JP4397269B2 - Proteolytic enzyme stabilizers, cosmetics and detergents - Google Patents
Proteolytic enzyme stabilizers, cosmetics and detergents Download PDFInfo
- Publication number
- JP4397269B2 JP4397269B2 JP2004129848A JP2004129848A JP4397269B2 JP 4397269 B2 JP4397269 B2 JP 4397269B2 JP 2004129848 A JP2004129848 A JP 2004129848A JP 2004129848 A JP2004129848 A JP 2004129848A JP 4397269 B2 JP4397269 B2 JP 4397269B2
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- JP
- Japan
- Prior art keywords
- parts
- mass
- proteolytic enzyme
- weight
- enzyme
- 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 - Lifetime
Links
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- 239000003381 stabilizer Substances 0.000 title claims description 29
- 239000003599 detergent Substances 0.000 title claims description 24
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- WTFUTSCZYYCBAY-SXBRIOAWSA-N 6-[(E)-C-[[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperazin-1-yl]methyl]-N-hydroxycarbonimidoyl]-3H-1,3-benzoxazol-2-one Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)N1CCN(CC1)C/C(=N/O)/C1=CC2=C(NC(O2)=O)C=C1 WTFUTSCZYYCBAY-SXBRIOAWSA-N 0.000 description 1
- DFGKGUXTPFWHIX-UHFFFAOYSA-N 6-[2-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperazin-1-yl]acetyl]-3H-1,3-benzoxazol-2-one Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)N1CCN(CC1)CC(=O)C1=CC2=C(NC(O2)=O)C=C1 DFGKGUXTPFWHIX-UHFFFAOYSA-N 0.000 description 1
- DEXFNLNNUZKHNO-UHFFFAOYSA-N 6-[3-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperidin-1-yl]-3-oxopropyl]-3H-1,3-benzoxazol-2-one Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C1CCN(CC1)C(CCC1=CC2=C(NC(O2)=O)C=C1)=O DEXFNLNNUZKHNO-UHFFFAOYSA-N 0.000 description 1
- LLQHSBBZNDXTIV-UHFFFAOYSA-N 6-[5-[[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperazin-1-yl]methyl]-4,5-dihydro-1,2-oxazol-3-yl]-3H-1,3-benzoxazol-2-one Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)N1CCN(CC1)CC1CC(=NO1)C1=CC2=C(NC(O2)=O)C=C1 LLQHSBBZNDXTIV-UHFFFAOYSA-N 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 239000005995 Aluminium silicate Substances 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 235000021357 Behenic acid Nutrition 0.000 description 1
- 108010004032 Bromelains Proteins 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 229920002261 Corn starch Polymers 0.000 description 1
- ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- FPVVYTCTZKCSOJ-UHFFFAOYSA-N Ethylene glycol distearate Chemical compound CCCCCCCCCCCCCCCCCC(=O)OCCOC(=O)CCCCCCCCCCCCCCCCC FPVVYTCTZKCSOJ-UHFFFAOYSA-N 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 239000004354 Hydroxyethyl cellulose Substances 0.000 description 1
- 229920000663 Hydroxyethyl cellulose Polymers 0.000 description 1
- 102000011782 Keratins Human genes 0.000 description 1
- 108010076876 Keratins Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 229920002125 Sokalan® Polymers 0.000 description 1
- GWEVSGVZZGPLCZ-UHFFFAOYSA-N Titan oxide Chemical compound O=[Ti]=O GWEVSGVZZGPLCZ-UHFFFAOYSA-N 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 230000006750 UV protection Effects 0.000 description 1
- FWFKWYODLSFYLE-UHFFFAOYSA-J [Na+].[Na+].[Na+].[Na+].CCO.[O-]P(=O)OP([O-])=O.[O-]P(=O)OP([O-])=O Chemical compound [Na+].[Na+].[Na+].[Na+].CCO.[O-]P(=O)OP([O-])=O.[O-]P(=O)OP([O-])=O FWFKWYODLSFYLE-UHFFFAOYSA-J 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 229920000800 acrylic rubber Polymers 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000005215 alkyl ethers Chemical class 0.000 description 1
- BJEPYKJPYRNKOW-UHFFFAOYSA-N alpha-hydroxysuccinic acid Natural products OC(=O)C(O)CC(O)=O BJEPYKJPYRNKOW-UHFFFAOYSA-N 0.000 description 1
- 235000012211 aluminium silicate Nutrition 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- 239000002216 antistatic agent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 238000003287 bathing Methods 0.000 description 1
- 229940116226 behenic acid Drugs 0.000 description 1
- 239000007844 bleaching agent Substances 0.000 description 1
- 235000019835 bromelain Nutrition 0.000 description 1
- 235000019437 butane-1,3-diol Nutrition 0.000 description 1
- 235000010354 butylated hydroxytoluene Nutrition 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 239000008120 corn starch Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 229940105990 diglycerin Drugs 0.000 description 1
- GPLRAVKSCUXZTP-UHFFFAOYSA-N diglycerol Chemical compound OCC(O)COCC(O)CO GPLRAVKSCUXZTP-UHFFFAOYSA-N 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- SMVRDGHCVNAOIN-UHFFFAOYSA-L disodium;1-dodecoxydodecane;sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O.CCCCCCCCCCCCOCCCCCCCCCCCC SMVRDGHCVNAOIN-UHFFFAOYSA-L 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 235000019197 fats Nutrition 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000012812 general test Methods 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- UHUSDOQQWJGJQS-UHFFFAOYSA-N glycerol 1,2-dioctadecanoate Chemical compound CCCCCCCCCCCCCCCCCC(=O)OCC(CO)OC(=O)CCCCCCCCCCCCCCCCC UHUSDOQQWJGJQS-UHFFFAOYSA-N 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 235000019447 hydroxyethyl cellulose Nutrition 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- NLYAJNPCOHFWQQ-UHFFFAOYSA-N kaolin Chemical compound O.O.O=[Al]O[Si](=O)O[Si](=O)O[Al]=O NLYAJNPCOHFWQQ-UHFFFAOYSA-N 0.000 description 1
- 239000001630 malic acid Substances 0.000 description 1
- 235000011090 malic acid Nutrition 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 238000000034 method Methods 0.000 description 1
- 235000014593 oils and fats Nutrition 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000003002 pH adjusting agent Substances 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920001451 polypropylene glycol Polymers 0.000 description 1
- 229920001296 polysiloxane Polymers 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- PYJBVGYZXWPIKK-UHFFFAOYSA-M potassium;tetradecanoate Chemical compound [K+].CCCCCCCCCCCCCC([O-])=O PYJBVGYZXWPIKK-UHFFFAOYSA-M 0.000 description 1
- 238000011533 pre-incubation Methods 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 239000011814 protection agent Substances 0.000 description 1
- 125000001453 quaternary ammonium group Chemical group 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- RMAQACBXLXPBSY-UHFFFAOYSA-N silicic acid Chemical compound O[Si](O)(O)O RMAQACBXLXPBSY-UHFFFAOYSA-N 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 235000012239 silicon dioxide Nutrition 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- RUTSRVMUIGMTHJ-UHFFFAOYSA-M sodium;tetradec-1-ene-1-sulfonate Chemical compound [Na+].CCCCCCCCCCCCC=CS([O-])(=O)=O RUTSRVMUIGMTHJ-UHFFFAOYSA-M 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- TUNFSRHWOTWDNC-HKGQFRNVSA-N tetradecanoic acid Chemical compound CCCCCCCCCCCCC[14C](O)=O TUNFSRHWOTWDNC-HKGQFRNVSA-N 0.000 description 1
- OGIDPMRJRNCKJF-UHFFFAOYSA-N titanium oxide Inorganic materials [Ti]=O OGIDPMRJRNCKJF-UHFFFAOYSA-N 0.000 description 1
- ZIBGPFATKBEMQZ-UHFFFAOYSA-N triethylene glycol Chemical compound OCCOCCOCCO ZIBGPFATKBEMQZ-UHFFFAOYSA-N 0.000 description 1
- 229920001285 xanthan gum Polymers 0.000 description 1
- 239000000230 xanthan gum Substances 0.000 description 1
- 235000010493 xanthan gum Nutrition 0.000 description 1
- 229940082509 xanthan gum Drugs 0.000 description 1
- 239000004711 α-olefin Substances 0.000 description 1
Landscapes
- Cosmetics (AREA)
- Detergent Compositions (AREA)
- Enzymes And Modification Thereof (AREA)
Description
本発明は、蛋白分解酵素を含む化粧料又は洗浄剤等に配合して、蛋白分解酵素の活性低下を抑制し、安定に保持しうる蛋白分解酵素安定化剤、該安定化剤を含む液状、クリーム状、ペースト状、顆粒状、錠剤又は粉体等の剤型の化粧料及び洗浄剤に関する。 The present invention is a proteolytic enzyme stabilizer that is blended in a cosmetic or detergent containing a proteolytic enzyme, suppresses a decrease in the activity of the proteolytic enzyme, and can be stably maintained, a liquid containing the stabilizer, The present invention relates to cosmetics and detergents in the form of creams, pastes, granules, tablets or powders.
近年、蛋白にかかる汚れ等を有効に取除くために蛋白分解酵素を配合した化粧料や洗浄剤が多く提案されている。しかし、酵素は、化粧料等に配合された他の成分との接触、酸化、若しくは大気中の水分の影響等により失活し易く、酵素配合により期待する十分な効果が期待できない場合が生じる。
そこで、化粧料等に配合した酵素、特に蛋白分解酵素が保存中に失活せず、使用時に酵素活性を充分に発揮しうるように種々の蛋白分解酵素安定化剤が提案されている。例えば、特許文献１には、安定化剤としてＮ−アシルアミノ酸を用いた洗剤が、特許文献２には、安定化剤として４級アンモニウム基と水酸基とを含む水溶性高分子を用いたコンタクトレンズ用保存液が、特許文献３には、安定化剤としてコラーゲン、アルブミンを配合することが、特許文献４には、安定化剤としてアミドアミン型界面活性剤を配合することが、特許文献５には、安定剤としてケラチン、卵白ペプタイドを配合することがそれぞれ提案されている。
ところで、最近、牛海綿状脳症(ＢＳＥ)等をはじめとする動物にかかる感染性症が問題となっており、動物起源の安定化剤等が敬遠されるようになっている。また、従来提案されている蛋白分解酵素安定化剤の中には、化粧料等として用いた場合に、皮膚に対する使用感が良くないものや、基剤臭が生じるものもあり、これらの問題を改善した新たな安定化剤の開発が望まれている。
Therefore, various proteolytic enzyme stabilizers have been proposed so that enzymes blended in cosmetics and the like, particularly proteolytic enzymes, are not inactivated during storage and can fully exhibit enzyme activity when used. For example, Patent Document 1 discloses a detergent using an N-acylamino acid as a stabilizer, and Patent Document 2 discloses a contact lens using a water-soluble polymer containing a quaternary ammonium group and a hydroxyl group as a stabilizer. Patent Document 3 contains collagen and albumin as stabilizers, Patent Document 4 contains amidoamine surfactants as stabilizers, Patent Document 5 In addition, it has been proposed that keratin and egg white peptide are added as stabilizers.
Recently, infectious diseases related to animals such as bovine spongiform encephalopathy (BSE) have become a problem, and stabilizers derived from animals have been avoided. In addition, some of the proteolytic enzyme stabilizers that have been proposed in the past have a poor feeling on the skin when used as cosmetics, and those that produce a base odor. Development of new and improved stabilizers is desired.
従って、本発明の目的は、蛋白分解酵素を含む化粧料や洗浄剤等に配合した場合に、該酵素の活性低下を有効に抑制することができ、更に化粧料に配合した場合に皮膚に対する使用感が悪化し難い蛋白分解酵素安定化剤を提供することにある。
本発明の別の目的は、配合されている蛋白分解酵素の活性低下が抑制され、蛋白の汚れ等の除去作用が十分期待できる使用感に優れた化粧料や、洗浄剤を提供することにある。
Accordingly, an object of the present invention is to effectively suppress the decrease in the activity of the enzyme when formulated in a cosmetic or detergent containing a proteolytic enzyme, and further to use on the skin when formulated in a cosmetic. An object of the present invention is to provide a proteolytic enzyme stabilizer that does not deteriorate feeling.
Another object of the present invention is to provide a cosmetic and a cleaning agent excellent in the feeling of use, in which the decrease in the activity of the incorporated proteolytic enzyme is suppressed and the removal action of protein stains and the like can be sufficiently expected. .
本発明によれば、イソマルトオリゴ糖、ラフィノース、フルクトース、グリシルグリシン、L-アルギニン-L-グルタミン酸及びイガイグリコーゲンからなる群より選択される１種又は２種以上を有効成分として含む蛋白分解酵素安定化剤が提供される。
また本発明によれば、蛋白分解酵素と、前記蛋白分解酵素安定化剤と、化粧料成分とを含むことを特徴とする化粧料が提供される。
更に本発明によれば、蛋白分解酵素と、前記蛋白分解酵素安定化剤と、洗浄剤成分とを含むことを特徴とする洗浄剤が提供される。
According to the present invention, a proteolytic enzyme stable comprising, as an active ingredient, one or more selected from the group consisting of isomaltoligosaccharide, raffinose, fructose, glycylglycine, L-arginine-L-glutamic acid and mussel glycogen An agent is provided.
Moreover, according to this invention, the cosmetics characterized by including a protease, the said protease inhibitor, and a cosmetic ingredient are provided.
Furthermore, according to the present invention, there is provided a cleaning agent comprising a proteolytic enzyme, the proteolytic enzyme stabilizer, and a cleaning agent component.
本発明の蛋白分解酵素安定化剤は、特定のジペプチドを有効成分として含むので、化粧料や洗浄剤等に配合した場合に、蛋白分解酵素の活性低下を有効に抑制することができ、更には化粧料に配合した場合に皮膚に対する使用感が悪化し難い。従って、蛋白分解酵素を配合した液状、クリーム状、ペースト状、顆粒状、錠剤又は粉体等の剤型の化粧料や洗浄剤等に利用することができる。
本発明の化粧料及び洗浄剤は、前記本発明の蛋白分解酵素安定化剤を含むので、液状、クリーム状、ペースト状、顆粒状、錠剤又は粉体等の剤型の化粧料や洗浄剤において、配
合された蛋白分解酵素を有効に安定化させることができ、保存した際等においても蛋白分
解酵素の効果を有効に得ることができる。
Proteolytic enzyme stabilizer of the present invention contain a certain di-peptide as an active ingredient, when incorporated into cosmetics and detergents, etc., it is possible to effectively suppress the reduction in activity of proteolytic enzymes, Furthermore, when blended in cosmetics, the feeling on the skin is unlikely to deteriorate. Therefore, it can be used for liquid-type, cream-like, paste-like, granule-like, tablet or powder-type cosmetics and detergents containing proteolytic enzymes.
Since the cosmetics and cleaning agents of the present invention contain the protease inhibitor of the present invention, the cosmetics and cleaning agents in the form of liquids, creams, pastes, granules, tablets or powders, etc. The blended proteolytic enzyme can be effectively stabilized, and the effect of the proteolytic enzyme can be effectively obtained even when stored.
以下本発明を更に詳細に説明する。
本発明の蛋白分解酵素安定化剤は、有効成分として、グリシルグリシン及び／又はL-アルギニン-L-グルタミン酸を含む。
The present invention will be described in detail below.
Proteolytic enzyme stabilizer of the present invention, as an active ingredient, including grayed Rishirugurishin and / or L- arginine -L- glutamic acid.
グリシルグリシンはグリシン２分子がペプチド結合したジペプチドであり、L-アルギニン-L-グルタミン酸はアルギニンとグルタミン酸が結合したジペプチドである。 Grayed Rishirugurishin is a dipeptide glycine 2 molecule is a peptide bond, the L- arginine -L- glutamic dipeptide arginine and glutamic acid were combined.
本発明の蛋白分解酵素安定化剤は、上記必須の有効成分の他に、その作用に影響を及ぼさない範囲において他の成分を含んでいても良く、また、多価アルコール等の他の安定化剤を含んでいても良い。
多価アルコールとしては、例えば、エチレングリコール、ジエチレングリコール、トリエチレングリコール、ポリエチレングリコール、プロピレングリコール、ジプロピレングリコール、ポリプロピレングリコール、グリセリン、ジグリセリン、ポリグリセリン、３−メチル−１，３−ブタンジオール、１，３−ブチレングリコール等が挙げられる。多価アルコールを配合する場合の配合割合は、前記必須の有効成分の合計量１００質量部に対して、１〜７０質量部が好ましい。
The proteolytic enzyme stabilizer of the present invention may contain other components in addition to the essential active ingredients as long as they do not affect the action thereof, and other stabilizing agents such as polyhydric alcohols. An agent may be included.
Examples of the polyhydric alcohol include ethylene glycol, diethylene glycol, triethylene glycol, polyethylene glycol, propylene glycol, dipropylene glycol, polypropylene glycol, glycerin, diglycerin, polyglycerin, 3-methyl-1,3-butanediol, 1 , 3-butylene glycol and the like. The blending ratio when blending the polyhydric alcohol is preferably 1 to 70 parts by mass with respect to 100 parts by mass of the total amount of the essential active ingredients.
本発明の蛋白分解酵素安定化剤において、安定化しうる酵素は、蛋白分解酵素であれば特に限定されないが、例えば、枯草菌等の微生物起源の蛋白分解酵素、パンクレアチン等の動物起源の蛋白分解酵素、パパイン、ブロメライン等の植物起源の蛋白分解酵素等が挙げられる。 In the proteolytic enzyme stabilizer of the present invention, the enzyme that can be stabilized is not particularly limited as long as it is a proteolytic enzyme. Examples include proteolytic enzymes of plant origin such as enzymes, papain and bromelain.
本発明の化粧料は、前記蛋白分解酵素と、前記蛋白分解酵素安定化剤と、化粧料成分とを含み、例えば、洗顔料、ボディソープ、シャンプー、パック又は入浴剤等とすることができる。その剤型は特に限定されず、液状、クリーム状、ペースト状又は粉体等にすることができ、このような剤型の化粧料は、前記蛋白分解酵素安定化剤を配合する以外は、公知の蛋白分解酵素を配合した各化粧料の製造法等に準じて調製することができる。
前記化粧料成分は、その化粧料の種類に応じて公知の成分等から適宜選択して配合することができ、各成分の配合割合もその目的等に応じて適宜選択することができる。
The cosmetic of the present invention contains the proteolytic enzyme, the proteolytic enzyme stabilizer, and a cosmetic ingredient, and can be, for example, a facial cleanser, body soap, shampoo, pack, or bath agent. The dosage form is not particularly limited and can be liquid, creamy, pasty or powdery. Cosmetics of such dosage form are publicly known except that the proteolytic enzyme stabilizer is blended. It can be prepared according to the production method of each cosmetic containing the proteolytic enzyme.
The cosmetic component can be appropriately selected and blended from known components according to the type of the cosmetic, and the blending ratio of each component can also be appropriately selected according to the purpose and the like.
化粧料成分としては、例えば、炭酸水素ナトリウム等の無機塩、クエン酸、リンゴ酸等の有機酸、酸化チタン、酸化鉄、カオリン、タルク等の粉末、アニオン界面活性剤、ノニオン界面活性剤、両性界面活性剤、カチオン界面活性剤、防腐剤、保湿剤、植物抽出物、水溶性高分子、シリコン、酸化防止剤、油脂類、アルコール、紫外線防止剤、キレート剤、ｐＨ調整剤、色素、香料、精製水又はこれらの２種以上の混合物等が挙げられる。 Cosmetic ingredients include, for example, inorganic salts such as sodium bicarbonate, organic acids such as citric acid and malic acid, powders such as titanium oxide, iron oxide, kaolin and talc, anionic surfactants, nonionic surfactants, amphoteric Surfactant, Cationic surfactant, Preservative, Moisturizer, Plant extract, Water-soluble polymer, Silicone, Antioxidant, Oils and fats, Alcohol, UV protection agent, Chelating agent, pH adjuster, Dye, Fragrance, Examples include purified water or a mixture of two or more of these.
本発明の化粧料に配合する蛋白分解酵素の配合割合は、化粧料の種類や目的に応じてその酵素の力価等に応じて適宜決定することができるが、通常、化粧料全量に対して０．００１〜２質量％で配合することができる。 The proportion of the proteolytic enzyme to be blended in the cosmetic of the present invention can be determined as appropriate according to the potency of the enzyme depending on the type and purpose of the cosmetic, but is generally based on the total amount of the cosmetic. It can mix | blend by 0.001-2 mass%.
本発明の化粧料において、前記蛋白分解酵素安定化剤の配合割合は、後述する実施例から判るように濃度が高くなるほど安定化作用が高くなるので、化粧料の種類、蛋白分解酵素の配合量やその力価、化粧料の使用感等を勘案して適宜決定することができる。 In the cosmetics of the present invention, the blending ratio of the proteolytic enzyme stabilizer increases the stabilizing action as the concentration increases, as will be understood from the examples described later. It can be appropriately determined in consideration of the potency, its potency, the feeling of use of cosmetics, and the like.
本発明の洗浄剤は、前記蛋白分解酵素と、前記蛋白分解酵素安定化剤と、洗浄剤成分とを含む。その剤型は特に限定されず、液状、クリーム状、ペースト状又は粉体等にすることができ、このような剤型の洗浄剤は、前記蛋白分解酵素安定化剤を配合する以外は、公知の蛋白分解酵素を配合した洗浄剤の製造法等に準じて調製することができる。
前記洗浄剤成分は、その洗浄剤の種類に応じて公知の成分等から適宜選択して配合することができ、各成分の配合割合もその目的等に応じて適宜選択することができる。
The detergent of the present invention includes the proteolytic enzyme, the proteolytic enzyme stabilizer, and a detergent component. The dosage form is not particularly limited and can be liquid, creamy, pasty or powdery. Such a detergent is known except that it contains the protease inhibitor. Can be prepared according to a method for producing a detergent containing the proteolytic enzyme.
The detergent component can be appropriately selected and blended from known components according to the type of the detergent, and the blending ratio of each component can be appropriately selected according to the purpose and the like.
洗浄剤成分としては、例えば、漂白剤、帯電防止剤、柔軟剤、アニオン界面活性剤、ノニオン界面活性剤、両性界面活性剤、カチオン界面活性剤、防腐剤、保湿剤、植物抽出物、水溶性高分子、シリコン、酸化防止剤、油脂類、アルコール、紫外線防止剤、キレート剤、ｐＨ調整剤、色素、香料、精製水又はこれらの２種以上の混合物等が挙げられる。 Examples of detergent components include bleaching agents, antistatic agents, softeners, anionic surfactants, nonionic surfactants, amphoteric surfactants, cationic surfactants, preservatives, moisturizers, plant extracts, water-soluble Examples thereof include polymers, silicon, antioxidants, fats and oils, alcohols, ultraviolet inhibitors, chelating agents, pH adjusters, dyes, fragrances, purified water, or a mixture of two or more thereof.
本発明の洗浄剤に配合する蛋白分解酵素の配合割合は、洗浄剤の種類や目的に応じてその酵素の力価等に応じて適宜決定することができるが、通常、洗浄剤全量に対して０．００１〜５質量％で配合することができる。 The proportion of the proteolytic enzyme to be blended in the detergent of the present invention can be appropriately determined depending on the type and purpose of the detergent, depending on the enzyme titer, etc. It can mix | blend by 0.001-5 mass%.
本発明の洗浄剤において、前記蛋白分解酵素安定化剤の配合割合は、後述する実施例から判るように濃度が高くなるほど安定化作用が高くなるので、洗浄剤の種類、蛋白分解酵素の配合量やその力価等を勘案して適宜決定することができる。 In the cleaning agent of the present invention, the mixing ratio of the proteolytic enzyme stabilizer increases the stabilizing action as the concentration increases as will be understood from the examples described later. It can be determined as appropriate by taking into account its titer and the like.
以下実施例、比較例及び処方例により、本発明を更に詳細に説明するが、本発明はこれらに限定されない。
尚、例中において用いた全ての蛋白分解酵素は、日本薬局方 一般試験法「消化力試験法」に基づいて測定した結果、７５０００単位／ｇのものを用いた。
実施例１−１〜１−６及び比較例１−１〜１−３
蛋白分解酵素０．２質量部、表１に示す蛋白分解酵素安定化剤２質量部、防腐剤としてのメチルパラベン０．１５質量部及び蒸留水を総量が１００質量部となるように加え、試験溶液を調製した。また、対照として、蛋白分解酵素安定化剤を配合しない試験溶液を調製した。得られた各試験溶液について、以下に示す酵素活性の残存率測定を行なった。結果を表１に示す。
EXAMPLES Hereinafter, although an Example, a comparative example, and a formulation example demonstrate this invention further in detail, this invention is not limited to these.
In addition, as a result of measuring based on the Japanese Pharmacopoeia general test method “digestion test method”, all proteolytic enzymes used in the examples were 75000 units / g.
Examples 1-1 to 1-6 and Comparative Examples 1-1 to 1-3
Add 0.2 parts by mass of proteolytic enzyme, 2 parts by mass of proteolytic enzyme stabilizer shown in Table 1, 0.15 parts by mass of methylparaben as preservative and distilled water so that the total amount becomes 100 parts by mass, and test solution Was prepared. As a control, a test solution containing no proteolytic enzyme stabilizer was prepared. With respect to each of the obtained test solutions, the residual rate of enzyme activity shown below was measured. The results are shown in Table 1.
＜酵素活性の残存率測定＞
０．５５ＭのＮａ2ＨＰＯ4水溶液に最終濃度が１質量％になるように脱脂粉乳を加え、８０℃以上で１時間加熱して脱脂粉乳を溶解させた。続いて、室温まで冷却後、１MのＨＣｌによりｐＨを７．５に調整し、１質量％の脱脂粉乳溶液を調製した。得られた脱脂粉乳溶液３．８ｍｌを試験管に取り、１０分間プレインキュベートした後、試験溶液２００μｌを加えて十分に撹拌し、比色計で正確に２０分後の透過率(測定波長６６０ｎｍ)を測定した。得られた透過率から、蛋白分解酵素の検量線を用いて酵素力価を測定した。
酵素活性の残存率は、試験溶液調製直後の酵素力価を１００％とした際の、試験溶液調製後４０℃で３０日間保存した後の酵素力価から算出した。結果を表１に示す。
尚、蛋白分解酵素の検量線は、１ｍＭ酢酸カルシウム−２０ｍＭ無水酢酸ナトリウム−１００ｍＭ塩化ナトリウムを蒸留水で溶解したｐＨ７．５の酵素希釈液を用いて所定濃度の蛋白分解酵素溶液をそれぞれ調製し、得られた蛋白分解酵素溶液１００μｌを、予め上記１質量％脱脂粉乳溶液３．９ｍｌを試験管に入れて１０分間プレインキュベートした後の試験管に加え、十分撹拌して正確に２０分後に透過率を比色計にて測定した結果から作成した。
<Measurement of residual rate of enzyme activity>
Nonfat dry milk was added to a 0.55 M Na 2 HPO 4 aqueous solution so that the final concentration was 1% by mass, and heated at 80 ° C. or higher for 1 hour to dissolve the nonfat dry milk. Subsequently, after cooling to room temperature, the pH was adjusted to 7.5 with 1M HCl to prepare a 1% by mass skim milk solution. 3.8 ml of the obtained skim milk solution is taken into a test tube, pre-incubated for 10 minutes, then added with 200 μl of the test solution and sufficiently stirred, and the transmittance after 20 minutes with a colorimeter (measurement wavelength: 660 nm). Was measured. The enzyme titer was measured from the obtained transmittance using a calibration curve of proteolytic enzyme.
The residual rate of enzyme activity was calculated from the enzyme titer after 30 days of storage at 40 ° C. after preparation of the test solution when the enzyme titer immediately after preparation of the test solution was taken as 100%. The results are shown in Table 1.
In addition, the calibration curve of the proteolytic enzyme was prepared by respectively preparing a proteolytic enzyme solution having a predetermined concentration using a pH 7.5 enzyme dilution solution obtained by dissolving 1 mM calcium acetate-20 mM anhydrous sodium acetate-100 mM sodium chloride in distilled water. 100 μl of the resulting proteolytic enzyme solution was added to the test tube after pre-incubating for 10 minutes with 3.9 ml of the above-mentioned 1% by weight skim milk solution in advance. Was prepared from the results of measurement with a colorimeter.
実施例２−１
イソマルトオリゴ糖０．２質量部、蛋白分解酵素０．２質量部、イソプロピルメチルフェノール０．１質量部、グリチルリチン酸ジカリウム０．１質量部、ラウロイルメチル−β−アラニンナトリウム液１０質量部、ラウリン酸ジエタノールアミド３質量部、テトラデセンスルホン酸ナトリウム液７質量部、ラウリルジメチルアミノ酢酸ベタイン液３質量部、ポリオキシエチレン硬化ヒマシ油１質量部、濃グリセリン２５質量部、１，３−ブチレングリコール１０質量部、メチルパラベン０．３質量部、香料０．０５質量部、色素０．００２質量部及び精製水を総量が１００質量部となるように加え、常法により液状のボディソープを調製した。得られたボディソープを被検試料として以下に示す酵素活性測定試験を行なった。
Example 2-1
0.2 parts by mass of isomaltoligosaccharide, 0.2 parts by mass of protease, 0.1 parts by mass of isopropylmethylphenol, 0.1 parts by mass of dipotassium glycyrrhizinate, 10 parts by mass of sodium lauroylmethyl-β-alanine, lauric acid 3 parts by weight of diethanolamide, 7 parts by weight of sodium tetradecenesulfonate, 3 parts by weight of lauryldimethylaminoacetic acid betaine solution, 1 part by weight of polyoxyethylene hydrogenated castor oil, 25 parts by weight of concentrated glycerin, 10 parts by weight of 1,3-butylene glycol Part, methyl paraben 0.3 part by mass, fragrance 0.05 part by mass, pigment 0.002 part by mass and purified water were added so that the total amount would be 100 parts by mass, and a liquid body soap was prepared by a conventional method. Using the obtained body soap as a test sample, the following enzyme activity measurement test was performed.
＜酵素活性測定試験＞
予め４０℃で３０日間保存した被検試料０．６ｇに、１ｍＭ酢酸カルシウム−２０ｍＭ無水酢酸ナトリウム−１００ｍＭ塩化ナトリウムからなるｐＨ７．５の酵素希釈液１０ｍｌを加えた溶液を、試験管に１ｍｌ入れ、３０℃で１０分間プレインキュベートした。次いで、カゼイン濃度が０．６質量％となるように５０ｍＭリン酸１水素ナトリウム水溶液を加えて８０℃で２０分間加熱溶解し、室温まで冷却した後にｐＨを７．５に調整したカゼイン溶液５ｍｌを、前記プレインキュベートした溶液に加え、十分に撹拌し、正確に１０分間反応させた。続いて、トリクロロ酢酸溶液(０．１１molトリクロロ酢酸、０．２２mol無水酢酸ナトリウム、６Mの酢酸溶液５５ｍｌに水を加えて総量を１リットルとしたもの、以後、この液をＴＣＡ溶液と略す)５ｍｌを加えて酵素を失活させて反応を停止させた。
反応停止後、３０℃で３０分間放置した後、ろ過を行なった。得られたろ液に、ジエチルエーテル５ｍｌを加えて３０分間撹拌した。次に、エーテル層を吸引除去し、更に、２０００ｒｐｍ、５分間遠心分離することによりエーテル層を完全に除去した。次いで、波長２８０ｎｍにおける吸光度を測定した。これをサンプルの吸光度とする。
<Enzyme activity measurement test>
1 ml of a solution obtained by adding 10 ml of a pH 7.5 enzyme dilution solution consisting of 1 mM calcium acetate-20 mM anhydrous sodium acetate-100 mM sodium chloride to 0.6 g of a test sample stored in advance at 40 ° C. for 30 days is placed in a test tube, Pre-incubation at 30 ° C. for 10 minutes. Next, 50 mM sodium monohydrogen phosphate aqueous solution was added so that the casein concentration was 0.6% by mass, dissolved by heating at 80 ° C. for 20 minutes, cooled to room temperature, and then 5 ml of casein solution adjusted to pH 7.5 was added. In addition to the pre-incubated solution, it was thoroughly stirred and allowed to react for exactly 10 minutes. Subsequently, 5 ml of a trichloroacetic acid solution (0.11 mol trichloroacetic acid, 0.22 mol sodium acetate, 55 ml of 6M acetic acid solution was added to water to make the total volume 1 liter, hereinafter this liquid is abbreviated as TCA solution) In addition, the enzyme was deactivated to stop the reaction.
After stopping the reaction, it was allowed to stand at 30 ° C. for 30 minutes, and then filtered. To the obtained filtrate, 5 ml of diethyl ether was added and stirred for 30 minutes. Next, the ether layer was removed by suction, and the ether layer was completely removed by centrifuging at 2000 rpm for 5 minutes. Next, the absorbance at a wavelength of 280 nm was measured. This is the absorbance of the sample.
一方、予め４０℃で３０日間保存した被検試料０．６ｇに、１ｍＭ酢酸カルシウム−２０ｍＭ無水酢酸ナトリウム−１００ｍＭ塩化ナトリウムからなるｐＨ７．５の酵素希釈液１０ｍｌを加えた溶液を、試験管に１ｍｌ入れ、３０℃で１０分間プレインキュベートした。次いで、前記ＴＣＡ溶液５ｍｌを加えて酵素を失活させた後、上記と同様なカゼイン溶液５ｍｌを加えて３０℃で３０分間放置しろ過を行なった。得られたろ液に、ジエチルエーテル５ｍｌを加えて３０分間撹拌した。次に、エーテル層を吸引除去し、更に、２０００ｒｐｍ、５分間遠心分離することによりエーテル層を完全に除去した。次いで、波長２８０ｎｍにおける吸光度を測定した。これをブランクの吸光度とする。
上記で測定したサンプルの吸光度からブランクの吸光度を差し引き補正して被検試料における酵素活性の残存率を測定した。結果を表２に示す。
尚、蛋白分解酵素の検量線は、蛋白分解酵素を所定の濃度に調製したものをサンプルとして、以後前記測定方法と同様に操作して得られた結果から作成した。
On the other hand, a solution obtained by adding 10 ml of a pH 7.5 enzyme dilution solution consisting of 1 mM calcium acetate-20 mM anhydrous sodium acetate-100 mM sodium chloride to 0.6 g of a test sample stored in advance at 40 ° C. for 30 days was added to 1 ml of a test tube. And preincubated for 10 minutes at 30 ° C. Next, 5 ml of the TCA solution was added to inactivate the enzyme, 5 ml of the same casein solution as above was added, and the mixture was allowed to stand at 30 ° C. for 30 minutes for filtration. To the obtained filtrate, 5 ml of diethyl ether was added and stirred for 30 minutes. Next, the ether layer was removed by suction, and the ether layer was completely removed by centrifuging at 2000 rpm for 5 minutes. Next, the absorbance at a wavelength of 280 nm was measured. This is the blank absorbance.
The absorbance of the blank was subtracted from the absorbance of the sample measured above and corrected to measure the residual rate of enzyme activity in the test sample. The results are shown in Table 2.
The calibration curve for the proteolytic enzyme was prepared from the results obtained by operating in the same manner as in the above measurement method using a sample prepared by proteolytic enzyme at a predetermined concentration.
実施例２−２〜２−６及び比較例２−１
イソマルトオリゴ糖０．２質量部の代わりに、ラフィノース１質量部(実施例２−２)を、フルクトース０．５質量部(実施例２−３)を、グリシルグリシン２．５質量部(実施例２−４)を、L-アルギニン-L-グルタミン酸１質量部(実施例２−５)を、若しくはイガイグリコーゲン３質量部(実施例２−６)を用いた以外は実施例２−１と同様に液状のボディソープを調製した。また、比較例２−１として、イソマルトオリゴ糖０．２質量部を配合しない以外は実施例２−１と同様に液状のボディソープを調製した。得られた各ボディソープを被検試料として、実施例２−１と同様にそれぞれ酵素活性の残存率を測定した。結果を表２に示す。
Examples 2-2 to 2-6 and Comparative Example 2-1
Instead of 0.2 parts by mass of isomaltoligosaccharide, 1 part by mass of raffinose (Example 2-2), 0.5 parts by mass of fructose (Example 2-3), 2.5 parts by mass of glycylglycine (implementation) Example 2-4) was replaced with Example 2-1 except that 1 part by mass of L-arginine-L-glutamic acid (Example 2-5) or 3 parts by mass of mussel glycogen (Example 2-6) was used. Similarly, a liquid body soap was prepared. Further, as Comparative Example 2-1, a liquid body soap was prepared in the same manner as in Example 2-1, except that 0.2 parts by mass of isomaltoligosaccharide was not blended. Using the obtained body soaps as test samples, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 2.
実施例３−１
イソマルトオリゴ糖０．５質量部、ミリスチン酸カリウム２５質量部、カリウム石鹸素地１０質量部、蛋白分解酵素０．１５質量部、タルク３質量部、マルトース５質量部、グリチルリチン酸ジカリウム０．１質量部、イソプロピルメチルフェノール０．１質量部及びトウモロコシデンプンを総量が１００質量部となるように加え、常法により洗顔パウダーを調製した。得られた洗顔パウダーを被検試料として実施例２−１と同様に酵素活性の残存率を測定した。結果を表３に示す。
Example 3-1
0.5 parts by weight of isomaltoligosaccharides, 25 parts by weight of potassium myristate, 10 parts by weight of potassium soap base, 0.15 parts by weight of protease, 3 parts by weight of talc, 5 parts by weight of maltose, 0.1 parts by weight of dipotassium glycyrrhizinate Then, 0.1 parts by mass of isopropylmethylphenol and corn starch were added so that the total amount was 100 parts by mass, and a face washing powder was prepared by a conventional method. Using the obtained face washing powder as a test sample, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 3.
実施例３−２〜３−６及び比較例３−１
イソマルトオリゴ糖０．５質量部の代わりに、ラフィノース２質量部(実施例３−２)を、フルクトース１質量部(実施例３−３)を、グリシルグリシン０．５質量部(実施例３−４)を、L-アルギニン-L-グルタミン酸０．１質量部(実施例３−５)を、若しくはイガイグリコーゲン１質量部(実施例３−６)を用いた以外は実施例３−１と同様に洗顔パウダーを調製した。また、比較例３−１として、イソマルトオリゴ糖０．５質量部を配合しない以外は実施例３−１と同様に洗顔パウダーを調製した。得られた各洗顔パウダーを被検試料として、実施例２−１と同様にそれぞれ酵素活性の残存率を測定した。結果を表３に示す。
Examples 3-2 to 3-6 and Comparative Example 3-1
Instead of 0.5 parts by mass of isomaltoligosaccharide, 2 parts by mass of raffinose (Example 3-2), 1 part by mass of fructose (Example 3-3), 0.5 parts by mass of glycylglycine (Example 3) -4), and Example 3-1 except that 0.1 part by mass of L-arginine-L-glutamic acid (Example 3-5) or 1 part by mass of mussel glycogen (Example 3-6) was used. Similarly, a face washing powder was prepared. Further, as Comparative Example 3-1, a face washing powder was prepared in the same manner as in Example 3-1, except that 0.5 part by mass of isomaltoligosaccharide was not blended. Using each of the obtained facial cleansing powders as a test sample, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 3.
実施例４−１
イソマルトオリゴ糖０．２質量部、α−オレフィンスルホン酸ナトリウム５質量部、メチルパラベン０．２質量部、ソルビット１０質量部、ラウリン酸１質量部、ミリスチン酸７質量部、ベヘン酸３質量部、ジステアリン酸エチレングリコール２．５質量部、ヒドロキシエタンジホスホン酸４ナトリウム０．１質量部、トリエタノールアミン５．５質量部、ジブチルヒドロキシトルエン０．０２質量部、蛋白分解酵素０．２質量部、香料０．０５質量部、濃グリセリン５４質量部及び精製水を総量が１００質量部となるように加え、常法により洗顔クリームを調製した。得られた洗顔クリームを被検試料として、実施例２−１と同様に酵素活性の残存率を測定した。結果を表４に示す。
Example 4-1
0.2 parts by weight of isomaltoligosaccharide, 5 parts by weight of sodium α-olefin sulfonate, 0.2 parts by weight of methyl paraben, 10 parts by weight of sorbit, 1 part by weight of lauric acid, 7 parts by weight of myristic acid, 3 parts by weight of behenic acid, distearin Ethylene glycol 2.5 parts by mass, hydroxyethane diphosphonate tetrasodium 0.1 parts by mass, triethanolamine 5.5 parts by mass, dibutylhydroxytoluene 0.02 parts by mass, proteolytic enzyme 0.2 parts by mass, fragrance 0.05 parts by mass, 54 parts by mass of concentrated glycerin and purified water were added so that the total amount was 100 parts by mass, and a face-wash cream was prepared by a conventional method. Using the obtained facial cleansing cream as a test sample, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 4.
実施例４−２〜４−６及び比較例４−１
イソマルトオリゴ糖０．２質量部の代わりに、ラフィノース０．５質量部(実施例４−２)を、フルクトース１質量部(実施例４−３)を、グリシルグリシン０．０５質量部(実施例４−４)を、L-アルギニン-L-グルタミン酸０．５質量部(実施例４−５)を、若しくはイガイグリコーゲン０．４質量部(実施例４−６)を用いた以外は実施例４−１と同様に洗顔クリームを調製した。また、比較例４−１として、イソマルトオリゴ糖０．２質量部を配合しない以外は実施例４−１と同様に洗顔クリームを調製した。得られた各洗顔クリームを被検試料として、実施例２−１と同様にそれぞれ酵素活性の残存率を測定した。結果を表４に示す。
Examples 4-2 to 4-6 and Comparative Example 4-1
Instead of 0.2 parts by mass of isomaltooligosaccharide, 0.5 parts by mass of raffinose (Example 4-2), 1 part by mass of fructose (Example 4-3), 0.05 parts by mass of glycylglycine (implemented) Example 4-4), except that 0.5 parts by mass of L-arginine-L-glutamic acid (Example 4-5) or 0.4 parts by mass of mussel glycogen (Example 4-6) was used. A face cream was prepared in the same manner as in 4-1. Moreover, as Comparative Example 4-1, a face-washing cream was prepared in the same manner as in Example 4-1, except that 0.2 parts by mass of isomaltoligosaccharide was not blended. The obtained facial cleansing cream was used as a test sample, and the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 4.
実施例５−１
イソマルトオリゴ糖０．３質量部、炭酸水素ナトリウム９４質量部、無水ケイ酸０．７質量部、蛋白分解酵素０．６質量部、香料０．９質量部、色素０．０１質量部、硫酸ナトリウムで全量を１００質量部となるように加えて常法により粉末入浴剤を調製した。得られた入浴剤を被検試料として、実施例２−１と同様に酵素活性の残存率を測定した。結果を表５に示す。
Example 5-1
0.3 parts by weight of isomaltoligosaccharide, 94 parts by weight of sodium hydrogen carbonate, 0.7 parts by weight of anhydrous silicic acid, 0.6 parts by weight of protease, 0.9 parts by weight of fragrance, 0.01 parts by weight of dye, sodium sulfate And adding the total amount to 100 parts by mass to prepare a powder bath by a conventional method. Using the obtained bathing agent as a test sample, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 5.
実施例５−２〜５−６及び比較例５−１
イソマルトオリゴ糖０．３質量部の代わりに、ラフィノース１．５質量部(実施例５−２)を、フルクトース０．５質量部(実施例５−３)を、グリシルグリシン２質量部(実施例５−４)を、L-アルギニン-L-グルタミン酸１質量部(実施例５−５)を、若しくはイガイグリコーゲン２質量部(実施例５−６)を用いた以外は実施例５−１と同様に粉末入浴剤を調製した。また、比較例５−１として、イソマルトオリゴ糖０．３質量部を配合しない以外は実施例５−１と同様に粉末入浴剤を調製した。得られた各入浴剤を被検試料として、実施例２−１と同様にそれぞれ酵素活性の残存率を測定した。結果を表５に示す。
Examples 5-2 to 5-6 and Comparative Example 5-1
Instead of 0.3 parts by mass of isomaltoligosaccharide, 1.5 parts by mass of raffinose (Example 5-2), 0.5 parts by mass of fructose (Example 5-3), 2 parts by mass of glycylglycine (implemented) Example 5-4) and Example 5-1 except that 1 part by mass of L-arginine-L-glutamic acid (Example 5-5) or 2 parts by mass of mussel glycogen (Example 5-6) were used. Similarly, a powder bath was prepared. Moreover, as Comparative Example 5-1, a powder bath was prepared in the same manner as in Example 5-1, except that 0.3 parts by mass of isomaltoligosaccharide was not blended. Using each obtained bath as a test sample, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 5.
実施例６−１
イソマルトオリゴ糖２質量部、蛋白分解酵素１質量部、POEPOPアルキルエーテル１０質量部、ラウリルジメチルアミノ酢酸ベタイン液２０質量部、ヤシ油脂肪酸ジエタノールアミド５質量部、濃グリセリン２０質量部、ジプロピレングリコール１０質量部、エタノール３質量部、メチルパラベン０．２質量部、香料０．８質量部及び水で全量を１００質量部となるように加えて常法により台所用液体洗浄剤を調製した。得られた台所用液体洗浄剤を被検試料として、実施例２−１と同様に酵素活性の残存率を測定した。結果を表６に示す。
Example 6-1
2 parts by weight of isomaltoligosaccharide, 1 part by weight of protease, 10 parts by weight of POEPOP alkyl ether, 20 parts by weight of lauryldimethylaminoacetic acid betaine solution, 5 parts by weight of coconut oil fatty acid diethanolamide, 20 parts by weight of concentrated glycerin, 10 dipropylene glycol A liquid detergent for kitchen was prepared in a conventional manner by adding 100 parts by mass with 3 parts by mass, 3 parts by mass of ethanol, 0.2 parts by mass of methyl paraben, 0.8 parts by mass of perfume and water. The residual rate of enzyme activity was measured in the same manner as in Example 2-1, using the obtained kitchen liquid detergent as a test sample. The results are shown in Table 6.
実施例６−２〜６−６及び比較例６−１
イソマルトオリゴ糖２質量部の代わりに、ラフィノース０．５質量部(実施例６−２)を、フルクトース２質量部(実施例６−３)を、グリシルグリシン１質量部(実施例６−４)を、L-アルギニン-L-グルタミン酸１．５質量部(実施例６−５)を、若しくはイガイグリコーゲン２質量部(実施例６−６)を用いた以外は実施例６−１と同様に台所用液体洗浄剤を調製した。また、比較例６−１として、イソマルトオリゴ糖２質量部を配合しない以外は実施例６−１と同様に台所用液体洗浄剤を調製した。得られた各台所用液体洗浄剤を被検試料として、実施例２−１と同様にそれぞれ酵素活性の残存率を測定した。結果を表６に示す。
Examples 6-2 to 6-6 and Comparative Example 6-1
Instead of 2 parts by mass of isomaltooligosaccharide, 0.5 part by mass of raffinose (Example 6-2), 2 parts by mass of fructose (Example 6-3), 1 part by mass of glycylglycine (Example 6-4) ), 1.5 parts by mass of L-arginine-L-glutamic acid (Example 6-5) or 2 parts by mass of mussel glycogen (Example 6-6) was used in the same manner as in Example 6-1. A liquid detergent for kitchen was prepared. Moreover, as Comparative Example 6-1, a liquid detergent for kitchen was prepared in the same manner as in Example 6-1, except that 2 parts by mass of isomaltoligosaccharide was not blended. The remaining rate of enzyme activity was measured in the same manner as in Example 2-1, using the obtained kitchen liquid cleaners as test samples. The results are shown in Table 6.
実施例７−１
イソマルトオリゴ糖０．７質量部、POEラウリルエーテル硫酸ナトリウム液１８質量部、ヤシ油脂肪酸ジエタノールアミド２質量部、ヤシ油脂肪酸アミドプロピルベタイン液７質量部、濃グリセリン１５質量部、塩化ｏ−[２−ヒドロキシ−３−(トリメチルアンモニオ)プロピル]ヒドロキシエチルセルロース０．５質量部、アクリル酸アルキル共重合体エマルジョン０．５質量部、ジステアリン酸エチレングリコール１．５質量部、蛋白分解酵素０．２質量部、エタノール１質量部、エデト酸２ナトリウム０．１質量部、メチルパラベン０．１質量部、色素０．００１質量部、香料０．０５質量部、水で全量を１００質量部となるように加えて液体シャンプーを調製した。得られた液体シャンプーを被検試料として、実施例２−１と同様に酵素活性の残存率を測定した。結果を表７に示す。
Example 7-1
Isomaltooligosaccharide 0.7 parts by mass, POE sodium lauryl ether sulfate solution 18 parts by mass, coconut oil fatty acid diethanolamide 2 parts by mass, coconut oil fatty acid amidopropyl betaine solution 7 parts by mass, concentrated glycerin 15 parts by mass, o- [2 chloride -Hydroxy-3- (trimethylammonio) propyl] hydroxyethylcellulose 0.5 parts by weight, alkyl acrylate copolymer emulsion 0.5 parts by weight, ethylene glycol distearate 1.5 parts by weight, proteolytic enzyme 0.2 parts by weight Part, ethanol 1 part by mass, disodium edetate 0.1 part by mass, methyl paraben 0.1 part by mass, pigment 0.001 part by mass, fragrance 0.05 part by mass, and water so that the total amount becomes 100 parts by mass A liquid shampoo was prepared. Using the obtained liquid shampoo as a test sample, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 7.
実施例７−２〜７−６及び比較例７−１
イソマルトオリゴ糖０．７質量部の代わりに、ラフィノース１質量部(実施例７−２)を、フルクトース３質量部(実施例７−３)を、グリシルグリシン０．０５質量部(実施例７−４)を、L-アルギニン-L-グルタミン酸１質量部(実施例７−５)を、若しくはイガイグリコーゲン１質量部(実施例７−６)を用いた以外は実施例７−１と同様に液体シャンプーを調製した。また、比較例７−１として、イソマルトオリゴ糖０．７質量部を配合しない以外は実施例７−１と同様に液体シャンプーを調製した。得られた各液体シャンプーを被検試料として、実施例２−１と同様にそれぞれ酵素活性の残存率を測定した。結果を表７に示す。
Examples 7-2 to 7-6 and Comparative Example 7-1
Instead of 0.7 parts by mass of isomaltoligosaccharide, 1 part by mass of raffinose (Example 7-2), 3 parts by mass of fructose (Example 7-3), 0.05 parts by mass of glycylglycine (Example 7) -4) was used in the same manner as in Example 7-1 except that 1 part by mass of L-arginine-L-glutamic acid (Example 7-5) or 1 part by mass of mussel glycogen (Example 7-6) was used. A liquid shampoo was prepared. Moreover, as Comparative Example 7-1, a liquid shampoo was prepared in the same manner as in Example 7-1 except that 0.7 parts by mass of isomaltoligosaccharide was not blended. Using each liquid shampoo obtained as a test sample, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 7.
実施例８−１
イソマルトオリゴ糖１質量部、キサンタンガム０．５質量部、カルボキシビニルポリマー０．５１質量部、POE硬化ヒマシ油０．５質量部、蛋白分解酵素０．２質量部、エタノール７質量部、色素０．００１質量部、香料０．０２質量部、水酸化ナトリウム０．０９６質量部、メチルパラベン０．１質量部、水で全量を１００質量部となるように加えてジェル状パックを調製した。得られたジェル状パックを被検試料として、実施例２−１と同様に酵素活性の残存率を測定した。結果を表８に示す。
Example 8-1
1 part by weight of isomaltooligosaccharide, 0.5 part by weight of xanthan gum, 0.51 part by weight of carboxyvinyl polymer, 0.5 part by weight of POE hydrogenated castor oil, 0.2 part by weight of protease, 7 parts by weight of ethanol, 0. A gel pack was prepared by adding 001 parts by mass, 0.02 parts by mass of perfume, 0.096 parts by mass of sodium hydroxide, 0.1 parts by mass of methyl paraben, and 100 parts by mass of water. Using the obtained gel pack as a test sample, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 8.
実施例８−２〜８−６及び比較例８−１
イソマルトオリゴ糖１質量部の代わりに、ラフィノース１質量部(実施例８−２)を、フルクトース２質量部(実施例８−３)を、グリシルグリシン２．５質量部(実施例８−４)を、L-アルギニン-L-グルタミン酸０．５質量部(実施例８−５)を、若しくはイガイグリコーゲン１質量部(実施例８−６)を用いた以外は実施例８−１と同様にジェル状パックを調製した。また、比較例８−１として、イソマルトオリゴ糖１質量部を配合しない以外は実施例８−１と同様にジェル状パックを調製した。得られた各ジェル状パックを被検試料として、実施例２−１と同様にそれぞれ酵素活性の残存率を測定した。結果を表８に示す。
Examples 8-2 to 8-6 and Comparative Example 8-1
Instead of 1 part by mass of isomaltooligosaccharide, 1 part by mass of raffinose (Example 8-2), 2 parts by mass of fructose (Example 8-3), 2.5 parts by mass of glycylglycine (Example 8-4) ), 0.5 parts by mass of L-arginine-L-glutamic acid (Example 8-5) or 1 part by mass of mussel glycogen (Example 8-6) was used in the same manner as in Example 8-1. A gel pack was prepared. Moreover, as Comparative Example 8-1, a gel-like pack was prepared in the same manner as in Example 8-1, except that 1 part by mass of isomaltoligosaccharide was not blended. Using the obtained gel packs as test samples, the residual rate of enzyme activity was measured in the same manner as in Example 2-1. The results are shown in Table 8.
処方例１
表９に示すNo.１〜１２の組成を用いて、常法に従い液体ボディソープをそれぞれ調製した。
Formulation Example 1
Using the compositions of Nos. 1 to 12 shown in Table 9, liquid body soaps were prepared according to conventional methods.
処方例２
表１０に示すNo.１〜１２の組成を用いて、常法に従い洗顔パウダーをそれぞれ調製した。
Formulation example 2
Using the compositions of Nos. 1 to 12 shown in Table 10, facial cleansing powders were prepared according to conventional methods.
処方例３
表１１に示すNo.１〜１２の組成を用いて、常法に従い洗顔クリームをそれぞれ調製した。
Formulation Example 3
Using the compositions of Nos. 1 to 12 shown in Table 11, face wash creams were prepared according to conventional methods.
処方例４
表１２に示すNo.１〜１２の組成を用いて、常法に従い液体シャンプーをそれぞれ調製した。
Formulation Example 4
Using the compositions of Nos. 1 to 12 shown in Table 12, liquid shampoos were prepared according to conventional methods.
処方例５
表１３に示すNo.１〜１２の組成を用いて、常法に従い粉末入浴剤をそれぞれ調製した。
Formulation Example 5
Using the compositions of Nos. 1 to 12 shown in Table 13, powder baths were prepared in accordance with conventional methods.
処方例６
表１４に示すNo.１〜１２の組成を用いて、常法に従い液体入浴剤をそれぞれ調製した。
Formulation Example 6
Using the compositions of Nos. 1 to 12 shown in Table 14, liquid bath agents were prepared according to conventional methods.
処方例７
表１５に示すNo.１〜１２の組成を用いて、常法に従いクレンジングオイルをそれぞれ調製した。
Formulation Example 7
Cleansing oils were prepared according to conventional methods using the compositions of Nos. 1 to 12 shown in Table 15.
処方例８
表１６に示すNo.１〜１２の組成を用いて、常法に従い液状台所洗剤をそれぞれ調製した。
Formulation Example 8
Using the compositions of Nos. 1 to 12 shown in Table 16, liquid kitchen detergents were prepared according to conventional methods.
処方例９
表１７に示すNo.１〜１２の組成を用いて、常法に従い粉末シャンプーをそれぞれ調製した。
Formulation Example 9
Using the compositions of Nos. 1 to 12 shown in Table 17, powder shampoos were prepared according to conventional methods.
処方例１０
表１８に示すNo.１〜１２の組成を用いて、常法に従い粉末パックをそれぞれ調製した。
Formulation Example 10
Using the compositions of Nos. 1 to 12 shown in Table 18, powder packs were prepared according to a conventional method.
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| JP2005306823A (en) * | 2004-04-26 | 2005-11-04 | Kansai Koso Kk | Oily cleansing cosmetic in which enzyme is formulated |
| JP2007186447A (en) * | 2006-01-12 | 2007-07-26 | Japan Royal Jelly Co Ltd | Bath preparation |
| JP5225642B2 (en) * | 2007-09-21 | 2013-07-03 | ツキオカフィルム製薬株式会社 | Soap sheet |
| JP5210693B2 (en) * | 2008-04-11 | 2013-06-12 | 持田製薬株式会社 | Enzyme cleansing powder |
| JP5950557B2 (en) * | 2011-11-18 | 2016-07-13 | サラヤ株式会社 | Liquid detergent composition |
| RU2642077C2 (en) | 2013-11-11 | 2018-01-24 | ЭКОЛАБ ЮЭсЭй ИНК. | Multi-purpose enzyme detergent and methods of stabilizing applicable solution |
| JP6468650B2 (en) * | 2015-05-25 | 2019-02-13 | 関西酵素株式会社 | Oil-based cleansing cosmetic |
| JP6918361B2 (en) * | 2018-07-13 | 2021-08-11 | 関西酵素株式会社 | Cleaning fee |
| TW202320731A (en) * | 2021-08-10 | 2023-06-01 | 日商樂敦製藥股份有限公司 | Cleaning composition and production method for same |
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