JP2008239507A - Stabilizer of triple helical structure of collagen - Google Patents
Stabilizer of triple helical structure of collagen Download PDFInfo
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- JP2008239507A JP2008239507A JP2007078850A JP2007078850A JP2008239507A JP 2008239507 A JP2008239507 A JP 2008239507A JP 2007078850 A JP2007078850 A JP 2007078850A JP 2007078850 A JP2007078850 A JP 2007078850A JP 2008239507 A JP2008239507 A JP 2008239507A
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- helical structure
- atelocollagen
- triple helical
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Abstract
Description
本発明は、コラーゲンの三重螺旋構造の安定化技術に関する。 The present invention relates to a technique for stabilizing a triple helix structure of collagen.
コラーゲンは、動物の結合組織の主要な蛋白質の一種で、動物の皮膚に多く存在する。ヒトの全タンパク質の３０％はコラーゲンであると言われている。コラーゲンは３本の分子鎖からなる三重螺旋構造を有し、両端にテロペプタイドが結合している。このテロペプタイドは溶解性の妨げとなり、また、抗原性を有するので、除去することが望ましい。このテロペプタイドをプロテアーゼ処理により除去する方法が一般的に知られており、テロペプタイドを除去したコラーゲンはアテロコラーゲンと呼ばれている。アテロコラーゲンの溶解性をさらに高めるために、アシル化する技術が知られている（特許文献１：特開２００３−１２８６９８号公報）。コラーゲンをアルキルオキシアルキレングリコール誘導体でエステル化して溶解性を向上させる技術が知られている（特許文献２：特許３７４２１３３号公報）。コラーゲンの三重螺旋構造に着目し、温和な条件で螺旋構造をほぐして、分子鎖を切断することなく、単独の分子鎖とすることにより溶解性を向上させる技術が知られている（特許文献３：特開２０００−１２８７５９号公報）。しかしながら、コラーゲンの三重螺旋構造を安定化する技術についての検討はなされていない。 Collagen is one of the main proteins in animal connective tissue and is abundant in animal skin. It is said that 30% of all human proteins are collagen. Collagen has a triple helical structure consisting of three molecular chains, and telopeptides are bonded to both ends. Since this telopeptide hinders solubility and has antigenicity, it is desirable to remove it. A method for removing this telopeptide by protease treatment is generally known, and collagen from which telopeptide has been removed is called atelocollagen. In order to further increase the solubility of atelocollagen, an acylation technique is known (Patent Document 1: Japanese Patent Application Laid-Open No. 2003-128698). A technique for improving the solubility by esterifying collagen with an alkyloxyalkylene glycol derivative is known (Patent Document 2: Japanese Patent No. 3742133). Focusing on the triple helical structure of collagen, a technique is known in which the helical structure is loosened under mild conditions, and the solubility is improved by breaking the molecular chain into a single molecular chain without breaking the molecular chain (Patent Document 3). : JP 2000-128759 A). However, a technique for stabilizing the triple helix structure of collagen has not been studied.
三重螺旋構造が安定化されたコラーゲンを提供すること。 To provide collagen in which a triple helix structure is stabilized.
本発明の主な構成は、次のとおりである。
（１）β−シクロデキストリン、ラクトース、ジグリセリン、ヒアルロン酸、ラフィノースからなる群から選ばれる１種または２種以上を含有するコラーゲンの三重螺旋構造安定化剤。
（２）コラーゲンがサクシニル化アテロコラーゲンである（１）に記載のコラーゲンの三重螺旋構造安定化剤。
（３） （１）または（２）に記載のコラーゲンの三重螺旋構造安定化剤とサクシニル化アテロコラーゲンを含有することを特徴とする化粧料。
（４）β−シクロデキストリン、ラクトース、ジグリセリン、ヒアルロン酸、ラフィノースからなる群から選ばれる１種または２種以上とサクシニル化アテロコラーゲンとからなる三重螺旋構造が安定化されたサクシニル化アテロコラーゲン。
The main configuration of the present invention is as follows.
(1) A triple-helical structure stabilizer for collagen containing one or more selected from the group consisting of β-cyclodextrin, lactose, diglycerin, hyaluronic acid, and raffinose.
(2) The collagen triple helical structure stabilizer according to (1), wherein the collagen is succinylated atelocollagen.
(3) A cosmetic comprising the collagen triple helical structure stabilizer according to (1) or (2) and succinylated atelocollagen.
(4) A succinylated atelocollagen in which a triple helical structure composed of one or more selected from the group consisting of β-cyclodextrin, lactose, diglycerin, hyaluronic acid and raffinose and a succinylated atelocollagen is stabilized.
三重螺旋構造を安定的に維持したサクシニル化アテロコラーゲン等のコラーゲンを提供することができる。
β−シクロデキストリン、ラクトース、ジグリセリン、ヒアルロン酸、ラフィノースから選択されるコラーゲンの三重螺旋構造安定化剤を提供することができる。
、β−シクロデキストリン、ラクトース、ジグリセリン、ヒアルロン酸、ラフィノースから選択されるコラーゲンの三重螺旋構造安定化剤とサクシニル化アテロコラーゲン等のコラーゲンを含有させて三重螺旋構造を保持したコラーゲンの機能を発揮する化粧料を提供することができる。
Collagens such as succinylated atelocollagen that stably maintain the triple helical structure can be provided.
A collagen triple-helical structure stabilizer selected from β-cyclodextrin, lactose, diglycerin, hyaluronic acid, and raffinose can be provided.
, Β-cyclodextrin, lactose, diglycerin, hyaluronic acid, raffinose selected from collagen triple helix structure stabilizer and collagen such as succinylated atelocollagen to exert the function of collagen retaining triple helix structure Cosmetics can be provided.
本発明に用いるコラーゲンは三重螺旋構造を維持したコラーゲンであり、特に、サクシニル化アテロコラーゲンである。
コラーゲンは動物の皮膚、例えば、牛皮、豚皮、魚皮から抽出することができる。抽出方法としては例えば、まず、魚皮から不純タンパク質、血液、色素、脂質等をナイフ等の刃物を用いたり、水流により除き、次いで塩溶液、塩基性溶液で洗浄し、さらに有機溶剤で洗浄して不純物を取り除く。得られた魚皮をｐＨ３に調整した酸溶液に分散し、酸性プロテアーゼによるプロテアーゼ処理をすることによりアテロコラーゲンが得られる。より具体的には、０．０１〜２ｍｏｌ／Ｌの希酢酸溶液、０．００１〜２ｍｏｌ／Ｌの希乳酸溶液、０．００１〜２ｍｏｌ／Ｌの希クエン酸溶液、０．００１〜０．２ｍｏｌ／Ｌの希塩酸溶液、０．００１〜０．５ｍｏｌ／Ｌの希リン酸溶液等の酸溶液に不純物を取り除いた魚皮を加え、さらに、酸性プロテアーゼを加え、３〜５℃の低温で１２〜４８時間攪拌することにより、三重螺旋構造を維持したアテロコラーゲンを抽出することができる。不溶解物は濾過法、遠心分離法により除去することが望ましい。酸性プロテアーゼはコラーゲン溶液を塩基を用いてｐＨ１０〜１２に調整し、３〜５℃の低温で１２〜４８時間攪拌することにより失活させることができる。
The collagen used in the present invention is a collagen maintaining a triple helical structure, and in particular, succinylated atelocollagen.
Collagen can be extracted from animal skin, such as cow skin, pig skin, and fish skin. As an extraction method, for example, first, impure proteins, blood, pigments, lipids, etc. are removed from fish skin using a knife or other blades, or washed with a water flow, then washed with a salt solution or a basic solution, and further washed with an organic solvent. To remove impurities. Atelocollagen is obtained by dispersing the obtained fish skin in an acid solution adjusted to pH 3 and subjecting it to a protease treatment with an acidic protease. More specifically, 0.01-2 mol / L dilute acetic acid solution, 0.001-2 mol / L dilute lactic acid solution, 0.001-2 mol / L dilute citric acid solution, 0.001-0.2 mol. The fish skin from which impurities are removed is added to an acid solution such as / L diluted hydrochloric acid solution or 0.001 to 0.5 mol / L diluted phosphoric acid solution, and further, an acidic protease is added, and 12 to 12 at a low temperature of 3 to 5 ° C. By stirring for 48 hours, atelocollagen maintaining a triple helical structure can be extracted. It is desirable to remove insoluble matter by filtration or centrifugation. The acidic protease can be inactivated by adjusting the collagen solution to pH 10-12 using a base and stirring at a low temperature of 3-5 ° C. for 12-48 hours.
アテロコラーゲンのサクシニル化は得られたアテロコラーゲン溶液に無水コハク酸を加え、ｐＨを９〜１２に維持するようにアルカリを添加しながら、３〜５℃の低温で反応させる。
サクシニル化アテロコラーゲンは塩析法、有機溶媒沈殿法、等電点沈殿法等の定法により精製することができる。
本発明の三重螺旋構造を維持したサクシニル化アテロコラーゲンは１５℃における比旋光度が約−４２０°〜−３１０°であり、加温攪拌して完全に三重螺旋構造をほぐしたサクシニル化アテロコラーゲンの１５℃における比旋光度は約−１００°である。
In the succinylation of atelocollagen, succinic anhydride is added to the obtained atelocollagen solution, and the reaction is carried out at a low temperature of 3-5 ° C. while adding an alkali so as to maintain the pH at 9-12.
Succinylated atelocollagen can be purified by conventional methods such as salting out, organic solvent precipitation, and isoelectric point precipitation.
The succinylated atelocollagen maintaining the triple helix structure of the present invention has a specific rotation of about -420 ° to -310 ° at 15 ° C. The specific optical rotation at is about -100 °.
本発明の三重螺旋構造を維持したサクシニル化アテロコラーゲンは化粧料に配合することにより、皮膚の柔軟性を向上させる優れた効果を有する。
本発明のサクシニル化アテロコラーゲンの化粧料への配合量は０．０００１〜２質量％が好ましく、０．００１〜０．５質量％が特に好ましい。０．０００１質量％未満では皮膚の柔軟性向上効果が発揮されず、２質量％を超えて配合するとべたつきが強く好ましくない。
The succinylated atelocollagen maintaining the triple helix structure of the present invention has an excellent effect of improving the flexibility of the skin when blended in cosmetics.
The amount of the succinylated atelocollagen of the present invention in the cosmetic is preferably 0.0001 to 2 mass%, particularly preferably 0.001 to 0.5 mass%. If it is less than 0.0001% by mass, the effect of improving skin flexibility is not exhibited, and if it exceeds 2% by mass, stickiness is strong and undesirable.
本発明のサクシニル化アテロコラーゲンを配合した化粧料には、植物油のような油脂類、高級脂肪酸、高級アルコール、シリコーン、アニオン界面活性剤、カチオン界面活性剤、両性界面活性剤、非イオン界面活性剤、防腐剤、糖類、金属イオン封鎖剤、水溶性高分子のような高分子、増粘剤、粉体成分、紫外線吸収剤、紫外線遮断剤、ヒアルロン酸のような保湿剤、香料、ｐＨ調整剤、乾燥剤等を含有させることができる。ビタミン類、皮膚賦活剤、血行促進剤、常在菌コントロール剤、活性酸素消去剤、抗炎症剤、美白剤、殺菌剤等の他の薬効成分、生理活性成分を含有させることができる。
本発明の化粧料は、例えば水溶液、乳液、けんだく液等の液剤、ゲル、クリーム等の半固形剤の形態で適用可能である。また、粉末、固形状の製剤として、使用時に水あるいは水溶液に溶解して皮膚に外用するものであっても良い。従来から公知の方法でこれらの形態に調製し、ローション剤、乳剤、ゲル剤、クリーム剤等の種々の剤型とすることができる。化粧料としては、化粧水、乳液、クリーム、パック等の皮膚化粧料、メイクアップベースローション、メイクアップクリーム、乳液状又はクリーム状のファンデーション等のメイクアップ化粧料、ハンドクリーム、レッグクリーム、ボディローション等の身体用化粧料等とすることができる。
Cosmetics containing the succinylated atelocollagen of the present invention include fats and oils such as vegetable oils, higher fatty acids, higher alcohols, silicones, anionic surfactants, cationic surfactants, amphoteric surfactants, nonionic surfactants, Preservatives, sugars, sequestering agents, polymers such as water-soluble polymers, thickeners, powder components, UV absorbers, UV blockers, moisturizers such as hyaluronic acid, fragrances, pH adjusters, A desiccant etc. can be contained. Vitamins, skin activators, blood circulation promoters, resident bacteria control agents, active oxygen scavengers, anti-inflammatory agents, whitening agents, bactericides, and other medicinal and physiologically active components can be included.
The cosmetic of the present invention can be applied, for example, in the form of a liquid agent such as an aqueous solution, milky lotion, or soap solution, or a semi-solid agent such as a gel or cream. Further, as a powder or solid preparation, it may be dissolved in water or an aqueous solution at the time of use and externally applied to the skin. It can be prepared in these forms by a conventionally known method to form various dosage forms such as lotions, emulsions, gels and creams. Cosmetics include skin lotions such as lotions, emulsions, creams, packs, makeup base lotions, makeup creams, makeup cosmetics such as emulsions or creamy foundations, hand creams, leg creams, body lotions. And so on.
安定性試験
以下の製法によりサクシニル化アテロコラーゲンを調製した。製造工程を通して温度は３℃〜５℃内の範囲を外れないようにコントロールした。
魚皮精製沈殿30gを0.03mol/Lの濃度のクエン酸水溶液3000mLに加え、1時間撹拌した後、ペプシン0.9gを加えさらに24時間攪拌抽出した。その後、温度が上昇しないように注意しながら1N水酸化ナトリウムを加えてpH10に調整し、24時間攪拌しペプシンを失活させた。得られたアテロコラーゲン溶液に無水コハク酸30mmolを加え、水酸化ナトリウム溶液を用いてpHを9〜12に調整しながら反応させた。反応終了後、溶液のpHを塩酸を用いてpH4.5に調整して、サクシニル化アテロコラーゲンを沈殿させ、濾過法及び遠心分離法(10000G,20分)により回収した後、4℃に冷やした50%エタノールを用いて洗浄した。1.0質量%の濃度となるように、４％の１，２−ペンタンジオールを含有する0.05mol/Lのリン酸緩衝溶液(pH6.0)に溶解し、サクシニル化アテロコラーゲン溶液を得た。
製造直後のサクシニル化アテロコラーゲンの１質量％水溶液（４％の１，２−ペンタンジオール含有）を４℃で保管した。β−シクロデキストリン、ラクトース、ジグリセリン、ラフィノース、マンニトール、グルコース、グリセリン、ガラクツロン酸、１，３−ブチレングリコール、Ｌ−セリンの１質量％水溶液及びヒアルロン酸の０．１質量％水溶液を調製し、サクシニル化アテロコラーゲンの１質量％水溶液と等量で混合することにより試験品とした。サクシニル化アテロコラーゲンの１質量％水溶液と水との等量混合液を対照試料とした。対照試料の１５℃における旋光度は−３８６°であった（測定装置：ＡＵＴＯＰＯＬ Ｖ（ＲＵＤＯＬＰＨ ＲＥＳＥＡＲＣＨ ＡＮＡＬＹＳＹＳ社））。
Stability test Succinylated atelocollagen was prepared by the following method. Throughout the manufacturing process, the temperature was controlled so as not to deviate from the range of 3 ° C to 5 ° C.
30 g of the fish skin purified precipitate was added to 3000 mL of an aqueous citric acid solution having a concentration of 0.03 mol / L, stirred for 1 hour, 0.9 g of pepsin was added, and the mixture was further extracted by stirring for 24 hours. Thereafter, 1N sodium hydroxide was added to adjust to pH 10 while taking care not to raise the temperature, and stirring was continued for 24 hours to inactivate pepsin. 30 mmol of succinic anhydride was added to the obtained atelocollagen solution, and the reaction was carried out while adjusting the pH to 9-12 using a sodium hydroxide solution. After completion of the reaction, the pH of the solution was adjusted to pH 4.5 using hydrochloric acid, succinylated atelocollagen was precipitated, recovered by filtration and centrifugation (10000 G, 20 minutes), and then cooled to 4 ° C. 50 Washed with% ethanol. A succinylated atelocollagen solution was obtained by dissolving in a 0.05 mol / L phosphate buffer solution (pH 6.0) containing 4% 1,2-pentanediol so as to have a concentration of 1.0% by mass.
A 1% by weight aqueous solution (containing 4% 1,2-pentanediol) of succinylated atelocollagen immediately after production was stored at 4 ° C. β-cyclodextrin, lactose, diglycerin, raffinose, mannitol, glucose, glycerin, galacturonic acid, 1,3-butylene glycol, L-serine 1% by weight aqueous solution and hyaluronic acid 0.1% by weight aqueous solution, A test product was prepared by mixing the succinylated atelocollagen with a 1% by weight aqueous solution in an equal amount. A control sample was a mixture of equal amounts of a 1% by weight aqueous solution of succinylated atelocollagen and water. The optical rotation at 15 ° C. of the control sample was −386 ° (measuring apparatus: AUTOPOL V (RUDOLPH RESEARCH ANALYSYS)).
試験品を４０℃で加温し、その後４℃に冷却し、１５℃に加温して１５℃の比旋光度の変化量と回復率を求めた。結果を表１に示す。
回復率は、加温前の対照試料の１５℃における旋光度−３８６°を基準として、次式により求めた。
回復率（％）＝（−３８６＋比旋光度の変化量）／（−３８６）×１００
The test article was heated at 40 ° C., then cooled to 4 ° C., heated to 15 ° C., and the amount of change in optical rotation and the recovery rate at 15 ° C. were determined. The results are shown in Table 1.
The recovery rate was determined by the following formula based on the optical rotation at −15 ° C. of the control sample before heating at −386 °.
Recovery rate (%) = (− 386 + change in specific rotation) / (− 386) × 100
対照試料の比旋光度の回復率が８１％であるのに対して、実施例１のβ−シクロデキストリン混合試料では９５％、実施例２のラクトース混合試料では９６％、実施例３のジグリセリン混合試料では９２％、実施例４のヒアルロン酸混合試料では９２％、実施例５のラフィノース混合試料では９０％であった。実施例１〜５の回復率は９０％以上と高く、コラーゲンの三重螺旋構造を安定化した。比較例１のマンニトール混合試料では８６％、比較例２のグルコース混合試料では８５％、比較例３のグリセリン混合試料では８２％であり、対照試料よりも変化量は小さかったが、三重螺旋構造の安定化効果は十分ではない。比較例４のガラクツロン酸混合試料では７８％、比較例５の１，３−ブチレングリコール混合試料では８０％、比較例６のＬ−セリンでは７９％であり、対照試料よりも三重螺旋構造の安定性が悪かった。
The recovery rate of the specific rotation of the control sample was 81%, while 95% for the β-cyclodextrin mixed sample of Example 1, 96% for the lactose mixed sample of Example 2, and diglycerin of Example 3 The mixed sample was 92%, the hyaluronic acid mixed sample of Example 4 was 92%, and the raffinose mixed sample of Example 5 was 90%. The recovery rate of Examples 1 to 5 was as high as 90% or more, and the collagen triple helix structure was stabilized. The mannitol mixed sample of Comparative Example 1 was 86%, the glucose mixed sample of Comparative Example 2 was 85%, the glycerin mixed sample of Comparative Example 3 was 82%, and the change amount was smaller than that of the control sample. The stabilizing effect is not enough. The galacturonic acid mixed sample of Comparative Example 4 was 78%, the 1,3-butylene glycol mixed sample of Comparative Example 5 was 80%, and the L-serine of Comparative Example 6 was 79%. The triple helical structure was more stable than the control sample. The nature was bad.
処方例１ 化粧水 質量％
精製水 残余
β−シクロデキストリン ５．０
ラクトース １．５
ジグリセリン ２．０
サクシニル化アテロコラーゲン ０．５
［製法］上記成分を混合溶解して化粧水を得た。
Formulation Example 1 Lotion Mass%
Purified water residue β-cyclodextrin 5.0
Lactose 1.5
Diglycerin 2.0
Succinylated atelocollagen 0.5
[Production Method] The above ingredients were mixed and dissolved to obtain a skin lotion.
処方例２ 乳液 質量％
（Ａ）精製水 残余
β―シクロデキストリン ６．０
ラクトース ２．０
ヒアルロン酸ナトリウム ０．０１
（Ｂ) ホホバ油 １．５
スクワラン １．５
ポリオキシエチレン硬化ヒマシ油 １．０
（Ｃ）サクシニル化アテロコラーゲン １．０
精製水 ３．０
［製法］Ａに属する水相成分とＢに属する油相成分をそれぞれ加熱溶解し、油相成分を水相成分に混合し、乳化機にて乳化する。冷却後、Ｃ成分を混合し、乳液を得た。
Formulation Example 2 Latex Mass%
(A) Purified water Residual β-cyclodextrin 6.0
Lactose 2.0
Sodium hyaluronate 0.01
(B) Jojoba oil 1.5
Squalane 1.5
Polyoxyethylene hydrogenated castor oil 1.0
(C) Succinylated atelocollagen 1.0
Purified water 3.0
[Production Method] The aqueous phase component belonging to A and the oil phase component belonging to B are heated and dissolved, respectively, and the oil phase component is mixed with the aqueous phase component and emulsified by an emulsifier. After cooling, component C was mixed to obtain an emulsion.
処方例３ 美容液 質量％
（Ａ）精製水 残余
β−シクロデキストリン ６．０
ラクトース ２．０
ジグリセリン １．０
ラフィノース １．０
カルボキシビニルポリマー ０．１５
（Ｂ）水酸化カリウム ０．０４
精製水 ２．０
（Ｃ）サクシニル化アテロコラーゲン １．０
精製水 ３．０
［製法］上記Ａに属する成分を混合溶解した後、Ｂに属する成分を混合し、さらに冷却後Ｃ成分を混合して美容液を得た。
Formulation 3 Essence Mass%
(A) Purified water Residual β-cyclodextrin 6.0
Lactose 2.0
Diglycerin 1.0
Raffinose 1.0
Carboxyvinyl polymer 0.15
(B) Potassium hydroxide 0.04
Purified water 2.0
(C) Succinylated atelocollagen 1.0
Purified water 3.0
[Production Method] After the components belonging to A were mixed and dissolved, the components belonging to B were mixed, and after cooling, the C component was mixed to obtain a cosmetic liquid.
処方例４ クリーム 質量％
（Ａ）精製水 残余
β−シクロデキストリン ３．０
ラクトース １．０
ラフィノース ０．５
ジグリセリン ２．０
（Ｂ）ホホバ油 ８．５
スクワラン １０．０
新油型モノステアリン酸グリセリン ３．０
モノステアリン酸ソルビタン １．５
モノステアリン酸ポリオキシエチレンソルビタン（２０Ｅ．Ｏ．) １．０
（Ｃ）サクシニル化アテロコラーゲン ２．０
精製水 ６．０
［製法］Ａに属する水相成分とＢに属する油相成分をそれぞれ加熱溶解し、油相成分を水相成分に混合し、乳下機にて乳化する。冷却後、Ｃ成分を混合してクリームを得た。
Formulation Example 4 Cream Mass%
(A) Purified water Residual β-cyclodextrin 3.0
Lactose 1.0
Raffinose 0.5
Diglycerin 2.0
(B) Jojoba oil 8.5
Squalane 10.0
New oil type glyceryl monostearate 3.0
Sorbitan monostearate 1.5
Polyoxyethylene sorbitan monostearate (20E.O.) 1.0
(C) Succinylated atelocollagen 2.0
Purified water 6.0
[Manufacturing method] The aqueous phase component belonging to A and the oil phase component belonging to B are heated and dissolved, respectively, and the oil phase component is mixed with the aqueous phase component and emulsified in a milking machine. After cooling, C component was mixed to obtain a cream.
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| JP2015134733A (en) * | 2014-01-17 | 2015-07-27 | 株式会社ファンケル | Stabilizer of triple helical structure of collagen |
| KR20200090628A (en) * | 2019-01-21 | 2020-07-29 | 주식회사 브라이언스랩 | Hibiscus extracts containing food composition thereof and preparation method of the hibiscus extracts |
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| JPS5528947A (en) * | 1978-08-22 | 1980-02-29 | Koken:Kk | Cosmetic and its preparation |
| JPS5869806A (en) * | 1981-10-20 | 1983-04-26 | Mochida Pharmaceut Co Ltd | Cosmetic lotion containing stable collagen |
| JPS62145006A (en) * | 1985-12-18 | 1987-06-29 | Koken:Kk | Makeup film comprising chemically modified collagen |
| JPH02184612A (en) * | 1989-01-12 | 1990-07-19 | Koken Co Ltd | Preparation-in-use type cosmetic |
| JPH08151598A (en) * | 1994-11-30 | 1996-06-11 | Kawaken Fine Chem Co Ltd | Solubilizing agent for undenatured water-soluble collagen |
| JPH09278639A (en) * | 1996-04-05 | 1997-10-28 | Taiken Enterp:Kk | Cosmetic containing collagen |
| JP2000256398A (en) * | 1999-03-09 | 2000-09-19 | Katakura Chikkarin Co Ltd | Collagen originated from fish skin and cosmetic containing the collagen |
| JP2002284618A (en) * | 2001-03-26 | 2002-10-03 | Mitsuo Matsumoto | Preparing and selling method of liquid cosmetics by custom made system |
| JP2003128698A (en) * | 2001-10-24 | 2003-05-08 | Katakura Chikkarin Co Ltd | Acylated attelo collagen from fish skin, its manufacturing method, and fine cosmetic compounded with its compound |
| JP2006193463A (en) * | 2005-01-13 | 2006-07-27 | Pola Chem Ind Inc | Cosmetic |
| JP2007070330A (en) * | 2005-09-06 | 2007-03-22 | Biomate International:Kk | Cosmetic |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2015134733A (en) * | 2014-01-17 | 2015-07-27 | 株式会社ファンケル | Stabilizer of triple helical structure of collagen |
| KR20200090628A (en) * | 2019-01-21 | 2020-07-29 | 주식회사 브라이언스랩 | Hibiscus extracts containing food composition thereof and preparation method of the hibiscus extracts |
| KR102398484B1 (en) * | 2019-01-21 | 2022-05-16 | 주식회사 브라이언스랩 | Hibiscus extracts containing food composition thereof and preparation method of the hibiscus extracts |
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