JPH03294211A - Cosmetic - Google Patents
CosmeticInfo
- Publication number
- JPH03294211A JPH03294211A JP9836490A JP9836490A JPH03294211A JP H03294211 A JPH03294211 A JP H03294211A JP 9836490 A JP9836490 A JP 9836490A JP 9836490 A JP9836490 A JP 9836490A JP H03294211 A JPH03294211 A JP H03294211A
- Authority
- JP
- Japan
- Prior art keywords
- cosmetic
- proteinase
- present
- water
- thermolysin
- 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 22
- 108091005804 Peptidases Proteins 0.000 claims abstract description 27
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims abstract description 23
- 102000035195 Peptidases Human genes 0.000 claims abstract description 22
- PUPZLCDOIYMWBV-UHFFFAOYSA-N (+/-)-1,3-Butanediol Chemical compound CC(O)CCO PUPZLCDOIYMWBV-UHFFFAOYSA-N 0.000 claims abstract description 15
- 108090001109 Thermolysin Proteins 0.000 claims abstract description 10
- 229940058015 1,3-butylene glycol Drugs 0.000 claims abstract description 7
- 235000019437 butane-1,3-diol Nutrition 0.000 claims abstract description 7
- -1 aqualysin Proteins 0.000 claims abstract description 4
- 108010031354 thermitase Proteins 0.000 claims abstract description 4
- 241000894006 Bacteria Species 0.000 claims description 13
- 235000011187 glycerol Nutrition 0.000 claims description 10
- 239000004365 Protease Substances 0.000 claims description 7
- 239000000203 mixture Substances 0.000 claims description 7
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 5
- 230000000694 effects Effects 0.000 abstract description 15
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 abstract description 14
- 102000004169 proteins and genes Human genes 0.000 abstract description 6
- 108090000623 proteins and genes Proteins 0.000 abstract description 6
- 235000019833 protease Nutrition 0.000 abstract 5
- 244000005700 microbiome Species 0.000 abstract 3
- 239000000654 additive Substances 0.000 abstract 1
- 230000000996 additive effect Effects 0.000 abstract 1
- 108010092440 caldolysin Proteins 0.000 abstract 1
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 8
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 239000006210 lotion Substances 0.000 description 5
- 235000018102 proteins Nutrition 0.000 description 5
- 239000008213 purified water Substances 0.000 description 5
- 210000003491 skin Anatomy 0.000 description 5
- 238000011156 evaluation Methods 0.000 description 4
- 239000003205 fragrance Substances 0.000 description 4
- 235000019419 proteases Nutrition 0.000 description 4
- 150000005846 sugar alcohols Polymers 0.000 description 4
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 3
- 239000002552 dosage form Substances 0.000 description 3
- 229960001617 ethyl hydroxybenzoate Drugs 0.000 description 3
- 235000010228 ethyl p-hydroxybenzoate Nutrition 0.000 description 3
- 239000004403 ethyl p-hydroxybenzoate Substances 0.000 description 3
- NUVBSKCKDOMJSU-UHFFFAOYSA-N ethylparaben Chemical compound CCOC(=O)C1=CC=C(O)C=C1 NUVBSKCKDOMJSU-UHFFFAOYSA-N 0.000 description 3
- 230000001815 facial effect Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 241000589596 Thermus Species 0.000 description 2
- 241000589500 Thermus aquaticus Species 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- POULHZVOKOAJMA-UHFFFAOYSA-N dodecanoic acid Chemical compound CCCCCCCCCCCC(O)=O POULHZVOKOAJMA-UHFFFAOYSA-N 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- KAKVFSYQVNHFBS-UHFFFAOYSA-N (5-hydroxycyclopenten-1-yl)-phenylmethanone Chemical compound OC1CCC=C1C(=O)C1=CC=CC=C1 KAKVFSYQVNHFBS-UHFFFAOYSA-N 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 239000005639 Lauric acid Substances 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 229920002125 Sokalan® Polymers 0.000 description 1
- 241000203770 Thermoactinomyces vulgaris Species 0.000 description 1
- 239000006096 absorbing agent Substances 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- QGZDXQHLEQAGJB-INIZCTEOSA-N benzyl n-[2-[[(2s)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-2-oxoethyl]carbamate Chemical compound C([C@@H](C(=O)N)NC(=O)CNC(=O)OCC=1C=CC=CC=1)C1=CC=CC=C1 QGZDXQHLEQAGJB-INIZCTEOSA-N 0.000 description 1
- 108010092174 carbobenzoxyglycylphenylalanine amide Proteins 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 235000019864 coconut oil Nutrition 0.000 description 1
- 239000003240 coconut oil Substances 0.000 description 1
- 239000000306 component Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- SZXQTJUDPRGNJN-UHFFFAOYSA-N dipropylene glycol Chemical compound OCCCOCCCO SZXQTJUDPRGNJN-UHFFFAOYSA-N 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
- 239000006260 foam Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 210000000232 gallbladder Anatomy 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 239000004584 polyacrylic acid Substances 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 210000004927 skin cell Anatomy 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 210000000106 sweat gland Anatomy 0.000 description 1
- 239000000454 talc Substances 0.000 description 1
- 229910052623 talc Inorganic materials 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
Landscapes
- Cosmetics (AREA)
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
本発明は化粧料に関し、更に詳細には好熱性菌由来の蛋
白質分解酵素を含有し、皮膚表面の蛋白質汚れの除去効
果に優れ、かつ水に対する安定性の良好な化粧料に関す
る。[Detailed Description of the Invention] [Field of Industrial Application] The present invention relates to cosmetics, and more particularly, the present invention relates to cosmetics that contain a proteolytic enzyme derived from thermophilic bacteria, have an excellent effect of removing protein stains on the skin surface, and are water resistant. The present invention relates to a cosmetic with good stability against.
皮膚表面の汚れは、蛋白質、脂質をはじめとする種々の
物質から成り、なかでも蛋白質は老化して不要となった
角質や汗腺分泌物に由来している。Dirt on the skin surface is made up of various substances including proteins and lipids, and among these, proteins originate from dead skin cells and sweat gland secretions that are no longer needed due to aging.
これらの汚れは皮膚の正常な生理機能や代謝を低下させ
る原因となっている。このため従来より、蛋白質汚れを
除去する目的で蛋白質分解酵素を化粧料中に配合する試
みがなされてきた。These stains cause a decline in the normal physiological functions and metabolism of the skin. For this reason, attempts have been made to incorporate proteolytic enzymes into cosmetics for the purpose of removing protein stains.
しかしながら、従来使用されてきた蛋白質分解酵素、例
えばパパイン、プロメライン、ビオブラーゼ等は安定性
が悪く、経時的に酵素活性が消失するという欠点を有し
ており、特に水分を含有する剤型の化粧料中に配合した
場合にはそれが著しいことが知られている。However, conventionally used proteolytic enzymes, such as papain, promelain, and biobrase, have the disadvantage of poor stability and loss of enzyme activity over time. It is known that this effect is significant when it is added to food.
そこで、更に１，３−ブチレングリコール、グリセリン
、ジプロピレングリコール等の多価アルコールを組み合
わせることによってその安定性を向上させる試みがなさ
れてきたが、未だ十分満足し得るものではなかった。Therefore, attempts have been made to improve the stability by further combining polyhydric alcohols such as 1,3-butylene glycol, glycerin, and dipropylene glycol, but these efforts have not yet been fully satisfactory.
上記実情に鑑み、本発明者らは鋭意研究を重ねた結果、
好熱性菌由来の蛋白質分解酵素を配合すれば、水分を含
有する剤型においても安定性に優れた化粧料が得られ、
またこの剤型に１，３−ブチレングリコール又はグリセ
リンを配合すれば当該蛋白質分解酵素の安定性が更に向
上することを見出し、本発明を完成するに至った。In view of the above circumstances, the inventors of the present invention have conducted extensive research, and as a result,
By incorporating proteolytic enzymes derived from thermophilic bacteria, cosmetics with excellent stability can be obtained even in the form of formulations containing water.
Furthermore, the inventors have discovered that the stability of the proteolytic enzyme can be further improved by adding 1,3-butylene glycol or glycerin to this dosage form, and have completed the present invention.
すなわち、本発明は好熱性菌由来の蛋白質分解酵素を含
有することを特徴とする化粧料を提供するものである。That is, the present invention provides a cosmetic composition characterized by containing a proteolytic enzyme derived from a thermophilic bacterium.
本発明に用いられる好熱性菌由来の蛋白質分解酵素とし
ては、特に制限されないが、サーモリシン、アクアリシ
ン、サーミターゼ又はカルドリシンが好ましい。これら
の蛋白質分解酵素の起源となる好熱性菌の菌株としては
、サーモリシンについてはバチルス サーモブロテオリ
イティカス（Ｂａｃｉｌｌｕｓ ｔｈｅｒｍｏ ｒｏｔ
ｅｏｌ ｔｉｃｕｓ） 、アクアリシンについてはサー
マス アクアティカス ＹＴ−１（Ｔｈｅｒｍｕｓ ｕ
堀１説邦Ｙ Ｔ−１） 、サーミターゼについてはサー
モアクチノマイセス ブルガリス（Ｔｈｅｒｍｏａｃｔ
ｉｎｏｍ ｃｅｓ 胆肱肛旦） 、カルドリシンについ
てはサーマス アクアティカス ストレイン Ｔ −３
５１（Ｔｈｅｒｍｕｓ 籾旺実耶５ｔｒａｉｎＴ−３５
１）が挙げられる。The thermophilic bacterium-derived protease used in the present invention is not particularly limited, but thermolysin, aquaricin, thermitase, or caldrisin is preferred. As for thermophilic bacterial strains that are the origin of these proteolytic enzymes, for thermolysin, Bacillus thermobroteolyticus
eol ticus), and Thermus aquaticus YT-1 (Thermus u
For the thermitase, Thermoactinomyces vulgaris (Thermoact
inom ces gallbladder), Thermus aquaticus strain T-3 for caldrisin
51 (Thermus 5 train T-35
1) is mentioned.
本発明において、蛋白質分解酵素は上記の菌株を常法に
従って培養し、得られた粗酵素又はこれを精製したもの
が用いられるが、これら蛋白質分解酵素の市販品を用い
てもよい。In the present invention, the protease used is a crude enzyme obtained by culturing the above-mentioned bacterial strain according to a conventional method, or a purified product thereof, but commercially available products of these proteolytic enzymes may also be used.
本発明の化粧料には、斯かる蛋白質分解酵素は一種又は
二種以上を組み合わせて配合することができ、その配合
量は全化粧料中、０．００１〜２０重量％、特にＯ，Ｏ
Ｓ〜５重量％の範囲であることが好ましい。In the cosmetics of the present invention, such proteolytic enzymes can be blended singly or in combination of two or more, and the blending amount is 0.001 to 20% by weight, especially O, O
It is preferably in the range of S to 5% by weight.
また、本発明の化粧料には、水分を含有する剤型におい
て蛋白質分解酵素の安定性を更に向上させる目的で１，
３−ブチレングリコール及びグリセリンの一方あるいは
双方を配合することができる。１，３−ブチレングリコ
ール及びグリセリンの配合量は全化粧料中、５〜３０重
量％の範囲であることが好ましい。In addition, the cosmetic of the present invention contains 1,
One or both of 3-butylene glycol and glycerin can be blended. The blending amount of 1,3-butylene glycol and glycerin is preferably in the range of 5 to 30% by weight based on the total cosmetic composition.
尚、本発明の化粧料には、その効果を損わない範囲内で
上記必須成分の他に必要に応じて、水、界面活性剤、油
剤、粉体、水溶性高分子、低級アルコール、美容成分、
防腐剤、酸化防止剤、紫外線吸収剤などを配合すること
ができる。また、本発明化粧料の剤型は蛋白質分解酵素
の作用を損わない剤型、例えば、皮膚洗浄液、化粧水、
クリーム、乳液、ファンデーション、パック、養毛・育
毛剤等が挙げられ、更には、使用時に水や他の化粧水に
溶解して用いる用時混合型の剤型とすることもできる。In addition to the above-mentioned essential ingredients, the cosmetic of the present invention may contain water, surfactants, oils, powders, water-soluble polymers, lower alcohols, cosmetics, etc., as necessary, within a range that does not impair its effects. component,
Preservatives, antioxidants, ultraviolet absorbers, etc. can be added. In addition, the dosage form of the cosmetic of the present invention is a dosage form that does not impair the action of proteolytic enzymes, such as skin cleansing liquid, lotion,
Examples include creams, milky lotions, foundations, packs, hair nourishing agents, and the like.Furthermore, they can also be prepared in the form of mix-and-mix formulations that are dissolved in water or other lotions at the time of use.
（１）好熱性菌由来の蛋白質分解酵素についての酵素安
定性の評価：
（評価方法）
本発明に係わる好熱性菌由来の蛋白質分解酵素であるサ
ーそりシン（シグマ社製、以下同じ）及び従来から常温
性菌由来の蛋白質分解酵素とじて知られているビオブラ
ーゼ（ナガセ生化学工業株式会社製、以下同じ）につい
て、４０℃の水中における経時的な活性変化を、サーモ
リシンについてはカルボベンゾキシグリシル−し−フェ
ニルアラニンアミドを、ビオプラーゼについてはカゼイ
ンを基質として測定し、その結果を表１に示した。(1) Evaluation of enzyme stability for proteases derived from thermophilic bacteria: (Evaluation method) Sarsolicin (manufactured by Sigma, hereinafter the same), which is a protease derived from thermophilic bacteria according to the present invention, and conventional For biobrase (manufactured by Nagase Seikagaku Kogyo Co., Ltd., hereinafter the same), which is known as a proteolytic enzyme derived from a thermophilic bacterium, the change in activity over time in water at 40°C was investigated, and for thermolysin, carbobenzoxyglycyl -Phenylalanine amide and bioplase were measured using casein as a substrate, and the results are shown in Table 1.
（結果）
表１ 経時的活性変化
注）単位：酵素溶液調製時の活性を１００とした場合の
相対活性
表１の結果から明らかな如く、好熱性菌由来の蛋白質分
解酵素であるサーモリシンは、常温性菌由来の蛋白質分
解酵素であるビオブラーゼに比べ、著しく酵素安定性に
優れていることがわかる。(Results) Table 1 Change in activity over time Note: Unit: Relative activity when the activity at the time of enzyme solution preparation is taken as 100 As is clear from the results in Table 1, thermolysin, a proteolytic enzyme derived from thermophilic bacteria, is active at room temperature. It can be seen that this enzyme has significantly superior enzyme stability compared to biobrase, which is a proteolytic enzyme derived from sexually transmitted bacteria.
（２）１．３−ブチレンゲリコール又はグリセリン溶液
中での好熱性菌由来の蛋白質分解酵素についての酵素安
定性の評価：
（評価方法）
表２に示す４種類の多価アルコールの３０重量％溶液又
は水にサーモリシン又はビオブラーゼを溶解し、４０℃
における３週間の活性変化を前記と同様にして測定し、
その結果を表２に示した。(2) Evaluation of enzyme stability of protease derived from thermophilic bacteria in 1.3-butylene gellicol or glycerin solution: (Evaluation method) 30% by weight of the four types of polyhydric alcohols shown in Table 2 Dissolve thermolysin or biobrase in solution or water and heat at 40°C.
Measure the activity change for 3 weeks in the same manner as above,
The results are shown in Table 2.
表２ 多価アルコールによる酵素活性変化性）Ｎｏ、６
以外はサーモリシンについての結果単位：酵素溶液調製
時の活性を１００とした場合の相対活性表２の結果から
明らかな如く、本発明に係わる１、３−ブチレングリコ
ール及びグリセリンには、サーモリシンに対し優れた酵
素安定化作用が認められるが、他の多価アルコールは何
も添加しない場合と比べて、むしろ酵素を失活させてい
る。またサーモリシンについて見られたグリセリンの効
果は、ビオブラーゼに対しては見られないことがわかる
。Table 2 Enzyme activity change due to polyhydric alcohol) No. 6
As is clear from the results in Table 2, 1,3-butylene glycol and glycerin according to the present invention have superior properties to thermolysin. However, other polyhydric alcohols actually deactivate the enzyme compared to when nothing is added. Furthermore, it can be seen that the effect of glycerin observed on thermolysin is not observed on biobrase.
以下、本発明について実施例を挙げて更に具体的に説明
するが、本発明はこれら実施例によって何ら限定される
ものではない。EXAMPLES Hereinafter, the present invention will be described in more detail with reference to Examples, but the present invention is not limited to these Examples in any way.
実施例１ 粉末洗顔料
（２）タルク
（３）結晶セルロース
（４）ポリアクリル酸
（５）ポリビニルピロリドン
（６）ラウリン酸カリウム
３１．９
２４．０
３．０
５．０
５．０
＠蚤にて調製したもの）
（８）香料 ０．１（
９）精製水（乾燥後揮散） 処方外（ｌＯ）
エタノール（乾燥後揮散） 処方外（製造法）
Ａ、 （１）〜（３）、（６）及び（７）を（９）及び
（１０）の適当量に混合溶解する。Example 1 Powdered facial cleanser (2) Talc (3) Crystalline cellulose (4) Polyacrylic acid (5) Polyvinylpyrrolidone (6) Potassium laurate 31.9 24.0 3.0 5.0 5.0 @Flea (8) Fragrance 0.1 (
9) Purified water (volatized after drying) Not prescribed (lO)
Ethanol (volatized after drying) Not prescribed (manufacturing method) A. Mix and dissolve (1) to (3), (6) and (7) in appropriate amounts of (9) and (10).
Ｂ、 （４）、（５）及び（８）を混合する。B. Mix (4), (5) and (8).
Ｃ，ＡをＢに噴霧造粒し、乾燥する。C, A is spray granulated onto B and dried.
（使用法）
本発明の粉末洗顔料は、使用時にその適当量を精製水ま
たは化粧水に溶解して用いることができる。(How to use) The powdered facial cleanser of the present invention can be used by dissolving an appropriate amount in purified water or lotion at the time of use.
実施例２ 洗顔フオーム
エーテルリン酸
（２）ラウリン酸ジェタノールアミド ２．０（
３）ヤシ油脂肪酸トリエタノ−ルア ４．０ミン
（６）水酸化カリウム ３．０（
７）グリセリン ８．０（８
）１．３−ブチレングリコール １６．０（９）
エチルパラベン ０．３（１０）
サーモリシン １．０（１１）香
料 ０，１（１２）精製
水 残量（製造法）
Ａ、 （１）〜（９）と（１２）の一部を８０℃にて加
熱混合溶解する。Example 2 Facial cleansing foam ether phosphoric acid (2) Lauric acid jetanolamide 2.0 (
3) Coconut oil fatty acid triethanol 4.0 (6) Potassium hydroxide 3.0 (
7) Glycerin 8.0 (8
)1.3-Butylene glycol 16.0(9)
Ethylparaben 0.3 (10)
Thermolysin 1.0 (11) Fragrance 0.1 (12) Purified water Remaining amount (manufacturing method) A. Mix and dissolve parts of (1) to (9) and (12) by heating at 80°C.
Ｂ、 （１０）及び（１１）と残りの（１２）をを混合
溶解する。B. Mix and dissolve (10) and (11) and the remaining (12).
Ｃ，Ａを冷却しながらこれにＢを加え、攪拌する。Add B to C and A while cooling and stir.
実施例３ バック剤
（２）グリセリン
（３）エタノール
１５．０
５．０
（５）エチルパラベン
０．２
（７）香料 ０．１（
８）精製水 残量Ａ、 （
１） 〜（２）及び（８）ノ一部を８０℃ニテ加熱膨潤
する。Example 3 Backing agent (2) Glycerin (3) Ethanol 15.0 5.0 (5) Ethylparaben 0.2 (7) Fragrance 0.1 (
8) Purified water remaining amount A, (
1) Parts of to (2) and (8) are heated and swollen at 80°C.
Ｂ、 （３）〜（５）及び（７）を混合溶解する。B. Mix and dissolve (3) to (5) and (7).
Ｃ，Ａを冷却しながら、これに（６）、残りの（８）２
ｉびＢを加え、攪拌する。While cooling C and A, add (6) to this and the remaining (8) 2
Add I and B and stir.
実施例４ クレンジングローション
（３）１．３−ブチレングリコール
（４）エタノール
（５）エチルパラベン
１６．０
５．０
０．２
（７）香料 ０．１（
８）精製水 残量（製造法
）
Ａ、 （１）、（２）、（４）、（５）及び（７）を混
合溶解する。Example 4 Cleansing lotion (3) 1,3-butylene glycol (4) Ethanol (5) Ethylparaben 16.0 5.0 0.2 (7) Fragrance 0.1 (
8) Purified water Remaining amount (manufacturing method) A. Mix and dissolve (1), (2), (4), (5) and (7).
Ｂ、 （３）、（６）及び（８）を混合溶解する。B. Mix and dissolve (3), (6) and (8).
Ｃ，ＡにＢを加え、攪拌する。Add B to C and A and stir.
本発明の化粧料は、皮膚表面の蛋白質汚れの除去効果に
優れ、かつ水に対する蛋白質分解酵素の安定性が良好で
あり、極めて有用なものである。The cosmetic composition of the present invention has an excellent effect of removing protein stains on the skin surface, and has good stability of proteolytic enzymes with respect to water, making it extremely useful.
以上that's all
Claims (1)
徴とする化粧料。 ２、好熱性菌由来の蛋白質分解酵素がサーモリシン、ア
クアリシン、サーミターゼ及びカルドリシンからなる群
より選ばれたものである請求項１記載の化粧料。 ３、次の成分（Ａ）及び（Ｂ） （Ａ）好熱性菌由来の蛋白質分解酵素 （Ｂ）１，３−ブチレングリコール及び／又はグリセリ
ン を含有することを特徴とする化粧料。[Scope of Claims] 1. A cosmetic containing a proteolytic enzyme derived from a thermophilic bacterium. 2. The cosmetic composition according to claim 1, wherein the proteolytic enzyme derived from thermophilic bacteria is selected from the group consisting of thermolysin, aquaricin, thermitase, and cardolysin. 3. A cosmetic comprising the following components (A) and (B) (A) a protease derived from a thermophilic bacterium (B) 1,3-butylene glycol and/or glycerin.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP9836490A JP2863946B2 (en) | 1990-04-13 | 1990-04-13 | Cosmetics |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP9836490A JP2863946B2 (en) | 1990-04-13 | 1990-04-13 | Cosmetics |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH03294211A true JPH03294211A (en) | 1991-12-25 |
| JP2863946B2 JP2863946B2 (en) | 1999-03-03 |
Family
ID=14217829
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP9836490A Expired - Fee Related JP2863946B2 (en) | 1990-04-13 | 1990-04-13 | Cosmetics |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP2863946B2 (en) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0940544A (en) * | 1995-07-25 | 1997-02-10 | L'oreal Sa | Stable composition containing enzyme |
| JPH0940543A (en) * | 1995-07-25 | 1997-02-10 | L'oreal Sa | Stable composition containing water-oversensitive make-up and/or dermatological activator |
| JP2002037726A (en) * | 2000-07-25 | 2002-02-06 | Kose Corp | Detergent composition |
| FR2843879A1 (en) * | 2002-08-27 | 2004-03-05 | Svr Lab | New cosmetic compositions with anti-oxidant properties comprises anti-radical agents, useful for skin protection and with anti-ageing effects |
| US7785584B2 (en) * | 2003-08-13 | 2010-08-31 | Healthpoint, Ltd. | Ointment wound spray |
-
1990
- 1990-04-13 JP JP9836490A patent/JP2863946B2/en not_active Expired - Fee Related
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0940544A (en) * | 1995-07-25 | 1997-02-10 | L'oreal Sa | Stable composition containing enzyme |
| JPH0940543A (en) * | 1995-07-25 | 1997-02-10 | L'oreal Sa | Stable composition containing water-oversensitive make-up and/or dermatological activator |
| JP2002037726A (en) * | 2000-07-25 | 2002-02-06 | Kose Corp | Detergent composition |
| FR2843879A1 (en) * | 2002-08-27 | 2004-03-05 | Svr Lab | New cosmetic compositions with anti-oxidant properties comprises anti-radical agents, useful for skin protection and with anti-ageing effects |
| US7785584B2 (en) * | 2003-08-13 | 2010-08-31 | Healthpoint, Ltd. | Ointment wound spray |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2863946B2 (en) | 1999-03-03 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5624906A (en) | Oral hygiene compositions comprising heteroatom containing alkyl aldonamide compounds | |
| US5030374A (en) | Clear neutral non-foaming rapidly-rinsable gel facial cleanser formulation | |
| JPH03244696A (en) | Use of type ii endoglycosidase | |
| TWI293983B (en) | ||
| JPH01283213A (en) | Toiletry product blended with enzyme | |
| JPH03294211A (en) | Cosmetic | |
| JP4397269B2 (en) | Proteolytic enzyme stabilizers, cosmetics and detergents | |
| CN108441350A (en) | A kind of kitchen cleaning agent and preparation method thereof based on bio-based compounds | |
| JPS63290808A (en) | Cosmetic | |
| JP4886105B2 (en) | Cleaning composition | |
| JPH10287540A (en) | Moisturizer | |
| JPH10251155A (en) | Protease inhibitor | |
| JPH1112126A (en) | Gel-like thermal massage material | |
| JPH05140597A (en) | Detergent for skin | |
| JPH01283206A (en) | Toiletry product blended with lysozyme chloride | |
| JP2002308725A (en) | Fever cosmetics | |
| KR20020045300A (en) | Powder Compositions for Washing Cosmetics | |
| JPS62260900A (en) | Detergent composition | |
| JP2002051770A (en) | Protease stabilizer and liquid cosmetic composition | |
| JP2001114624A (en) | Composition for cosmetic and cleaning and storing solution | |
| JPH10175815A (en) | Enzymic cosmetic | |
| KR101763239B1 (en) | A surfactantless composition for cleanign dentures | |
| JP2004307360A (en) | Detergent composition | |
| JP2006298814A (en) | Skin preparation for acne | |
| KR960004015B1 (en) | Cleaning agents for skin |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| LAPS | Cancellation because of no payment of annual fees |