JPS60109518A - Production of bath agent containing enzyme - Google Patents

Production of bath agent containing enzyme

Info

Publication number
JPS60109518A
JPS60109518A JP58215631A JP21563183A JPS60109518A JP S60109518 A JPS60109518 A JP S60109518A JP 58215631 A JP58215631 A JP 58215631A JP 21563183 A JP21563183 A JP 21563183A JP S60109518 A JPS60109518 A JP S60109518A
Authority
JP
Japan
Prior art keywords
dyestuff
crude drug
activity
enzyme
enzymes
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
Application number
JP58215631A
Other languages
Japanese (ja)
Other versions
JPS6324973B2 (en
Inventor
Tadao Shiraishi
白石 忠生
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Individual
Original Assignee
Individual
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Individual filed Critical Individual
Priority to JP58215631A priority Critical patent/JPS60109518A/en
Publication of JPS60109518A publication Critical patent/JPS60109518A/en
Publication of JPS6324973B2 publication Critical patent/JPS6324973B2/ja
Granted legal-status Critical Current

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Classifications

    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00Cosmetics or similar toiletry preparations
    • A61K8/18Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64Proteins; Peptides; Derivatives or degradation products thereof
    • A61K8/66Enzymes
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61QSPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00Preparations for care of the skin
    • A61Q19/10Washing or bathing preparations

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Dermatology (AREA)
  • Birds (AREA)
  • Epidemiology (AREA)
  • Cosmetics (AREA)

Abstract

PURPOSE:To obtain a bath agent having improved cleaning ability of the skin, detergency as washing water, good stability of a dyestuff and improved heat insulating effect, by incorporating a proteolytic enzyme derived from microorganisms with an enzyme from animal internal organs, a crude drug, dyestuff and perfume. CONSTITUTION:A bath agent obtained by incroporating a proteolytic enzyme, e.g. ASP protease, derived from microorganisms with an enzyme from animal internal organs, e.g. pancreatin, and a crude drug, e.g. ginseng powder, poeny root powder or cork tree bark extract, adding a dyestuff, e.g. Blue No.1 or Yellow No.4, with a dyestuff dissolving agent, e.g. propylene glycol, to the resultant mixture, and mixing a perfume therewith. The two kinds of the enzymes enhance the cleaning ability of the skin and detergency as washing water within a wide pH and temperature range, and the crude drug stabilizes the enzymes. The stabilization of the dyestuff is promoted by the crude drug and the dyestuff stabilizer. The heat insulation property is further enhanced by the overall action of the respective components.

Description

【発明の詳細な説明】 本発明は酵素入り入浴剤の製法に関するものである。[Detailed description of the invention] The present invention relates to a method for producing enzyme-containing bath additives.

従来、酵素入り入浴剤の酵素としては、パパインなど植
物起源の蛋白分解酵素が単独で用いられるものであるが
、かかる甲類の酵素のみでは、広いpl−1域又は広い
温度域で均一な蛋白質の分解能を保持し得ないと共に皮
膚表面に存在する脂肪、でんぷん等の分解が行えず、水
質によるpト1の相違又は使用時における湿度の相違に
より皮膚の清浄化が充分に行えないため、白鮮菌等の温
床となり易(、皮虐病の予防とはなり得なかった。更に
風呂の残り湯を洗濯水として用いる際には、比較的低い
湿度で使用されるために酵素の活性が低く酵素にJ−る
洗滌力強化が開時できなかった。また、他にかかる入浴
剤は入浴剤としては重要な要素の一つである配合色素の
安定性を欠き、更には、酵素白身の安定性もよくなく、
酵素の経時変化によって分解能力が低下し、所望の効果
を発揮できないおそれがあり、実際に効果、効能として
うたわれている皮膚の清浄化、風呂の残り湯を洗擢水に
使用する場合の洗滌促進効果等が充分に得られなかった
。 本発明では、微生物起源の蛋白分解酵素と、蛋白分
解作用、脂肪分解作用、でんぷん分解作用を右づる動物
の臓器より得られる酵素と、生栗成分とを混合して、広
いpト(域及び広い温度域での皮膚清浄化及び風呂の残
り渇を洗濯水に使用する場合の洗滌力強化に優れ、皮膚
病の予防を図れると共に、酵素自身の安定化による酵素
の分解能力の保持、並びに色素の安定性保持を図れる酵
素入り入浴剤の製法を提供せんとするものである。
Conventionally, plant-derived proteolytic enzymes such as papain have been used alone as enzymes in enzyme-containing bath additives, but such enzymes alone cannot produce homogeneous proteins over a wide pl-1 range or a wide temperature range. In addition to being unable to maintain the resolution of fat and starch present on the skin surface, it is also difficult to cleanse the skin sufficiently due to differences in pto1 due to water quality or differences in humidity during use. It easily became a breeding ground for fresh germs (and could not prevent skin diseases. Furthermore, when leftover bath water is used as washing water, it is used at a relatively low humidity, so the enzyme activity is low and the enzyme In addition, other bath additives lack the stability of the blended pigments, which is one of the important elements for bath additives, and furthermore, the stability of the enzyme whites is poor. It's not good either,
Due to changes in the enzyme over time, the decomposition ability may decrease and the desired effect may not be achieved.Actually, the effects and efficacy of the product are skin cleansing and promotion of cleansing when leftover hot water from a bath is used as cleansing water. The effects etc. were not sufficiently obtained. In the present invention, proteolytic enzymes of microbial origin, enzymes obtained from animal organs that have proteolytic, lipolytic, and starch decomposing effects, and raw chestnut components are mixed together. It is excellent for skin cleansing in a wide temperature range and for strengthening the detergent power when using the residual thirst from the bath as washing water, and can prevent skin diseases, maintain the degrading ability of enzymes by stabilizing the enzymes themselves, and improve pigmentation. The purpose of the present invention is to provide a method for producing enzyme-containing bath additives that maintains the stability of the enzymes.

本発明の実施例を信脱すれば次の通りである。The following is a deviation from the embodiment of the present invention.

即ち、この発明の実施例の配合は、酵素、ナトリウム素
材、生薬末又は生葉エキス、色素及び色素溶解剤、色素
安定剤、並びに香料より成るものであり、配合順序は酵
素、ナトリウム素材、生薬末又は生薬エキスの混合物に
色素溶解剤に溶解せしめた色素を混入し、次いで香1′
i1、色素安定剤を順次混入せしめるものである。
That is, the formulation of the embodiment of this invention consists of an enzyme, a sodium material, a herbal medicine powder or a fresh leaf extract, a pigment and a pigment solubilizing agent, a pigment stabilizer, and a fragrance. Alternatively, a mixture of crude drug extracts is mixed with a pigment dissolved in a pigment dissolving agent, and then fragrance 1' is added.
i1, a dye stabilizer is sequentially mixed.

酵素どしては、微生物起源の蛋白分解酵素及び蛋白分解
作用、脂肪分解作用、でんぷん分解作用を有する動物の
臓器より得られる酵素を“二梗類配合しており、このう
ち微生物起源の蛋白分解酵素にはたとえばΔSPプロテ
アービ、敢線菌プロテアーゼ、黒麹菌プロテアーゼ等を
用い、動物の臓器より1!?られる酵素にはパンクレア
チン等を用いる。またfl−リウム素材としてはt!A
酸水素ナトリウム、塩化ナトリウムを用いる。
The enzymes include proteolytic enzymes derived from microorganisms and enzymes obtained from animal organs that have proteolytic, lipolytic, and starch degrading actions. Examples of enzymes used include ΔSP proteavi, Mycobacterium protease, and Aspergillus Aspergillus protease, and pancreatin and the like are used as enzymes derived from animal organs.Furthermore, as the fl-rium material, t!A is used.
Use sodium oxyhydrogen and sodium chloride.

また生薬末又は生薬エキスどしては、シャクA7り末、
コウボク末、ヂンビ末、人参末、オウバクエキス等を用
いる。
In addition, as crude drug powder or crude drug extract, Shaku A7 powder,
Uses powdered Koboku, powdered ginseng, powdered ginseng, extract of Prunus japonicus, etc.

また色素としては青色1号及び黄色4号を、色素溶解剤
としてはプロピレングリコールをそれぞれ用いている。
Blue No. 1 and Yellow No. 4 are used as dyes, and propylene glycol is used as a dye solubilizer.

また色素安定剤として(よジペンタエリトリッ]・脂肪
酸エステルを用いる。
In addition, fatty acid ester (yodipentaerythritol) is used as a dye stabilizer.

上記実施例の配合は次のような作用を目的として設定し
たものである。即ち、二種の酵素は、皮m清浄化、及び
風呂の残り潟を洗)「水に用いた場合の洗滌力の強化を
広いII 1−1域及び広い温度域で保有しうるべく配
合し、生薬末又は生薬エキスは酵素の安定化を図るべく
配合し、生薬末又は生薬エキス並びに色素安定剤は色素
の安定化を図るべく配合し、かつ各配合成分の総合的作
用により保温1シ1を図るべく配合したものである。
The formulations in the above examples were designed to achieve the following effects. In other words, the two types of enzymes are formulated to maintain enhanced cleaning power when used in water (for skin cleansing and for cleaning bath residue) over a wide temperature range and a wide temperature range. The herbal medicine powder or herbal medicine extract is blended to stabilize enzymes, and the herbal medicine powder or herbal medicine extract and pigment stabilizer are blended to stabilize pigments. It was formulated to achieve this goal.

かかる目的の作用効果の証明として、上記実施例を4秤
の具体的な実施例に設定し、各作用効果について実験デ
ータをとった。
As a proof of the intended effect, the above-mentioned example was set as a specific example of four scales, and experimental data was collected for each effect.

また皮膚清浄化、洗濯水としての洗滌力の比較のために
動物の臓器より1qられる酵素としてのパンクレアチン
を除いた]ントロールAを設定するどJtに、微生物起
源の蛋白分解酵素としての△SPプロテアーピを除いた
コントロールBを設定した。
In addition, in order to compare the detergent power of skin cleansing and washing water, pancreatin, an enzyme derived from animal organs, was removed. Control B excluding Proteapi was set up.

また酵素安定化及び色素安定化の比較のために生薬末及
び生薬エキスを除いたコントロールCを設定した。
In addition, for comparison of enzyme stabilization and pigment stabilization, a control C was set in which crude drug powder and crude drug extract were excluded.

また色素安定化の比較のために生薬末及び生薬エキスな
らびに色素安定剤としてのジペンタエリ1−リット脂肪
酸エステルの両方を除いたコントロールDを設定すると
共に、色素安定剤を除いたコン1−ロール[を設定した
。各配合を表1に示す。
In addition, for comparison of dye stabilization, a control D was set up in which both herbal drug powder and herbal drug extract as well as dipentaeri 1-lit fatty acid ester as a dye stabilizer were removed, and Control D was set up in which both the herbal drug powder and herbal drug extract and dipentaeri 1-lit fatty acid ester as a dye stabilizer were removed. Set. Table 1 shows each formulation.

イ)皮膚清浄化及び風呂の残り渇を洗濯水に用いた場合
の洗滌力 所定の温度域及び所定のpl−1域におけるタンパク質
、脂肪、でんぷんの各々の分解力を酵素の相対活性及び
残存活性の比較により判定した。
b) Detergent power when the remaining thirst from skin cleansing and bathing is used as washing water The decomposition power of proteins, fats, and starches in a specified temperature range and a specified PL-1 range is determined by the relative activity and residual activity of enzymes. Judgment was made by comparing.

i)タンパク質の分解試験 植物起源蛋白分W?酵素配合の市販入浴剤と、二1ン1
〜ロールΔ並びに実施例1を比較するものであり、Hf
fa11定の方法は[アンソン−萩原氏変法」により、
1分間当りチロシン1/11に相当する呈色疫を示すも
のを1単位として行った。
i) Protein degradation test Plant-derived protein W? Commercial bath salts containing enzymes and 21-1
~Roll Δ and Example 1 are compared, and Hf
The fa11 method is based on [Anson-Hagiwara's modified method].
The test was carried out with one unit showing a color change corresponding to 1/11 of tyrosine per minute.

反応温度と活性測定結果を表2−1、グラフ2−1に、
反応p1−1と活性測定結果を表2−2、グラフ2−2
に、試別を水溶液とした際の残存活性測定結果を表2−
3、グラフ2−3にそれぞれ示しており、同データより
、実施例4、コント[1−ル△、市販入浴剤の順で広い
温度域において、又は広いpト1域において一定した高
い相対活性をそれぞれ示すと共に、同順で経過時間に対
して高い残存活性を示すことが確認された。
The reaction temperature and activity measurement results are shown in Table 2-1 and Graph 2-1.
Reaction p1-1 and activity measurement results are shown in Table 2-2 and Graph 2-2.
Table 2 shows the residual activity measurement results when the sample was made into an aqueous solution.
3. They are shown in graphs 2-3, and from the same data, it was found that Example 4, Control [1-L △, and commercially available bath additives] had a constant high relative activity in a wide temperature range or in a wide temperature range. It was confirmed that these compounds showed high residual activity over time in the same order.

従って市販入浴剤とコントロールAとの比較により、f
i動物源のタンパク分ill!r酵素に対して、微生物
起源のタンパク分解酵素であろΔSPプロテアーゼ、若
しくはASPプロテアーゼと生薬成分どの組合わせの配
合が、広い温度域、広いrlH域において一定した高い
相対活性を示すと其に、経過時間に対して一定した高い
残存活性を示すことが証明された。またコン1ヘロール
八と実施例4との比較ににす、ASPプロテアーゼ単独
よりも、これに動物のII器より得られる酵素であるパ
ンクレアチンを加えたもののほうがより広い湿度域、p
l−1taJにおいて一定した高い相対活性を示す共に
、経過時間に対して一定した高い残存活性を示すことが
証明された。
Therefore, by comparing commercially available bath additives and Control A, f
Ill protein from animal sources! ΔSP protease, which is a proteolytic enzyme of microbial origin, or a combination of ASP protease and crude drug ingredients shows a constant high relative activity over a wide temperature range and a wide rlH range. It was proven that it showed a constant and high residual activity over time. In addition, when comparing Con 1 Herol 8 and Example 4, it was found that ASP protease combined with pancreatin, an enzyme obtained from animal organ II, had a wider humidity range and p.
It was proved that it showed a constant high relative activity at l-1taJ and a constant high residual activity over time.

11)脂肪の分解試験 W)J物の臓器より得られる酵素配合の市販入浴剤と、
コントロールB並びに実施例4とを比較するものであり
、活性測定の方法は基質としてオリブ油を用い、リパー
ゼ作用によって′tL111シた脂肪酸をアルカリ滴定
で定晧し、その数値からリパーゼ活性をめた。
11) Fat decomposition test W) Commercially available bath additives containing enzymes obtained from J animal organs;
Control B and Example 4 were compared, and the activity was measured by using olive oil as a substrate and determining the fatty acid produced by lipase action by alkaline titration, and determining the lipase activity from the value. .

反応温度と活性測定結果を表3−1、グラフ3−1に、
反応01−1と活性測定結果を表3−2、グラフ3−2
に、水溶液とした際の残存活性測定結果を表3−3、グ
ラフ3−3にそれぞれ示しており、同データより実施例
4、コントロール81市販入浴剤の順で、広い温度域に
おいて、又は広いo l−1域において一定した高い相
対活性をそれぞれ示すと共に、同順で経過時間に対して
高い残存活性を示すことが確認された。
The reaction temperature and activity measurement results are shown in Table 3-1 and Graph 3-1.
Reaction 01-1 and activity measurement results are shown in Table 3-2 and Graph 3-2.
Table 3-3 and Graph 3-3 show the results of measuring the residual activity when made into an aqueous solution, respectively. From the same data, Example 4 and Control 81 commercially available bath additives were tested in order of activity in a wide temperature range or in a wide temperature range. It was confirmed that each showed a constant high relative activity in the o l-1 region, and also showed a high residual activity with respect to elapsed time in the same order.

従って、市販入浴剤とコン1ヘロールBとの比較により
、動物の臓器より得られる酵素であるパンクレアチン、
若しくはパンクレアチンと生薬成分との相合ゼの配合が
、広い渇i域、広いpf(域において一定した高い相対
活性を示寸ど共に、経過時間に対して一定した高い残存
活性を示すことが証明された。
Therefore, by comparing commercially available bath additives and Con 1 Herol B, we found that pancreatin, an enzyme obtained from animal organs,
Or, it has been proven that the combination of pancreatin and herbal medicine ingredients exhibits a constant high relative activity over a wide thirst range and a wide pf range, as well as a constant high residual activity over time. It was done.

またコントロールBと実施例4との比較にJ:す、パン
クレアチン単独よりも、これにΔSPプロテアーげを加
えたものの方が、より広い温度域、1)ト1域において
一定した高い相対活性を示すと共に、g過時間に対して
一定した高い残存活性を示すことが証明された。
In addition, a comparison between Control B and Example 4 showed that, compared to pancreatin alone, the product containing ΔSP protease had a constant high relative activity over a wider temperature range, 1) and 1). In addition, it was proven that the residual activity was constant and high over time.

iii )でんぷんの分解試験 動物の臓器にす1qられる酵素配合の市販入浴剤とコン
トロールB並びに実施例4を比較するものであり、活性
測定の方法は、基質として馬鈴薯でんぷんを用い、アミ
ラーゼ作用によるでんぷん中の直鎖成分(アミロース)
の低分子化に伴うヨウ素呈色を測定しアミラーゼ活性を
めた。
iii) Starch decomposition test This is a comparison of commercially available bath additives containing enzymes that are administered to the organs of animals, Control B, and Example 4. The activity measurement method is to use potato starch as a substrate and to decompose starch through the action of amylase. Straight chain component (amylose)
The amylase activity was determined by measuring the iodine coloration associated with the lowering of the molecular weight.

反応温度と活性測定結果を表4−1、グラフ4−1に、
反応p トIと活性測定結果を表4−2、グラフ4−2
に、水溶液どした際の残存活性測定結末を表4−3、グ
ラフ4−3にイれぞれ示しており、同データより、実施
例4、コントロール81市販入浴剤の順で広い温度域に
おいて、又は広いpH域において一定した高い相対活性
をそれぞれ示すと共に、同順で経過時間に対して高い残
存活性を示することが確認された。
The reaction temperature and activity measurement results are shown in Table 4-1 and Graph 4-1.
Table 4-2 and graph 4-2 show reaction p-I and activity measurement results.
Table 4-3 and Graph 4-3 show the results of residual activity measurement when dipping into an aqueous solution, respectively. From the same data, Example 4 and Control 81 commercially available bath additives were found to have a wide temperature range in that order. It was confirmed that they exhibited a constant high relative activity over a wide pH range, and a high residual activity over time in the same order.

従って、市販入浴剤とコントロールBとの比較により、
パンクレアチン、若しくはパンクレアチンと生薬成分と
の組合わせの配合が、広い温度域、広いpl、1域にJ
3いて一定した高い相対活性を示すと共に、経11;’
i変化に対して一定した高い残存′fA竹を示すことが
証明された。また、コントロールBと実施例4どの比較
により、パンクレアチン単独のものより、これにASP
プロテアーゼを加えたもののほうが広い温度域、pト1
域において一定した高い相対活性を示すと共に、経時変
化に対して一定した高い活性を示すことが証明されに0
口)酵素安定化 経過時間に対するタンパク質、脂肪、でんぷんの名々の
分解作用の残存活性の比較により判定した。
Therefore, by comparing commercially available bath additives and Control B,
The formulation of pancreatin or a combination of pancreatin and herbal medicine ingredients has a wide temperature range, wide PL, and J
3 shows a constant high relative activity, and 11;'
It was proved that the residual 'fA bamboo remained constant with respect to i changes. Also, the comparison between Control B and Example 4 showed that ASP was more effective in this than in pancreatin alone.
The one with protease added has a wider temperature range, pto1
It has been proven that it shows a constant high relative activity in the range, and also shows a constant high activity over time.
(1) Judgment was made by comparing the residual activities of the degrading activities of proteins, fats, and starches against the elapsed enzyme stabilization time.

i) タンパク分解作用の残存活性 コントロールDと実施例1乃至実施例4とを比較Jるも
のであり、活性測定の方法は前記タンパク質の分解試験
と同様である。保存温度が40℃の場合の残存活11を
表5−1、グラフ5−1に、保存湿度が室温の場合の残
存活ヤ1を表5−2、グラフ5−2にそれぞれ示してお
り、同データより0ずれの保存溜1僚においても、各実
施例が生薬成分を除いたコン1−〇−ルCに対して高い
残存活性を示していることが確z2された。
i) Residual activity of proteolytic activity Control D and Examples 1 to 4 are compared, and the method for measuring the activity is the same as in the protein degradation test described above. The remaining activity 11 when the storage temperature is 40°C is shown in Table 5-1 and graph 5-1, and the remaining activity 1 when the storage humidity is room temperature is shown in Table 5-2 and graph 5-2, respectively. From the same data, it was confirmed that even in the storage reservoir 1 group with a deviation of 0, each Example showed high residual activity against Con 1-0-C without herbal drug components.

従って、生薬成分が、タンパク分解作用の残存活ヤ1の
安定化、即ちASPプロアアーゼの安定化に寄りしてい
ることが証明された。
Therefore, it has been proven that the herbal medicine components are responsible for stabilizing the residual activity of proteolytic activity, that is, stabilizing ASP proase.

11) 脂肪分解作用の残存油t1 コントロールCと実施例1乃至実施例4とを比較するも
のであり、活性測定の方法(ま、前記脂肪分解試験と同
様である。
11) Residual oil t1 of lipolytic effect Control C and Examples 1 to 4 are compared, and the activity measurement method (well, the same as the lipolytic test described above).

保存渇麻が40℃の場合の残存活性を表6−1、グラフ
6−1に、保存湿度が室温の場合の残存活性を表6−2
、グラフ6−2にイれぞれ示しており、同データにより
、いずれの保存湿度【こお0ても、各実施例がコン1〜
ロールCに対して高し1残存活性を示していることが確
認された。従って生薬成分が脂肪分解作用の残存=fl
の安定化、OrIち)くンクレアザンの安定化に寄りし
ていることカー証明された。
Table 6-1 and graph 6-1 show the residual activity when the storage humidity is 40°C, and Table 6-2 shows the residual activity when the storage humidity is room temperature.
, are shown in graph 6-2, and based on the same data, each example is
It was confirmed that it showed a high residual activity of 1% against Roll C. Therefore, the herbal medicine ingredients still have a lipolytic effect = fl
It has been proven that the stabilization of OrI-kuncreazan is helpful.

iii ) でlυぶん分解作用の残存活性]ントロー
ルCと実施例1乃至実施例4とを比較するものであり、
活性測定の方法(ま1己でlνぷん分解試験と同様であ
る。
iii) The residual activity of lυ-degrading action] is compared between Control C and Examples 1 to 4,
The method for measuring activity (it is the same as the lv-particle decomposition test).

保存fA aが40℃の場合の残存活性を表7−1、グ
ラフ7−1に、保存温度が室温の場合の残存活性を表7
 ・−2、グラフ7−2に王ね5ぞれ示してd9す、同
データj二り、いずれの保存温度にお(、sでも各実施
例がコントロールCに対して高0残存活ftを示してい
ることが確認された。従って生薬成分がでんぷん分解作
用の残存活性の安定化、即ち、パンクレアチンの安定化
に寄与していることが確認された。
The residual activity when storage fA a is 40°C is shown in Table 7-1 and graph 7-1, and the residual activity when storage temperature is room temperature is shown in Table 7.
・-2, Graph 7-2 shows that each example has a high residual activity ft compared to control C at any storage temperature. Therefore, it was confirmed that the crude drug components contributed to stabilizing the residual activity of starch decomposition, that is, to stabilizing pancreatin.

ハ)色素安定化 コントロールC1コントロールD1コン1−ロールEと
実施例2とを比較し、経過時間に対18色素残存率にJ
、り判定するものであり、色素は黄色4舅及び(!!累
の中でも特に退色が著るしいとされる青色1@を用いて
実験を行い、保存温度も40℃という苛酷な条(’lと
した。m’l定方法は黄色4号は408川μ、青色1号
は630川μの最大吸収波長によってそれぞれの吸光度
を測定し色素残存率を測定しlこ 。
c) Dye stabilization control C1 control D1 control 1-Role E and Example 2 were compared, and the residual rate of dye J
The experiment was carried out using yellow 4-color and blue 1, which is said to be the most susceptible to discoloration among the pigments, and was stored under harsh conditions of 40℃. The m'l determination method was to measure the absorbance of each at the maximum absorption wavelength of 408 μ for Yellow No. 4 and 630 μ for Blue No. 1 to determine the dye residual rate.

経過時間に対ザる青色1舅の色素残存率の測定結果を表
8−1、グラフ8−1に、同じく黄色1舅の色素残存率
の測定結果を表8−2、グラフ8−2にそれぞれ示して
おり、同データより経過時間に対する青色1号の色素残
存率は実施例2、コン1〜〇−ル「1、コントロールD
1コン1ヘロールCの順に高い色素残存率を示すもので
あり、また黄色4F二の色素残存率も同順に高い色素残
存率を示すものである。
Table 8-1 and Graph 8-1 show the measurement results of the dye residual rate of the blue 1-year-old relative to the elapsed time, and Table 8-2 and Graph 8-2 show the measurement results of the dye residual rate of the yellow 1-year-old. From the same data, the dye residual rate of Blue No. 1 with respect to the elapsed time is shown in Example 2, Controls 1 to ○-1, Control D.
1 Con 1 Herol C shows the highest dye residual rate, and Yellow 4F2 also shows the highest dye residual rate in the same order.

従ってコン1〜ロールDどコン1−ロールCとの比較に
より、ジペンタエリトリット脂肪酸エステルが、色素安
定+!1に寄りし、またコン1へロールDと]ントロー
ルEとの比較により生薬成分が色素安定性に寄与し、ま
た、]ンI〜ロールC,D、Eと実施例2との比較によ
りジペンタエリトリット脂肪酸エステルと生薬成分との
双方を配合した場合のほうが更に優れた色素安定化を示
すことが証明された。
Therefore, by comparison with Con 1-Role D and Con 1-Role C, dipentaerythritol fatty acid ester is dye stable+! 1, and a comparison between Con1 Roll D and ] Control E shows that herbal ingredients contribute to dye stability, and a comparison of ] Control Rolls C, D, and E with Example 2 shows that It was proven that even better dye stabilization was achieved when both pentaerythritol fatty acid ester and crude drug ingredients were blended.

二)保温性 二種の市販入浴剤即ち酵素入り入浴剤a1生薬配合入浴
剤すと実施例4どを比較するものであり、健常者30名
を対象とIノで入浴前及び40± 1.0℃の温湯での
入浴後の身体の所定個所の皮膚表面温度を測定して平均
値をめ、温度変化を比較した。
2) Heat retention Two types of commercially available bath additives, namely enzyme-containing bath additive A1, herbal medicine-containing bath additive and Example 4, were compared, and 30 healthy people were tested before bathing and at 40 ± 1. After taking a bath in warm water at 0°C, the skin surface temperature of a predetermined part of the body was measured, the average value was calculated, and the temperature change was compared.

測定個所は親指の先端、人差し指の先端、指尖部丹示指
間、千の甲、耳朶とした。試験結甲は表9−(a)、9
−(h)、9−(c)、9−(d)、9− (c )の
通りである。
Measurement points were the tip of the thumb, the tip of the index finger, the tip of the finger, the back of the finger, and the earlobe. Test tubercles are Table 9-(a), 9
-(h), 9-(c), 9-(d), and 9-(c).

かかるデータより市販入浴剤の二種は、浴後00〜12
0分で、はぼ浴前値に復するのに比べ、本発明実施例4
では、浴後10〜20分で最高値となり、(の後も高い
保温↑11を絹持し、浴後120分になっても、指大部
用示指間では、1.3℃、耳朶でも1.4℃の差があり
、元に戻るのが近り、極めて高い保温性をli シ”C
いることが明らかになつ1c0従って、ASPプロテア
ーゼ、バンクレアチン、生薬成分等の配合によって高い
保澗ゼIを保有せしめられることが証明された。尚本発
明は上記実施例に限定されるものではなく、その配合量
もA(8)\プロテアーゼは4’−10%、バンクレア
チンはIfAlθ%、炭酸水素ナトリウムはZρ−7℃
%、IB化ナトリウムはρ、3〜/S%、生薬成分は4
A−/ρ%、ジベンタエリトツ1−脂Ilh酸エステル
はZ^3%程度であればよい。
Based on this data, two types of commercially available bath additives have a temperature of 0.00 to 12.0 after bathing.
Compared to the value returned to before the bath at 0 minutes, Example 4 of the present invention
The highest value was reached 10 to 20 minutes after bathing, and even after 120 minutes after bathing, the heat retention was 1.3℃ between the index fingers and 1.3℃ for the earlobe. There is a difference of 4℃, and the temperature will soon return to normal.
It has become clear that 1c0 is present in 1c0. Therefore, it has been proven that a high level of preservation I can be achieved by combining ASP protease, vancreatin, crude drug ingredients, etc. The present invention is not limited to the above examples, and the blending amounts are A(8)\protease at 4'-10%, vancreatin at IfAlθ%, and sodium hydrogen carbonate at Zρ-7°C.
%, IB sodium is ρ, 3~/S%, crude drug ingredients are 4
A-/ρ%, diventaerythritol 1-fatty Ilh acid ester may be about Z^3%.

本発明では、広いpト1域又は、広い温度域において均
一でかつ優れたタンパク分解力、脂肪分解力、でんぷん
分解力を保有でき、水質にJ:るp I−1の相違、使
用にJ、る’W IIJの相違にかかわらず、皮膚の清
浄化及び風呂の残り湯を洗)V水に使用する場合の洗滌
力を優れたものとすることができ、また配合色素の安定
11I及び酵素の安定性にも優れ、また保温効果ち優れ
た入浴剤を提供しうるという効果を奏する。
The present invention can maintain uniform and excellent proteolytic power, fat decomposition power, and starch decomposition power in a wide temperature range or in a wide temperature range, and can have a uniform and excellent proteolytic power, lipolytic power, and starch decomposition power in a wide temperature range, and can be used to improve water quality. Regardless of the difference in water, it can provide excellent cleaning power when used for skin cleansing and washing leftover hot water from a bath. It has the effect of providing a bath additive with excellent stability and heat retention effect.

” ”−’ # :zz!+#□□1jER;1llK
Aia[[Mニゲラフ2−1 タンパク分解作用の反応温度と活性測定結果相対活性(
5N) □実施例4 f′572−8 オッMacお2,6.ッ2.ウヵヵ□
□。イゆよ□、−。
” ”−'# :zz! +#□□1jER;1llK
Aia [[M Nigelaf 2-1 Reaction temperature and activity measurement results for proteolysis
5N) □Example 4 f'572-8 Oh Mac 2,6. 2. Ukaka□
□. Iyuyo□, -.

7”−1脂肪分解作用の反応ffi度と活性測定結果表
8−2 脂肪分解作用の反応PTTと活性測定結果相対活性(%
) 一−−−市販入浴剤 m−コントロールB □実施例4 % 表8−8 水い、I!1ゎおn6B’81力作□。工ゎ
性8,1果試Uil[:20 g/l 温度:40℃ 
1”’ニア、0表4−1 でんぷん分解作用の反応温度と活性測定結果相対活性(
%) 一−−−市販入浴剤 m−コノトロ1ルB 温度(℃) 相対活性(%) グ574−2 でんぷん分解作用の反応P■と活性測定
結宋−−−−市販入浴剤 一一コノドロールB □実施例4 表4−8 水溶液におけるでんぷん分解作用の残存活性測定結果試
料濃度: 20 gll m度:40’CP■:?、0
残存活性(96) グラフ4−8 表5−1 タンパク分解作用の残存活性率測定結果保存温度 40
℃ 保存温度 室温 タンパク分解作用の残存活性率測定結果グラフ5−1 グラフ5−2 1 °−’ nri肪分解作用の残存活性率。定結果保
存温度 室温 脂肪分解作用の残存活性率測定結果 グラフ6−1 グラフ6−2 表 7−1 でんぷん分解作用の残存活性率一定結果保
存温度 40℃ 保存温度 室温 でんぷん分解作用の残存活性率測定結果グラフ7−1 グラフ7−2 表S−を 青色1号 保存温度40℃ 黄色4号 保存温度40℃ 色票残存率測定゛結果 表 グラフ8−1 1
7”-1 Lipolysis reaction ffi degree and activity measurement results Table 8-2 Lipolysis reaction PTT and activity measurement results Relative activity (%
) 1---Commercial bath additive m-Control B □Example 4 % Table 8-8 Watery, I! 1ゎOn6B'81 masterpiece □. Workability 8.1 Fruit test Uil [: 20 g/l Temperature: 40℃
1"' Near, 0 Table 4-1 Reaction temperature and activity measurement results for starch decomposition action Relative activity (
%) 1---Commercial bath additive m-Conotrol B Temperature (℃) Relative activity (%) Gu574-2 Reaction P■ of starch decomposition action and activity measurement results Song---Commercial bath agent 11 Conodrol B □Example 4 Table 4-8 Measurement results of residual activity of starch decomposition in aqueous solution Sample concentration: 20 gll m degree: 40'CP■:? ,0
Residual activity (96) Graph 4-8 Table 5-1 Residual activity rate measurement results of proteolytic action Storage temperature 40
°C Storage temperature Room temperature Residual activity rate of proteolytic action Measurement results Graph 5-1 Graph 5-2 1 °-' Residual activity rate of nri lipolytic action. Constant result storage temperature Residual activity rate measurement result of room temperature lipolysis action Graph 6-1 Graph 6-2 Table 7-1 Residual activity rate of starch decomposition action Constant result storage temperature 40℃ Storage temperature Room temperature measurement of residual activity rate of starch decomposition action Result graph 7-1 Graph 7-2 Table S- Blue No. 1 Storage temperature 40℃ Yellow No. 4 Storage temperature 40℃ Color mark residual rate measurement ゛Result table Graph 8-1 1

Claims (1)

【特許請求の範囲】[Claims] 1) 微生物起源の蛋白分解酵素と、蛋白分解作用・脂
肪分解作用・でんぷん分解作用を右するパンクレアチン
等の動物の臓器より得られる酵素とニンジン末、シャク
ヤク末、゛]ウボク末、ヂンビ末等の生薬末或はAウバ
クエキス等の生薬エキスとを混合し、それに色素溶解剤
を介して色素を添加し、香料を混合して入浴剤を製造す
ることを特徴とする酵素入り入浴剤の製法。
1) Proteolytic enzymes originating from microorganisms, enzymes obtained from animal organs such as pancreatin that have proteolytic, lipolytic, and starch decomposing effects, and carrot powder, peony powder, ゛] uboku powder, jinbi powder, etc. A method for producing an enzyme-containing bath additive, which comprises mixing a crude drug extract such as a crude drug powder or A-ubaku extract, adding a pigment thereto via a pigment dissolving agent, and mixing a fragrance to produce a bath additive.
JP58215631A 1983-11-16 1983-11-16 Production of bath agent containing enzyme Granted JPS60109518A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP58215631A JPS60109518A (en) 1983-11-16 1983-11-16 Production of bath agent containing enzyme

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP58215631A JPS60109518A (en) 1983-11-16 1983-11-16 Production of bath agent containing enzyme

Publications (2)

Publication Number Publication Date
JPS60109518A true JPS60109518A (en) 1985-06-15
JPS6324973B2 JPS6324973B2 (en) 1988-05-23

Family

ID=16675599

Family Applications (1)

Application Number Title Priority Date Filing Date
JP58215631A Granted JPS60109518A (en) 1983-11-16 1983-11-16 Production of bath agent containing enzyme

Country Status (1)

Country Link
JP (1) JPS60109518A (en)

Cited By (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS6296416A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of enzyme-containing cleansing powder
JPS6296412A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of oxygen-containing bathing agent
JPS6296415A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of enzyme-containing cleansing powder
JPS6296414A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of enzyme-containing cleansing powder
JPS6296411A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of oxygen-containing bathing agent
JPS6296413A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production oxygen-containing bathing agent
JPS6299321A (en) * 1985-10-25 1987-05-08 Tadao Shiraishi Production of face washing powder containing enzyme
KR20000062042A (en) * 1999-03-30 2000-10-25 이창진 Aaaaa
JP2012158559A (en) * 2011-02-01 2012-08-23 Lion Corp Berberine-containing dentifrice composition, and stabilization method thereof

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WO2009034954A1 (en) 2007-09-13 2009-03-19 Asahi Glass Co., Ltd. TiO2-CONTAINING QUARTZ GLASS SUBSTRATE
TW200940472A (en) 2007-12-27 2009-10-01 Asahi Glass Co Ltd TiO2-containing silica glass
CN101978468B (en) 2008-03-18 2013-03-20 旭硝子株式会社 Reflective mask blank for EUV lithography and manufacture method thereof
JPWO2011068064A1 (en) 2009-12-01 2013-04-18 旭硝子株式会社 Silica glass containing TiO2
CN108060155A (en) * 2017-12-29 2018-05-22 舟山富晟食品科技有限公司 The protease extracted from squid viscera
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Cited By (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS6296416A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of enzyme-containing cleansing powder
JPS6296412A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of oxygen-containing bathing agent
JPS6296415A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of enzyme-containing cleansing powder
JPS6296414A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of enzyme-containing cleansing powder
JPS6296411A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production of oxygen-containing bathing agent
JPS6296413A (en) * 1985-10-23 1987-05-02 Tadao Shiraishi Production oxygen-containing bathing agent
JPS6299321A (en) * 1985-10-25 1987-05-08 Tadao Shiraishi Production of face washing powder containing enzyme
KR20000062042A (en) * 1999-03-30 2000-10-25 이창진 Aaaaa
JP2012158559A (en) * 2011-02-01 2012-08-23 Lion Corp Berberine-containing dentifrice composition, and stabilization method thereof

Also Published As

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