子間及び分子内でジスルフィド結合による架橋を形成していることが挙げられる。 Proteins exhibit various physical properties depending on their origin and the composition of the constituent amino acids. Many proteins, such as keratin and silk, are insoluble in water. Among the proteins used in cosmetics, it is difficult to dissolve keratin in water. The reason for this is that the amino acid composition constituting keratin contains a large amount of cysteine, and this cysteine forms a crosslink by a disulfide bond between and within the molecule.
従来、ケラチン等の水に不溶なタンパク質を化粧料に用いる場合には、加水分解又はタンパク質を変性させることにより、水へ可溶化させている。ケラチンのようにジスルフィド結合を多くもつタンパク質は通常、ジスルフィド結合を還元してチオール基(−SH)又はその誘導基とすることにより、ジスルフィド結合を開裂して可溶化することが行われている。例えば、特許文献1には、−SS−(CH2)nCOO−を側鎖基として備えるペプチドが配合されたヘアケア剤が記載されている。特許文献2には、水に不溶なタンパク質のジスルフィド結合をチオール基に還元し、その一部又は全部をカルボキシメチルジルスフィド基(−SSCH2COOH)とすることにより得られる可溶化タンパク質が記載されている。 Conventionally, when a protein insoluble in water such as keratin is used in cosmetics, it is solubilized in water by hydrolysis or denaturing the protein. A protein having many disulfide bonds, such as keratin, is usually solubilized by cleaving the disulfide bond by reducing the disulfide bond to a thiol group (-SH) or an inducing group thereof. For example, Patent Document 1, -SS- (CH 2) n COO - is described a hair care agent peptide is formulated with a side chain group. Patent Document 2 describes a solubilized protein obtained by reducing a disulfide bond of a protein insoluble in water to a thiol group and converting a part or all of the disulfide bond into a carboxymethylzyl spheride group (-SSCH 2 COOH). ing.
しかし、化粧料の成分は、適用部位(例えば、皮膚及び毛髪)における付着性に優れることが求められる。一方、特許文献2記載の可溶化タンパク質では、−COOHを側鎖に有する。このような可溶化タンパク質は、水溶性が向上する反面、毛髪には付着しにくいという問題がある。 However, the components of the cosmetic are required to have excellent adhesion at the application site (for example, skin and hair). On the other hand, the solubilized protein described in Patent Document 2 has -COOH in the side chain. Such a solubilized protein has a problem that it is difficult to adhere to hair while improving water solubility.
タンパク質の水溶性を向上させる方法の一つとして、加水分解によりタンパク質を低分子量化する方法も利用されている。しかし、この方法により得られた低分子量のタンパク質は、髪及び皮膚の被覆性が弱く、洗浄等で容易に洗い流されてしまう問題がある。 As one of the methods for improving the water solubility of a protein, a method for reducing the molecular weight of the protein by hydrolysis is also used. However, the low molecular weight protein obtained by this method has a problem that it has a weak covering property on hair and skin and is easily washed away by washing or the like.
本発明は、適用部位への付着性に優れ、適用部位の機能・特性を改善・保護又は補修することができる化粧料を提供することを目的とする。 An object of the present invention is to provide a cosmetic that has excellent adhesion to an application site and can improve, protect or repair the function and characteristics of the application site.
本発明の化粧料(以下、「本化粧料」という。)は、タンパク質を構成するアミノ酸のNH2基、OH基、及びSH基の一部又は全部に、アミジノシステインを付加させたタンパク質(以下、「付加タンパク質」という。)を含有する。 The cosmetic of the present invention (hereinafter, referred to as "the cosmetic".) Is, NH 2 groups of amino acids constituting proteins, some or all of OH groups and SH groups, a protein obtained by adding amidino cysteine (hereinafter , "Additional protein").
本発明の化粧料は付加タンパク質を含み、皮膚及び毛髪等の適用部位への付着性に優れていることから、適用部位の保護若しくは補修又は適用部位における機能若しくは特性を改善することができる。 Since the cosmetic of the present invention contains an addition protein and has excellent adhesion to the application site such as skin and hair, it is possible to protect or repair the application site or improve the function or property at the application site.
前記タンパク質の種類、由来及び構造に特に限定はない。化粧料へ配合するために、前記タンパク質として、水に可溶又は可溶化させたタンパク質が好ましい。前記タンパク質として具体的には、例えば、ケラチン、コラーゲン、シルクタンパク質、及び大豆タンパク質が挙げられる。 The type, origin and structure of the protein are not particularly limited. As the protein, a protein solubilized or solubilized in water is preferable for blending into cosmetics. Specific examples of the protein include keratin, collagen, silk protein, and soybean protein.
前記タンパク質として、精製・単離された該タンパク質を用いてもよく、あるいは該タンパク質を含む天然成分を用いてもよい。該天然成分として、例えば、ケラチンを含むヒト及び鳥獣の毛(人毛、羊毛、羽毛)、角、及び爪、コラーゲンを含む動物や魚類の鱗、皮、骨及び軟骨、シルクタンパク質を含む蚕の繭、並びに大豆タンパク質を含むダイズの種子が挙げられる。ヒト及び鳥獣の毛は、加水分解又はタンパク質変性により水に可溶化させた場合でも、タンパク質を構成するアミノ酸のうち疎水性アミノ酸の割合が多い。そのため、ヒト及び鳥獣の毛由来のケラチンは、他のタンパク質より髪や皮膚への付着性に優れるので好ましく、羊毛又は鳥の羽毛若しくは羽由来のケラチンがより好ましい。 As the protein, the purified / isolated protein may be used, or a natural component containing the protein may be used. The natural ingredients include, for example, keratin-containing human and bird-beast hair (human hair, wool, feathers), horns and nails, collagen-containing animal and fish scales, skin, bones and cartilage, silkworm-containing silkworms. Examples include cocoons, as well as soybean seeds containing soybean protein. Even when human and bird and animal hair is solubilized in water by hydrolysis or protein denaturation, the proportion of hydrophobic amino acids among the amino acids constituting the protein is large. Therefore, human and bird / animal hair-derived keratins are preferable because they have better adhesion to hair and skin than other proteins, and wool or bird feathers or feather-derived keratins are more preferable.
アミジノシステインの構造を式(1)に示す。アミジノシステインは通常、多くの化粧料のpH領域においてカチオン化される強い塩基性のアミジノ基と、幅広いpH領域で水溶性となる電解質に寄与するカルボキシル基と、を有する。 The structure of amidinocysteine is shown in the formula (1). Amidinocysteine usually has a strongly basic amidino group that is cationized in the pH range of many cosmetics and a carboxyl group that contributes to an electrolyte that becomes water soluble in a wide pH range.
前記付加タンパク質では、前記タンパク質を構成するアミノ酸のNH2基、OH基、及びSH基の一部又は全部に、アミジノシステインが付加されている。前記付加タンパク質は、強いカチオン化能を有するアミジノ基を分子内にもつアミジノシステインが付加することにより、水溶性とカチオン性が高く、皮膚及び毛髪等への付着性に優れる。前記付加の程度には特に限定はない。アミジノシステインは、前記タンパク質分子内に1分子、あるいは2分子以上付加されていてもよい。 The said additional proteins, NH 2 group of an amino acid constituting the protein, a part or all of OH groups and SH groups, amidino cysteine is added. The added protein is highly water-soluble and cationic due to the addition of amidinocysteine having an amidino group having a strong cationizing ability in the molecule, and is excellent in adhesion to skin, hair and the like. The degree of the addition is not particularly limited. One molecule or two or more amidinocysteines may be added to the protein molecule.
前記タンパク質へのアミジノシステインの付加の具体的態様及び方法には特に限定はない。アミジノシステインは通常、前記タンパク質中のNH2基、OH基、及びSH基と反応し、アミド結合、エステル結合、及びチオエステル結合を形成することにより、前記タンパク質に付加される。また、前記タンパク質のSH基とアミジノシステインのSH基とのジスルフィド結合を形成することにより、アミジノシステインを前記タンパク質に付加してもよい。前記ジスルフィド結合の形成は、前記タンパク質中のシスチン結合(分子間又は分子内のシステイン同士のジスルフィド結合)を還元した後に生成するSH基とアミジノシステインとを反応させることにより行ってもよい。 The specific mode and method of addition of amidinocysteine to the protein are not particularly limited. Amidino cysteine normally, NH 2 groups of the protein, reacts with the OH group and SH group, an amide bond, an ester bond, and by forming a thioester bond, is added to the protein. Further, amidinocysteine may be added to the protein by forming a disulfide bond between the SH group of the protein and the SH group of amidinocysteine. The formation of the disulfide bond may be carried out by reacting the SH group generated after reducing the cystine bond (disulfide bond between intermolecular or intramolecular cysteines) in the protein with amidinocysteine.
前記タンパク質中のシスチン結合の還元には通常、還元剤が用いられる。該還元剤は、シスチン結合を還元することができる限り、その種類に特に限定はない。該還元剤として、公知の還元剤、例えば、チオグリコール酸、システイン、システアミン、メルカプトエタノール、チオ乳酸、チオ尿素若しくはその塩等のチオール化合物、又は亜硫酸、ピロ亜硫酸若しくはその塩等を用いることができる。 A reducing agent is usually used to reduce the cystine bond in the protein. The type of the reducing agent is not particularly limited as long as it can reduce the cystine bond. As the reducing agent, known reducing agents such as thioglycolic acid, cysteine, cysteamine, mercaptoethanol, thiolactic acid, thiourea or a thiol compound such as a salt thereof, or sulfite, pyrosulfite or a salt thereof and the like can be used. ..
アミジノシステインの量その他反応条件によっては、前記タンパク質中のジスルフィド結合の一部が、アミジノシステインのチオール基により直接変換され、ジスルフィド結合の一方に付加する場合がある(式(2)参照)。前記「付加」には、このような付加も含まれる。下記式(2)中、「Cys」は、前記タンパク質に含まれるシステイン残基を、「R−SH」はアミジノシステインを意味する。 Depending on the amount of amidinocysteine and other reaction conditions, a part of the disulfide bond in the protein may be directly converted by the thiol group of amidinocysteine and added to one of the disulfide bonds (see formula (2)). The "addition" also includes such an addition. In the following formula (2), "Cys" means a cysteine residue contained in the protein, and "R-SH" means amidinocysteine.
Cys−S−S−Cys + R−SH
→ Cys−S−S−R + Cys−SH (2)
Cys-SS-Cys + R-SH
→ Cys-S-S-R + Cys-SH (2)
前記タンパク質及び前記付加タンパク質は、必要に応じて他の処理を行ってもよい。例えば、分子量及び分子サイズを低下させるために、前記タンパク質及び/又は前記付加タンパク質について、酵素、酸、又はアルカリにより加水分解を行ってもよい。また、前記タンパク質として、水可溶性を高めるために、従来公知の加水分解及びタンパク質変性等による可溶化を行ってもよい。更に、前記付加タンパク質を得た後、精製、ろ過、遠心分離等を行うことにより、他の成分又は不溶分を除去してもよい。 The protein and the addition protein may be subjected to other treatments as necessary. For example, the protein and / or the addition protein may be hydrolyzed with an enzyme, acid, or alkali in order to reduce the molecular weight and size. Further, the protein may be solubilized by conventionally known hydrolysis, protein denaturation or the like in order to increase the solubility in water. Further, after obtaining the added protein, other components or insoluble components may be removed by performing purification, filtration, centrifugation or the like.
本化粧料中、前記付加タンパク質の含有量は、有効量である限り特に限定はない。前記付加タンパク質の含有量は、通常、0.01〜10質量%である。 The content of the addition protein in the present cosmetic is not particularly limited as long as it is an effective amount. The content of the added protein is usually 0.01 to 10% by mass.
本化粧料は、本発明の作用効果を阻害しない限り、必要に応じて、前記付加タンパク質以外の他の成分を含んでいてもよい。該他の成分として、従来から化粧料に添加含有されている公知成分、あるいは他の機能性成分が挙げられる。該他の成分として具体的には、例えば、油脂、炭化水素油、高級脂肪酸、高級アルコール、エステル油、シリコーン油、アニオン界面活性剤(アニオン系、カチオン系、両性、非イオン系)、保湿剤、水溶性高分子、皮膜剤、紫外線吸収剤、金属イオン封鎖剤、低級アルコール、多価アルコール、糖類、アミノ酸、pH調整剤、ビタミン、酸化防止剤、色素、防腐剤、及び香料が挙げられる。 The present cosmetic may contain components other than the addition protein, if necessary, as long as the effects of the present invention are not impaired. Examples of the other component include known components that have been conventionally added and contained in cosmetics, or other functional components. Specifically, as the other components, for example, fats and oils, hydrocarbon oils, higher fatty acids, higher alcohols, ester oils, silicone oils, anionic surfactants (anionic, cationic, amphoteric, nonionic), moisturizers. , Water-soluble polymers, film agents, UV absorbers, metal ion blockers, lower alcohols, polyhydric alcohols, sugars, amino acids, pH adjusters, vitamins, antioxidants, pigments, preservatives, and fragrances.
本化粧料の剤形及び使用形態には特に限定はない。本化粧料は、例えば、ローション、エマルション、ゲル、軟膏・ワックス、フォーム状、固体・粉末、又は霧状で使用することができる。 The dosage form and usage form of this cosmetic are not particularly limited. This cosmetic can be used, for example, in lotion, emulsion, gel, ointment / wax, foam, solid / powder, or mist.
本化粧料の適用箇所には特に限定はない。本化粧料は、例えば、皮膚又は毛髪に適用することができる。本化粧料は、皮膚又は毛髪を改善、保護、又は補修するために使用することができる。 There are no particular restrictions on where this cosmetic is applied. This cosmetic can be applied to, for example, skin or hair. This cosmetic may be used to improve, protect or repair the skin or hair.
本化粧料の具体的用途には特に限定はない。本化粧料の用途として具体的には、例えば、化粧水・乳液・クリーム・オイル等の基礎化粧品、皮膚洗浄料、マッサージ用剤、除毛・脱毛剤及びその前後処理剤、ファンデーション・口紅・アイシャドウ・アイライナー・マスカラ等のメークアップ化粧料、フェイスマスク、テープ剤、シート剤、爪用補修剤・保護剤、育毛・養毛剤、並びに毛髪処理剤が挙げられる。 The specific use of this cosmetic is not particularly limited. Specifically, the uses of this cosmetic are, for example, basic cosmetics such as lotion, milky lotion, cream, oil, skin cleaning agent, massage agent, hair remover / depilatory and pre- and post-treatment agent, foundation / lipstick / eye. Examples include make-up cosmetics such as shadows, eyeliners, and mascaras, face masks, tapes, sheets, nail repair / protective agents, hair growth / hair restorers, and hair treatment agents.
毛髪はダメージを受けると、毛髪内のシステインがシステイン酸に変換されてマイナスの電荷が増えることにより、アニオン性が強くなる。その結果、カチオン性が強い前記付加タンパク質は、より毛髪に強く付着することができる。その結果、前記付加タンパク質を含有する毛髪処理剤は、ダメージを受けた毛髪の機能・特性を改善・保護又は補修に優れる。よって、本化粧料は、毛髪処理剤、例えば、シャンプー、リンス、トリートメント、コンディショナー、整髪剤、パーマネントウェーブ剤、カーリング剤、ヘアーカラー剤、又はこれらの剤を使用する前若しくは後処理剤として好適に使用することができる。また、本化粧料は、ヒト用だけでなく、ヒト以外の動物用化粧雑貨、ヒト以外の動物用医薬部外品、皮膚外用剤、及び毛髪処理剤等にも使用することができる。 When the hair is damaged, the cysteine in the hair is converted to cysteic acid and the negative charge increases, so that the anionic property becomes stronger. As a result, the highly cationic addition protein can adhere more strongly to the hair. As a result, the hair treatment agent containing the additional protein is excellent in improving, protecting or repairing the function and characteristics of damaged hair. Therefore, this cosmetic is suitable as a hair treatment agent, for example, shampoo, conditioner, treatment, conditioner, hair styling agent, permanent wave agent, curling agent, hair coloring agent, or before or after using these agents. Can be used. In addition, this cosmetic can be used not only for humans but also for non-human animal cosmetics, non-human quasi-drugs, skin external preparations, hair treatment agents and the like.
以下、実施例により本発明を具体的に説明する。尚、本発明は、実施例に示す形態に限定されない。本発明の実施形態は、目的及び用途等に応じて、本発明の範囲内で種々変更することができる。 Hereinafter, the present invention will be specifically described with reference to Examples. The present invention is not limited to the embodiments shown in the examples. The embodiments of the present invention can be variously modified within the scope of the present invention according to the purpose, use and the like.
処方例1〜20の化粧料の具体的組成を以下に示す。 The specific composition of the cosmetics of Formulation Examples 1 to 20 is shown below.
(処方例1)シャンプー
(処方例2)シャンプー
(処方例3)シャンプー
(処方例4)リンス
(処方例5)リンス
(処方例6)リンス
(処方例7)トリーメント
(処方例8)ヘアコンディショナー
(処方例9)ヘアオイル
(処方例10)ヘアセットローション
(処方例11)ヘアスタイリングジェル
(処方例12)ヘアスタイリングスプレー
(処方例13)ヘアフォーム
(処方例14)毛髪処理剤(前処理・後処理共用)
(処方例15)ヘアワックス
(処方例16)ヘアカラー剤
(処方例17)ヘアマニキュア
(処方例18)パーマネントウェーブ剤
(処方例19)縮毛矯正剤
(処方例20)カーリング剤
実施例1;毛髪強度改善試験
ブリーチ剤1剤(ホーユー株式会社製「レセ パウダーブリーチ EX」)及びブリーチ2剤(株式会社ミルボン社製「オルディーブ アディクシー オキシダン 6%」)を1:2:5(質量比)の比率で均一に混合してブリーチ混合液を得た。毛束(株式会社スタッフス社製「テスト用毛束1g10cm、人毛、黒」)に対し、ブリーチ混合液を均等に塗布し、25℃で30分放置後、しっかり水洗した。このブリーチ処理を2回行った。その毛束を1.0質量%ラウリル硫酸ナトリウム溶液中に25℃5分間浸漬した。次いでその毛束を水洗し、評価用毛束とした。
Example 1; Hair strength improvement test 1 bleaching agent (“Rece Powder Bleach EX” manufactured by Hoyu Co., Ltd.) and 2 bleaching agents (“Oldive Adixie Oxydan 6%” manufactured by Milbon Co., Ltd.) 1: 2: 5 ( A bleach mixture was obtained by uniformly mixing at a ratio of (mass ratio). The bleach mixture was evenly applied to the hair bundle (“test hair bundle 1 g 10 cm, human hair, black” manufactured by Staffs Co., Ltd.), left at 25 ° C. for 30 minutes, and then thoroughly washed with water. This bleaching process was performed twice. The hair bundle was immersed in a 1.0 mass% sodium lauryl sulfate solution at 25 ° C. for 5 minutes. Next, the hair bundle was washed with water to obtain a hair bundle for evaluation.
サンプル溶液として、以下の化粧料(A)〜(C)を用いた。
(A)処方例10のS−アミジノシステイニルケラチンの代わりに水を添加したもの。
(B)処方例10のS−アミジノシステイニルケラチンの代わりに、カチオン化ケラチンとして一丸ファルコス株式会社製「プロティキュート Cアルファ」を添加したもの。
(C)処方例10
The following cosmetics (A) to (C) were used as sample solutions.
(A) Water added instead of S-amidinocisteinyl keratin of Formulation Example 10.
(B) Instead of S-amidinocisteinyl keratin of Formulation Example 10, "Proticute C Alpha" manufactured by Ichimaru Falcos Co., Ltd. was added as cationized keratin.
(C) Prescription example 10
サンプル溶液に評価用毛束を5分間浸漬後、水洗し温風乾燥した。処理した毛束に対して、万能引張試験機(株式会社島津製作所製「AG−20k NXDplus」)を用いて、50mm/minの速度で毛髪1本当りの引張切断強度(N)及び伸長率(%)を測定した(n=10)。 The evaluation hair bundle was immersed in the sample solution for 5 minutes, washed with water, and dried with warm air. Tensile cutting strength (N) and elongation rate (N) per hair at a speed of 50 mm / min using a universal tensile tester (“AG-20k NXDplus” manufactured by Shimadzu Corporation) for the treated hair bundles. %) Was measured (n = 10).
毛髪強度改善試験の結果は以下の通りである。この結果を指標として、毛髪損傷を評価した。
化粧料(A):引張強度0.65(N)及び伸長率37.1(%)
化粧料(B):引張強度0.82(N)及び伸長率39.6(%)
化粧料(C):引張強度1.13(N)及び伸長率44.9(%)
The results of the hair strength improvement test are as follows. Hair damage was evaluated using this result as an index.
Cosmetics (A): Tensile strength 0.65 (N) and elongation 37.1 (%)
Cosmetics (B): Tensile strength 0.82 (N) and elongation 39.6 (%)
Cosmetics (C): Tensile strength 1.13 (N) and elongation 44.9 (%)
実施例2;毛髪付着性試験
評価用毛髪及びサンプル溶液として、実施例1の評価用毛束並びに化粧料(A)〜(C)及び(D)処方例10のS−アミジノシステイニルケラチンの代わりに東邦化学工業株式会社製「カチナールHC−200」(カチオン化度1.3meq/g)を用いた。
Example 2; Hair adhesion test As an evaluation hair and a sample solution, the evaluation hair bundle of Example 1 and the cosmetics (A) to (C) and (D) S-amidinosistinyl keratin of Formulation Example 10 Instead, "Katinal HC-200" (cationization degree 1.3 meq / g) manufactured by Toho Chemical Industry Co., Ltd. was used.
評価用毛束を20日間シリカゲルデシケーター中にて真空乾燥させ、各毛髪の質量を測定した。次いで、評価用毛束をサンプル溶液に30分間浸漬後、水洗し温風乾燥した。その後、評価用毛束を20日間シリカゲルデシケーター中にて真空乾燥させ、各毛髪の質量を測定した。毛髪付着率(%)は以下の式に基づいて算出した。
毛髪付着率(%)=(H2−H1)/H1×100
H1:試験前の毛髪の質量(g)
H2:試験後の毛髪の質量(g)
The evaluation hair bundle was vacuum dried in a silica gel desiccator for 20 days, and the mass of each hair was measured. Then, the evaluation hair bundle was immersed in the sample solution for 30 minutes, washed with water, and dried with warm air. Then, the evaluation hair bundle was vacuum dried in a silica gel desiccator for 20 days, and the mass of each hair was measured. The hair adhesion rate (%) was calculated based on the following formula.
Hair adhesion rate (%) = (H2-H1) / H1 × 100
H1: Hair mass (g) before the test
H2: Hair mass (g) after the test
毛髪付着性試験の結果は以下の通りである。この結果を指標として、毛髪損傷を評価した。
化粧料(A):毛髪付着率0.11(%)
化粧料(B):毛髪付着率0.84(%)
化粧料(C):毛髪付着率2.51(%)
化粧料(D):毛髪付着率1.04(%)
The results of the hair adhesion test are as follows. Hair damage was evaluated using this result as an index.
Cosmetic (A): Hair adhesion rate 0.11 (%)
Cosmetics (B): Hair adhesion rate 0.84 (%)
Cosmetics (C): Hair adhesion rate 2.51 (%)
Cosmetic (D): Hair adhesion rate 1.04 (%)
実施例3:毛髪摩擦ダメージの軽減試験
評価用毛髪として、株式会社スタッフス社製「テスト用毛束1g10cm、人毛、黒」の評価用毛束を用い、サンプル溶液として、以下の化粧料(A)〜(C)を用いた。
(A)処方例6のN−アミジノシステイニルケラチンの代わりに水を添加したもの。
(B)処方例6のN−アミジノシステイニルケラチンの代わりに、一丸ファルコス株式会社製「プロティキュートCアルファ」を添加したもの。
(C)処方例6
Example 3: Reduction test of hair friction damage Using the evaluation hair bundle of "Test hair bundle 1 g 10 cm, human hair, black" manufactured by Staffs Co., Ltd. as the evaluation hair, the following cosmetics (as a sample solution) A) to (C) were used.
(A) Water added in place of N-amidinocisteinyl keratin of Formulation Example 6.
(B) "Proticute C Alpha" manufactured by Ichimaru Falcos Co., Ltd. was added instead of N-amidinocisteinyl keratin of Formulation Example 6.
(C) Prescription example 6
評価用毛束にサンプル溶液を1g塗布後、水洗し温風乾燥した。乾燥後の毛髪に対して10回ブラッシングを行った。この工程を1回とし、50回繰り返した。その後、実施例1と同様の方法により、処理した評価用毛束の毛髪1本当りの引張切断強度(N)及び伸長率(%)を測定した(n=10)。 After applying 1 g of the sample solution to the evaluation hair bundle, it was washed with water and dried with warm air. The dried hair was brushed 10 times. This step was set to 1 time and repeated 50 times. Then, the tensile cutting strength (N) and the elongation rate (%) per hair of the treated evaluation hair bundle were measured by the same method as in Example 1 (n = 10).
毛髪摩擦ダメージの軽減試験の結果は以下の通りである。この結果を指標として、毛髪損傷を評価した。
化粧料(A):引張強度0.77(N)及び伸長率38.2(%)
化粧料(B):引張強度0.98(N)及び伸長率42.3(%)
化粧料(C):引張強度1.19(N)及び伸長率45.1(%)
The results of the hair friction damage reduction test are as follows. Hair damage was evaluated using this result as an index.
Cosmetics (A): Tensile strength 0.77 (N) and elongation 38.2 (%)
Cosmetics (B): Tensile strength 0.98 (N) and elongation 42.3 (%)
Cosmetics (C): Tensile strength 1.19 (N) and elongation 45.1 (%)
実施例4:シャンプーによる損傷に対する毛髪保護試験
評価用毛髪として、株式会社スタッフス社製「テスト用毛束1g10cm、人毛、黒」の評価用毛束を用い、サンプル溶液として、以下の化粧料(A)〜(D)を用いた。
(A)処方例2のN−アミジノシステイニルケラチンの代わりに水を添加したもの。
(B)処方例2のN−アミジノシステイニルケラチンの代わりに一丸ファルコス株式会社製「プロティキュート Cアルファ」を添加したもの。
(C)処方例2
(D)処方例2のN−アミジノシステイニルケラチンの代わりに、東邦化学工業株式会社製「カチナールHC−200」(カチオン化度1.3meq/g)を添加したもの。
Example 4: Hair protection test against damage caused by shampoo As the evaluation hair, the evaluation hair bundle of "Test hair bundle 1 g 10 cm, human hair, black" manufactured by Staffs Co., Ltd. was used, and the following cosmetics were used as a sample solution. (A) to (D) were used.
(A) Water added instead of N-amidinocisteinyl keratin of Formulation Example 2.
(B) "Proticute C Alpha" manufactured by Ichimaru Falcos Co., Ltd. was added instead of N-amidinocisteinyl keratin of Formulation Example 2.
(C) Prescription example 2
(D) In place of N-amidinocisteinyl keratin of Formulation Example 2, "Catinal HC-200" (cationization degree 1.3 meq / g) manufactured by Toho Chemical Industry Co., Ltd. was added.
評価用毛束にシャンプー剤である各サンプル溶液を1g塗布後、十分に泡立てた後、温水にて毛髪を濯ぎ、次いで温風乾燥させた。この工程を1回とし、30回繰り返した。その後、実施例1と同様の方法により、処理した評価用毛束の毛髪1本当りの引張切断強度(N)及び伸長率(%)を測定した(n=10)。 After applying 1 g of each sample solution as a shampoo to the evaluation hair bundle, the hair was sufficiently whipped, the hair was rinsed with warm water, and then the hair was dried with warm air. This step was set to 1 time and repeated 30 times. Then, the tensile cutting strength (N) and the elongation rate (%) per hair of the treated evaluation hair bundle were measured by the same method as in Example 1 (n = 10).
シャンプーによる損傷に対する毛髪保護試験結果は以下の通りである。この結果を指標として、毛髪損傷を評価した。
化粧料(A):引張強度0.95(N)及び伸長率38.0(%)
化粧料(B):引張強度1.08(N)及び伸長率42.5(%)
化粧料(C):引張強度1.22(N)及び伸長率44.4(%)
化粧料(D):引張強度1.03(N)及び伸長率42.2(%)
The results of the hair protection test against damage caused by shampoo are as follows. Hair damage was evaluated using this result as an index.
Cosmetics (A): Tensile strength 0.95 (N) and elongation 38.0 (%)
Cosmetics (B): Tensile strength 1.08 (N) and elongation 42.5 (%)
Cosmetics (C): Tensile strength 1.22 (N) and elongation 44.4 (%)
Cosmetics (D): Tensile strength 1.03 (N) and elongation 42.2 (%)
実施例1及び3より、本発明の実施品である化粧料(C)で処理した毛髪は、前記付加タンパク質を含まない化粧料(A)及び前記付加タンパク質に代えてカチオン化ケラチンを含む化粧料(B)で処理した毛髪と比べて、引張強度及び伸長率が大きい。同様に、実施例4より、本発明の実施品である化粧料(C)で処理した毛髪は、前記付加タンパク質を含まない化粧料(A)及び前記付加タンパク質に代えてカチオン化ケラチンを含む化粧料(B)及び(D)で処理した毛髪と比べて、引張強度及び伸長率が大きい。 From Examples 1 and 3, the hair treated with the cosmetic (C) which is the product of the present invention is the cosmetic (A) which does not contain the addition protein and the cosmetic which contains cationized keratin instead of the addition protein. The tensile strength and elongation rate are higher than those of the hair treated in (B). Similarly, from Example 4, the hair treated with the cosmetic (C), which is the product of the present invention, contains the cosmetic (A) containing no additional protein and the cosmetic containing cationized keratin in place of the additional protein. The tensile strength and elongation rate are higher than those of the hair treated with the agents (B) and (D).
更に、実施例2より、本発明の実施品である化粧料(C)は、前記付加タンパク質を含まない化粧料(A)及び前記付加タンパク質に代えてカチオン化ケラチンを含む化粧料(B)及び(D)と比べて、毛髪への付着率が2倍以上の高い。 Further, from Example 2, the cosmetics (C) which are the products of the present invention include the cosmetics (A) which do not contain the addition protein, and the cosmetics (B) which contain cationized keratin instead of the addition protein. Compared with (D), the adhesion rate to hair is more than twice as high.
これらの結果は、本発明の実施品である化粧料(C)は、適用部位(毛髪)への付着性に優れ、熱及び摩擦からの物理的な毛髪損傷に対する保護効果(実施例1及び3)と、シャンプーによる化学的な毛髪損傷に対する保護効果(実施例4)のいずれにも優れていることを示している。 These results show that the cosmetic product (C), which is the product of the present invention, has excellent adhesion to the application site (hair) and has a protective effect against physical hair damage from heat and friction (Examples 1 and 3). ) And the protective effect against chemical hair damage caused by shampoo (Example 4) are both excellent.
Claims (3)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2019027223A JP7281172B2 (en) | 2019-02-19 | 2019-02-19 | cosmetics |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2019027223A JP7281172B2 (en) | 2019-02-19 | 2019-02-19 | cosmetics |
Publications (2)
Publication Number | Publication Date |
---|---|
JP2020132563A true JP2020132563A (en) | 2020-08-31 |
JP7281172B2 JP7281172B2 (en) | 2023-05-25 |
Family
ID=72277669
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2019027223A Active JP7281172B2 (en) | 2019-02-19 | 2019-02-19 | cosmetics |
Country Status (1)
Country | Link |
---|---|
JP (1) | JP7281172B2 (en) |
Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH02243614A (en) * | 1988-12-19 | 1990-09-27 | Lion Corp | Hair cosmetic |
JP2002167437A (en) * | 2000-11-29 | 2002-06-11 | Lion Corp | Guanidine-modified silicone, method for producing the same, hair cosmetic, and fiber-treating agent using the same |
JP2008533218A (en) * | 2005-02-02 | 2008-08-21 | ゴールドシュミット ゲーエムベーハー | Guanidino group-containing siloxanes and their use for cosmetic formulations |
JP2017124983A (en) * | 2016-01-13 | 2017-07-20 | 株式会社 リトル・サイエンティスト | Cosmetic |
-
2019
- 2019-02-19 JP JP2019027223A patent/JP7281172B2/en active Active
Patent Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH02243614A (en) * | 1988-12-19 | 1990-09-27 | Lion Corp | Hair cosmetic |
JP2002167437A (en) * | 2000-11-29 | 2002-06-11 | Lion Corp | Guanidine-modified silicone, method for producing the same, hair cosmetic, and fiber-treating agent using the same |
JP2008533218A (en) * | 2005-02-02 | 2008-08-21 | ゴールドシュミット ゲーエムベーハー | Guanidino group-containing siloxanes and their use for cosmetic formulations |
JP2017124983A (en) * | 2016-01-13 | 2017-07-20 | 株式会社 リトル・サイエンティスト | Cosmetic |
Also Published As
Publication number | Publication date |
---|---|
JP7281172B2 (en) | 2023-05-25 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP5558242B2 (en) | Hair treatment agent | |
US5753214A (en) | Base material for cosmetics and uses of the same | |
JP4947749B1 (en) | Cosmetic base material and cosmetics containing the cosmetic base material | |
JP2011502171A (en) | Keratin derivative and method for producing the same | |
WO2017122615A1 (en) | Cosmetic | |
WO2016006529A1 (en) | Hair treatment agent | |
JP5288426B1 (en) | Cosmetic base material and cosmetics containing the cosmetic base material | |
JP7281172B2 (en) | cosmetics | |
WO2018198942A1 (en) | Fiber treatment agent and method for using same | |
JP2011088828A (en) | Cosmetic base and cosmetic containing the cosmetic base | |
Teglia et al. | Proteins in cosmetics | |
JP2005247692A (en) | Hair cosmetic | |
JP2000327545A (en) | First agent for permanent wave | |
JP4344644B2 (en) | Cosmetic base material | |
JPH10120533A (en) | Hair treatment composition of two-agent type | |
JP2001026521A (en) | Cosmetic substrate | |
JP2011084489A (en) | Cosmetic | |
JP2004175684A (en) | Cosmetic | |
JP2000281539A (en) | Cosmetic base | |
JP2009120523A (en) | Cosmetic | |
JP2000302652A (en) | Hair treating agent | |
JP2001039838A (en) | Hair processing agent | |
JPH11269045A (en) | Hair-protecting agent | |
JP2004175699A (en) | Hair treatment preparation | |
JP2002226330A (en) | Hair cosmetic |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20211206 |
|
A977 | Report on retrieval |
Free format text: JAPANESE INTERMEDIATE CODE: A971007 Effective date: 20220929 |
|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20221004 |
|
A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20221202 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20230127 |
|
TRDD | Decision of grant or rejection written | ||
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20230411 |
|
A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20230508 |
|
R150 | Certificate of patent or registration of utility model |
Ref document number: 7281172 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |