JP2863946B2 - Cosmetics - Google Patents
CosmeticsInfo
- Publication number
- JP2863946B2 JP2863946B2 JP9836490A JP9836490A JP2863946B2 JP 2863946 B2 JP2863946 B2 JP 2863946B2 JP 9836490 A JP9836490 A JP 9836490A JP 9836490 A JP9836490 A JP 9836490A JP 2863946 B2 JP2863946 B2 JP 2863946B2
- Authority
- JP
- Japan
- Prior art keywords
- present
- glycerin
- water
- thermolysin
- weight
- 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.)
- Expired - Fee Related
Links
- 239000002537 cosmetic Substances 0.000 title claims description 16
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims description 22
- 108091005804 Peptidases Proteins 0.000 claims description 20
- PUPZLCDOIYMWBV-UHFFFAOYSA-N (+/-)-1,3-Butanediol Chemical compound CC(O)CCO PUPZLCDOIYMWBV-UHFFFAOYSA-N 0.000 claims description 15
- 102000035195 Peptidases Human genes 0.000 claims description 14
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 13
- 241000894006 Bacteria Species 0.000 claims description 11
- 235000011187 glycerol Nutrition 0.000 claims description 11
- 108090001109 Thermolysin Proteins 0.000 claims description 10
- -1 aqualysin Proteins 0.000 claims description 8
- 108010031354 thermitase Proteins 0.000 claims description 4
- 239000004365 Protease Substances 0.000 description 11
- 230000000694 effects Effects 0.000 description 7
- 229940058015 1,3-butylene glycol Drugs 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 6
- 235000019437 butane-1,3-diol Nutrition 0.000 description 6
- 229940088598 enzyme Drugs 0.000 description 6
- 239000000203 mixture Substances 0.000 description 6
- 235000019419 proteases Nutrition 0.000 description 6
- 235000018102 proteins Nutrition 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 5
- 210000003491 skin Anatomy 0.000 description 5
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 4
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 4
- 241000589500 Thermus aquaticus Species 0.000 description 4
- 239000002552 dosage form Substances 0.000 description 4
- 238000011156 evaluation Methods 0.000 description 4
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 3
- 239000003240 coconut oil Substances 0.000 description 3
- 235000014113 dietary fatty acids Nutrition 0.000 description 3
- PXEDJBXQKAGXNJ-QTNFYWBSSA-L disodium L-glutamate Chemical compound [Na+].[Na+].[O-]C(=O)[C@@H](N)CCC([O-])=O PXEDJBXQKAGXNJ-QTNFYWBSSA-L 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
- 229930195729 fatty acid Natural products 0.000 description 3
- 239000000194 fatty acid Substances 0.000 description 3
- 150000004665 fatty acids Chemical class 0.000 description 3
- 239000008213 purified water Substances 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 150000005846 sugar alcohols Polymers 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- NWGKJDSIEKMTRX-AAZCQSIUSA-N Sorbitan monooleate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](O)[C@H]1OC[C@H](O)[C@H]1O NWGKJDSIEKMTRX-AAZCQSIUSA-N 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 235000019864 coconut oil Nutrition 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 230000003779 hair growth Effects 0.000 description 2
- 239000006210 lotion Substances 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000002304 perfume Substances 0.000 description 2
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 108010004032 Bromelains Proteins 0.000 description 1
- AOMUHOFOVNGZAN-UHFFFAOYSA-N N,N-bis(2-hydroxyethyl)dodecanamide Chemical compound CCCCCCCCCCCC(=O)N(CCO)CCO AOMUHOFOVNGZAN-UHFFFAOYSA-N 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 241000203770 Thermoactinomyces vulgaris Species 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 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
- 235000019835 bromelain Nutrition 0.000 description 1
- 108010043507 carbobenzoxyglycylphenylalanine 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
- 238000013329 compounding Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000008406 cosmetic ingredient Substances 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- SZXQTJUDPRGNJN-UHFFFAOYSA-N dipropylene glycol Chemical compound OCCCOCCCO SZXQTJUDPRGNJN-UHFFFAOYSA-N 0.000 description 1
- 125000003438 dodecyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000001815 facial effect Effects 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 229940031957 lauric acid diethanolamide Drugs 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 235000013923 monosodium glutamate Nutrition 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000003755 preservative agent 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
- 229940073490 sodium glutamate Drugs 0.000 description 1
- 229950004959 sorbitan oleate Drugs 0.000 description 1
- 230000000087 stabilizing effect Effects 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
- 229920003169 water-soluble polymer Polymers 0.000 description 1
Landscapes
- Cosmetics (AREA)
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。Description: TECHNICAL FIELD The present invention relates to cosmetics, and more particularly to cosmetics, which contain a protease that is derived from a thermophilic bacterium, have an excellent effect of removing protein stains on the surface of skin, and contain water. The present invention relates to cosmetics having good stability against
〔従来の技術〕 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。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。[Prior Art] Dirt on the skin surface is composed of various substances such as proteins and lipids. Among them, proteins are derived from dead skin cells and secretions of sweat glands, which have become unnecessary due to aging. These stains cause a decrease in the normal physiological function and metabolism of the skin. For this reason, attempts have conventionally 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、ブロメライン、ビオプラーゼ等は安定
性が悪く、経済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 proteases,
For example, papain, bromelain, bioprase, and the like have the disadvantage of poor stability and economical loss of enzymatic activity, especially when formulated in water-containing cosmetic formulations. It has been known.
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 they have not been sufficiently satisfactory.
上記実情に鑑み、本発明者らは鋭意研究を重ねた結
果、特定の好熱性菌由来の蛋白質分解酵素と、1,3−ブ
チレングリコール及び／又はグリセリンとを特定量配合
すれば、水を含有する剤型であっても安定性に優れた化
粧料が得られることを見出し、本発明を完成するに至っ
た。In view of the above circumstances, the present inventors have conducted intensive studies, and as a result, if a specific amount of a proteolytic enzyme derived from a specific thermophilic bacterium and 1,3-butylene glycol and / or glycerin are mixed in a specific amount, water is contained. The present inventors have found that a cosmetic composition having excellent stability can be obtained even in a dosage form of the present invention, and have completed the present invention.
すなわち、本発明は次の成分（Ａ）及び（Ｂ） （Ａ）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る好熱性菌由来の蛋
白質分解酵素 0.05〜５重量％ （Ｂ）1,3−ブチレングリコール及び／又はグリセリン ５〜30重量％ を含有することを特徴とする含水化粧料を提供するもの
である。That is, the present invention relates to the following components (A) and (B): (A) 0.05 to 5% by weight of a thermolytic bacterium-derived proteolytic enzyme selected from the group consisting of thermolysin, aqualysin, thermitase and cardrisin; The present invention provides a water-containing cosmetic comprising 5 to 30% by weight of butylene glycol and / or glycerin.
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、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 サーモプロテオリィティカス（Bacill
us thermoproteolyticus）、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 aquaticus
YT−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（Thermoactinomyces vulgaris）、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−351（Thermus aquaticus strain T351）が
挙げられる。As the proteolytic enzyme derived from a thermophilic bacterium used in the present invention, thermolysin, aqualysin, thermitase or cardrisin is preferable. The thermophilic strains that are the origins of these proteases include Bacillus thermoproteoliticus for thermolysin.
us thermoproteolyticus) and aqualysin for Thermus aquaticus YT-1 (Thermus aquaticus)
YT-1) and thermistase include Thermoactinomyces vulgaris, and caldricin includes Thermus aquaticus strain T351.
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, as the proteolytic enzyme, a crude enzyme obtained by culturing the above strain in accordance with a conventional method or a purified product thereof is used, but commercially available proteolytic enzymes may 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、0.05〜５重量％の範囲であることが
好ましい。In the cosmetic of the present invention, such a protease may be used alone or in combination of two or more, and the amount thereof is preferably in the range of 0.05 to 5% by weight of the total cosmetic.
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
方向を配合する。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, for the purpose of further improving the stability of the protease in a dosage form containing water.
Mix one or the direction of 3-butylene glycol and glycerin. It is preferable that the compounding amount of 1,3-butylene glycol and glycerin is in the range of 5 to 30% by weight in the total cosmetics.
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、皮膚洗浄剤、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る。Incidentally, the cosmetic of the present invention, if necessary, in addition to the essential components as long as the effect is not impaired, water, a surfactant,
Oils, powders, water-soluble polymers, lower alcohols, cosmetic ingredients, preservatives, antioxidants, ultraviolet absorbers and the like can be added. Examples of the dosage form of the cosmetic of the present invention include dosage forms that do not impair the action of proteolytic enzymes, such as skin cleansing agents, lotions, creams, emulsions, foundations, packs, and hair growth and hair growth agents.
（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
サーモリシン（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して知られているビオプ
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−Ｌ−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 Proteolytic Enzymes Derived from Thermophilic Bacteria: (Evaluation Method) Thermolysin (produced by Sigma, the same applies hereinafter), which is a protease degrading from a thermophilic bacterium according to the present invention, and conventionally at room temperature Changes in the activity of bioprase (produced by Nagase Seikagaku Co., Ltd., the same applies hereinafter) known as a proteolytic enzyme derived from bacterium in water at 40 ° C. over time, and carbobenzoxyglycyl-L- Phenylalanine amide was measured using casein as a substrate for bioprase, and the results are shown in Table 1.
（結果） 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プラーゼに比べ、著しく酵素安定性
に優れていることがわかる。(result) As is clear from the results shown in Table 1, it is found that thermolysin, which is a protease derived from a thermophilic bacterium, has remarkably superior enzyme stability as compared with bioprolase, which is a protease that is derived from a normal temperature bacterium.
（２）1,3−ブチレング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プラーゼを溶解し、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 proteases derived from thermophilic bacteria in 1,3-butylene glycol or glycerin solution: (Evaluation method) 30% by weight solution of four kinds of polyhydric alcohols shown in Table 2 Alternatively, thermolysin or bioprase was dissolved in water, and the activity change at 40 ° C. for 3 weeks was measured in the same manner as described above. The results are shown in Table 2.
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又はグリセリンには、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、ビオプラーゼに対しては見られな
いことがわかる。 As is clear from the results in Table 2, the 1,3--
Although butylene glycol or glycerin has an excellent enzyme stabilizing effect on thermolysin, the enzyme is inactivated rather than when no other polyhydric alcohol is added. In addition, it can be seen that the effect of glycerin observed for thermolysin is not observed for bioprase.
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。Hereinafter, the present invention will be described more specifically with reference to examples, but the present invention is not limited to these examples.
実施例１ 洗顔フォーム （組成） 重量％ （１）ポリオキシエチレン（２）ラウリル 18.0 エーテルリン酸 （２）ラウリン酸ジエタノールアミド 2.4 （３）ヤシ油脂肪酸トリエタノールア 4.0 ミン （４）Ｎ−ヤシ油脂肪酸アシル−Ｌ− 4.0 グルタミン酸ナトリウム （５）ジステアリン酸エチレングリコ 2.0 ール （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 1 Facial wash foam (composition)% by weight (1) Polyoxyethylene (2) lauryl 18.0 ether phosphoric acid (2) lauric acid diethanolamide 2.4 (3) coconut oil fatty acid triethanolamine 4.0 min (4) N-coconut oil Fatty acid acyl-L-4.0 sodium glutamate (5) ethylene glycol 2.0 distearate (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) Perfume 0.1 (12) Remaining amount of purified water (Production method) A. A part of (1) to (9) and (12) is heated and mixed at 80 ° C to dissolve.
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) with the remaining (12).
C.Aを冷却しながらこれにＢを加え、撹拌する。C. Add B to this while cooling A and stir.
実施例２ パック剤 （組成） 重量％ （１）ポリビニルアルコール 20.0 （２）グリセリン 15.0 （３）エタノール 5.0 （４）ポリオキシエチレン（15）オレイ 1.0 ルエーテル （５）エチルパラベン 0.2 （６）サーミターゼ 1.0 （Thermoactinomyces vulgaris の培養にて調製したもの） （７）香料 0.1 （８）精製水 残量 A.（１）〜（２）及び（８）の一部を80℃にて加熱膨潤
する。Example 2 Packing agent (composition)% by weight (1) Polyvinyl alcohol 20.0 (2) Glycerin 15.0 (3) Ethanol 5.0 (4) Polyoxyethylene (15) Oley 1.0 ether (5) Ethyl paraben 0.2 (6) Thermitase 1.0 ( (7) Perfume 0.1 (8) Purified water Remaining A. A portion of (1)-(2) and (8) is 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）及び
Ｂを加え、撹拌する。While cooling the CA, add (6), the remaining (8) and B, and stir.
実施例３ クレンジングローション （組成） 重量％ （１）ポリオキシエチレン（20）モノオ 0.5 レイン酸ソルビタン （２）ポリオキシエチレン（２）ヤシ油 0.5 脂肪酸モノエタノールアミド （３）1,3−ブチレングリコール 16.0 （４）エタノール 5.0 （５）エチルパラベン 0.2 （６）カルドリシン 1.0 （Thermus aquaticus strain Ｔ−351の培養にて調製したもの） （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 3 Cleansing lotion (composition)% by weight (1) polyoxyethylene (20) mono-0.5 sorbitan oleate (2) polyoxyethylene (2) coconut oil 0.5 fatty acid monoethanolamide (3) 1,3-butylene glycol 16.0 (4) Ethanol 5.0 (5) Ethyl paraben 0.2 (6) Cardrisin 1.0 (prepared by culturing Thermus aquaticus strain T-351) (7) Fragrance 0.1 (8) Remaining amount of purified water (Production method) 1), (2), (4), (5) and (7) are mixed and dissolved.
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、撹拌する。C. Add B to 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。INDUSTRIAL APPLICABILITY The cosmetic of the present invention has an excellent effect of removing protein stains on the skin surface, and has excellent stability of proteolytic enzymes in water, and is extremely useful.
───────────────────────────────────────────────────── フロントページの続き (56)参考文献 特開 平１−283213（ＪＰ，Ａ) 特開 平１−269492（ＪＰ，Ａ) 特開 昭63−267298（ＪＰ，Ａ) 特開 昭62−238214（ＪＰ，Ａ) 特公 昭39−4900（ＪＰ，Ｂ１) (58)調査した分野(Int.Cl.6，ＤＢ名) A61K 7/00 - 7/50──────────────────────────────────────────────────続 き Continuation of the front page (56) References JP-A-1-283213 (JP, A) JP-A-1-269492 (JP, A) JP-A-63-267298 (JP, A) JP-A-62-1987 238214 (JP, A) JP 39-4900 (JP, B1) (58) Fields investigated (Int. Cl. 6 , DB name) A61K 7/00-7/50
Claims (1)
カルドリシンからなる群より選ばれる好熱性菌由来の蛋
白質分解酵素 0.05〜５重量％ （Ｂ）1,3−ブチレングリコール及び／又はグリセリン ５〜30重量％ を含有することを特徴とする含水化粧料。1. The following components (A) and (B): (A) 0.05 to 5% by weight of a thermolytic bacterium-derived proteolytic enzyme selected from the group consisting of thermolysin, aqualysin, thermitase and cardrisin; -A water-containing cosmetic comprising 5 to 30% by weight of 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 JPH03294211A (en) | 1991-12-25 |
| JP2863946B2 true 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) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2737116B1 (en) * | 1995-07-25 | 1997-08-22 | Oreal | STABLE COMPOSITION CONTAINING A WATER SENSITIVE COSMETIC AND / OR DERMATOLOGICAL ACTIVE |
| FR2737115B1 (en) * | 1995-07-25 | 1997-08-22 | Oreal | STABLE COMPOSITION CONTAINING AN ENZYME |
| JP4886105B2 (en) * | 2000-07-25 | 2012-02-29 | 株式会社コーセー | Cleaning composition |
| FR2843879B1 (en) * | 2002-08-27 | 2005-12-30 | Svr Lab | NOVEL COSMETIC COMPOSITIONS WITH AN ANTI-OXIDIZING VIEW |
| 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
Also Published As
| Publication number | Publication date |
|---|---|
| JPH03294211A (en) | 1991-12-25 |
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