JP2005306822A - Protease stabilizer, cosmetic and cleansing agent - Google Patents
Protease stabilizer, cosmetic and cleansing agent Download PDFInfo
- Publication number
- JP2005306822A JP2005306822A JP2004129848A JP2004129848A JP2005306822A JP 2005306822 A JP2005306822 A JP 2005306822A JP 2004129848 A JP2004129848 A JP 2004129848A JP 2004129848 A JP2004129848 A JP 2004129848A JP 2005306822 A JP2005306822 A JP 2005306822A
- Authority
- JP
- Japan
- Prior art keywords
- mass
- parts
- cosmetic
- proteolytic enzyme
- stabilizer
- 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
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- 239000002537 cosmetic Substances 0.000 title claims abstract description 33
- 239000003381 stabilizer Substances 0.000 title claims abstract description 33
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Landscapes
- Enzymes And Modification Thereof (AREA)
- Cosmetics (AREA)
- Detergent Compositions (AREA)
Abstract
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、オリゴ糖類、糖類、ジペプチド、多糖類の少なくとも1種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。
Since the proteolytic enzyme stabilizer of the present invention contains at least one specific oligosaccharide, saccharide, dipeptide, or polysaccharide as an active ingredient, when it is incorporated into cosmetics or detergents, The decrease in activity can be effectively suppressed, and further, when blended in a cosmetic, the feeling of use 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、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種以上を含む。
The present invention will be described in detail below.
The proteolytic enzyme stabilizer of the present invention is one or more selected from the group consisting of isomaltooligosaccharide, raffinose, fructose, glycylglycine, L-arginine-L-glutamic acid and mussel glycogen as an active ingredient. including.
前記イソマルトオリゴ糖は、例えば、マルトースを主成分とした水飴に転移酵素を作用させて得られる、デンプンの分岐部分の構造を有するオリゴ糖であり、具体的にはパノース、イソマルトース、イソマルトトリオース等を含むものが挙げられる。また、市販品を用いることもでき、例えば、(株)林原生物化学研究所製の「PANORUP」(登録商標)等が挙げられる。
前記ラフィノースは、D−ガラクトース、D−グルコース、D−フラクトースからなる三糖(オリゴ糖)であって、ビート、サトウキビ、蜂蜜、キャベツ、酵母、ジャガイモ、ブドウ、麦類、トウモロコシや多くの豆科植物の種子等に存在し、これらから得ることができる。また、市販品を用いることもでき、例えば、旭化成(株)製の「オリゴGGF」(登録商標)等が挙げられる。
前記フルクトースは、果汁や蜂蜜等に存在する還元力を有する糖である。また、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。
前記イガイグリコーゲンは、ムラサキイガイ(ムール貝)の貝肉から抽出したイガイ由来のポリサッカライドであるグリコーゲンであり、例えば、市販品の「ビオサッカライドGY」(商品名、山川貿易株式会社)等を用いることができる。
The isomaltoligosaccharide is an oligosaccharide having a structure of a branched portion of starch obtained by, for example, acting a transferase on a starch syrup containing maltose as a main component, specifically, panose, isomaltose, isomaltoltrio. The thing containing ausus etc. is mentioned. Commercial products can also be used, and examples thereof include “PANORUP” (registered trademark) manufactured by Hayashibara Biochemical Laboratories.
The raffinose is a trisaccharide (oligosaccharide) composed of D-galactose, D-glucose, and D-fructose, and includes beet, sugarcane, honey, cabbage, yeast, potato, grape, wheat, corn and many legumes. It exists in plant seeds and can be obtained from these. Commercial products can also be used, and examples thereof include “Oligo GGF” (registered trademark) manufactured by Asahi Kasei Corporation.
The fructose is a sugar having a reducing power that exists in fruit juice, honey and the like. In addition, glycylglycine is a dipeptide in which two molecules of glycine are peptide-bonded, and L-arginine-L-glutamic acid is a dipeptide in which arginine and glutamic acid are bonded.
The mussel glycogen is glycogen which is a mussel-derived polysaccharide extracted from mussel (mussel) shell, and for example, commercially available “Biosaccharide GY” (trade name, Yamakawa Trading Co., Ltd.) can be used. it can.
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 in consideration of the price and the titer.
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, preincubated 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, each of the calibration curves of proteolytic enzymes was prepared by respectively preparing a proteolytic enzyme solution having a predetermined concentration using an enzyme dilution solution of pH 7.5 in which 1 mM calcium acetate-20 mM anhydrous sodium acetate-100 mM sodium chloride was dissolved 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, and after 20 minutes with sufficient stirring, the transmittance 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 mass of isomaltoligosaccharide, 25 parts by mass of potassium myristate, 10 parts by mass of potassium soap base, 0.15 parts by mass of protease, 3 parts by mass of talc, 5 parts by mass of maltose, 0.1 parts by mass 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-wash 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 isomaltoligosaccharide, 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 fragrance, 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
Using the compositions of Nos. 1 to 12 shown in Table 15, cleansing oils were respectively prepared according to conventional methods.
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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Cited By (9)
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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 |
JP2009073974A (en) * | 2007-09-21 | 2009-04-09 | Showa Kako Kk | Sheet shaped soap |
JP2009256211A (en) * | 2008-04-11 | 2009-11-05 | Mochida Pharmaceut Co Ltd | Enzyme-compounded face-washing powder |
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Cited By (12)
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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 |
JP2009073974A (en) * | 2007-09-21 | 2009-04-09 | Showa Kako Kk | Sheet shaped soap |
JP2009256211A (en) * | 2008-04-11 | 2009-11-05 | Mochida Pharmaceut Co Ltd | Enzyme-compounded face-washing powder |
JP2013108048A (en) * | 2011-11-18 | 2013-06-06 | Saraya Kk | Liquid detergent composition |
EP3068861B1 (en) | 2013-11-11 | 2020-03-18 | Ecolab USA Inc. | Multiuse, enzymatic detergent and methods of stabilizing a use solution |
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JP2016216417A (en) * | 2015-05-25 | 2016-12-22 | 関西酵素株式会社 | Oily cleansing cosmetic |
JP2020011909A (en) * | 2018-07-13 | 2020-01-23 | 関西酵素株式会社 | Detergent |
WO2023017790A1 (en) * | 2021-08-10 | 2023-02-16 | ロート製薬株式会社 | Cleaning composition and production method for same |
JP7265100B1 (en) * | 2021-08-10 | 2023-04-25 | ロート製薬株式会社 | CLEANING COMPOSITION AND PRODUCTION METHOD THEREOF |
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