JPH0729899B2 - Manufacturing method of purified cosmetic ingredients - Google Patents
Manufacturing method of purified cosmetic ingredientsInfo
- Publication number
- JPH0729899B2 JPH0729899B2 JP62155232A JP15523287A JPH0729899B2 JP H0729899 B2 JPH0729899 B2 JP H0729899B2 JP 62155232 A JP62155232 A JP 62155232A JP 15523287 A JP15523287 A JP 15523287A JP H0729899 B2 JPH0729899 B2 JP H0729899B2
- Authority
- JP
- Japan
- Prior art keywords
- derivative
- hydrolyzed
- molecular weight
- hydrolyzed protein
- protein
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 238000004519 manufacturing process Methods 0.000 title claims description 7
- 239000008406 cosmetic ingredient Substances 0.000 title 1
- 102000004169 proteins and genes Human genes 0.000 claims description 29
- 108090000623 proteins and genes Proteins 0.000 claims description 29
- 239000002537 cosmetic Substances 0.000 claims description 21
- 102000011782 Keratins Human genes 0.000 claims description 11
- 108010076876 Keratins Proteins 0.000 claims description 11
- 244000068988 Glycine max Species 0.000 claims description 10
- 235000010469 Glycine max Nutrition 0.000 claims description 10
- 241000209140 Triticum Species 0.000 claims description 10
- 235000021307 Triticum Nutrition 0.000 claims description 10
- 239000012528 membrane Substances 0.000 claims description 9
- 239000002994 raw material Substances 0.000 claims description 7
- 238000000108 ultra-filtration Methods 0.000 claims description 7
- 238000001914 filtration Methods 0.000 claims 2
- 235000018102 proteins Nutrition 0.000 description 28
- 239000000243 solution Substances 0.000 description 15
- 238000001556 precipitation Methods 0.000 description 10
- 238000000034 method Methods 0.000 description 9
- 239000007864 aqueous solution Substances 0.000 description 8
- 102000008186 Collagen Human genes 0.000 description 5
- 108010035532 Collagen Proteins 0.000 description 5
- 229920001436 collagen Polymers 0.000 description 5
- 239000000047 product Substances 0.000 description 4
- 125000003277 amino group Chemical group 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 230000003301 hydrolyzing effect Effects 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 125000001453 quaternary ammonium group Chemical group 0.000 description 3
- -1 rechuculin Proteins 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- XDOFQFKRPWOURC-UHFFFAOYSA-N 16-methylheptadecanoic acid Chemical compound CC(C)CCCCCCCCCCCCCCC(O)=O XDOFQFKRPWOURC-UHFFFAOYSA-N 0.000 description 2
- 244000144725 Amygdalus communis Species 0.000 description 2
- 235000011437 Amygdalus communis Nutrition 0.000 description 2
- 102000016942 Elastin Human genes 0.000 description 2
- 108010014258 Elastin Proteins 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108010009736 Protein Hydrolysates Proteins 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 235000020224 almond Nutrition 0.000 description 2
- 239000012752 auxiliary agent Substances 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 229920002549 elastin Polymers 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 239000003531 protein hydrolysate Substances 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- XIUCEANTZSXBQQ-UHFFFAOYSA-N (3-chloro-2-hydroxypropyl)-trimethylazanium Chemical class C[N+](C)(C)CC(O)CCl XIUCEANTZSXBQQ-UHFFFAOYSA-N 0.000 description 1
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 239000005909 Kieselgur Substances 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108010064851 Plant Proteins Proteins 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical class OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 230000002862 amidating effect Effects 0.000 description 1
- 150000003863 ammonium salts Chemical class 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 239000003125 aqueous solvent Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002301 cellulose acetate Polymers 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000019864 coconut oil Nutrition 0.000 description 1
- 239000003240 coconut oil Substances 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 235000013312 flour Nutrition 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- AFEQENGXSMURHA-UHFFFAOYSA-N oxiran-2-ylmethanamine Chemical class NCC1CO1 AFEQENGXSMURHA-UHFFFAOYSA-N 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 235000021118 plant-derived protein Nutrition 0.000 description 1
- 229920002492 poly(sulfone) Polymers 0.000 description 1
- 229920002239 polyacrylonitrile Polymers 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920000098 polyolefin Polymers 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 229960001322 trypsin Drugs 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- LTVDFSLWFKLJDQ-UHFFFAOYSA-N α-tocopherolquinone Chemical compound CC(C)CCCC(C)CCCC(C)CCCC(C)(O)CCC1=C(C)C(=O)C(C)=C(C)C1=O LTVDFSLWFKLJDQ-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/20—Chemical, physico-chemical or functional or structural properties of the composition as a whole
- A61K2800/26—Optical properties
- A61K2800/262—Transparent; Translucent
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)
- Birds (AREA)
- Epidemiology (AREA)
- Dermatology (AREA)
- Cosmetics (AREA)
Description
【発明の詳細な説明】 ［産業上の利用分野］ 本発明は化粧料に原料として配合される大豆、小麦また
はケラチンの加水分解蛋白質またはその誘導体であっ
て、潜在的不溶化成分を除去したものの製法に関する。DETAILED DESCRIPTION OF THE INVENTION [Industrial field of application] The present invention is a method for producing a hydrolyzed protein of soybean, wheat or keratin or a derivative thereof which is blended as a raw material in a cosmetic composition, in which a potential insolubilizing component is removed. Regarding
［従来の技術・発明が解決しようとする問題点］ 化粧料に配合される加水分解蛋白質として、動物起源の
ものおよび植物起源のものが使用されている。[Problems to be Solved by Conventional Techniques and Inventions] As a hydrolyzed protein blended in cosmetics, those of animal origin and those of plant origin are used.
前記動物起源のものの具体例としては、コラーゲン、エ
ラスチン、レチュクリン、ケラチン、シルク、牛乳、鶏
卵などの蛋白質の加水分解物、また植物起源のものの具
体例としては、大豆、小麦、トウモロコシ、アーモンド
などの蛋白質の加水分解物が知られている（特開昭62−
53909号公報参照）。Specific examples of those of animal origin include collagen, elastin, rechuculin, keratin, silk, milk, protein hydrolysates such as eggs, and specific examples of those of vegetable origin include soybean, wheat, corn, almond, etc. Protein hydrolysates are known (Japanese Patent Application Laid-Open No. 62-
See 53909 publication).
これら化粧料配合用の加水分解蛋白質は、通常、水を主
体とする溶液（以下、水性溶液という）または乾燥固体
（粉末）として市場に供給されているが、固体のばあい
でも化粧料に配合されるときには水性溶液として使用さ
れることが多い。これらの水性溶液は化粧料の均一性を
維持し、また商品価値を高めるため、長期間保存しても
透明で、曇り、にごり、沈澱などの生じないことが必要
である。さらにこれを配合した化粧料においても、とく
にその化粧料が透明な製品であるばあいには、長期間透
明であることが要求される。These hydrolyzed proteins for blending cosmetics are usually supplied to the market as a solution mainly composed of water (hereinafter referred to as an aqueous solution) or as a dry solid (powder). Often used as an aqueous solution. In order to maintain the uniformity of cosmetics and enhance the commercial value of these aqueous solutions, it is necessary that they are transparent and do not cause cloudiness, turbidity, precipitation or the like even after long-term storage. Further, also in the cosmetics containing the same, it is required that the cosmetics be transparent for a long period of time, especially when the cosmetics are transparent products.
しかし、従来市場に供給されている加水分解蛋白質また
はその誘導体は、製造時に過された際には透明なもの
でも、１〜６カ月程度保存すれば曇り、にごりなどが生
じ、６カ月〜１年以上保存すれば沈澱が生じるものが多
く、化粧料原料としての商品価値も下り、化粧料に配合
するにも制限のあるものである。However, even if the hydrolyzed protein or its derivative that has been supplied to the market in the past is transparent even when it is passed through the manufacturing process, it will become cloudy and turbid if it is stored for about 1 to 6 months, and it will last for 6 months to 1 year. Preservation as described above often causes precipitation, which lowers the commercial value as a raw material for cosmetics and limits its incorporation into cosmetics.
このようなにごり、沈澱などが生じる現象は、一般に加
水分解蛋白質の平均分子量が大きい程著しく、また植物
性蛋白質およびケラチン起源のものがコラーゲンなどを
起源とするものより著しいことが知られている。It is known that the phenomenon in which such turbidity and precipitation occur is generally more pronounced as the average molecular weight of the hydrolyzed protein is higher, and that those of vegetable protein and keratin origin are more significant than those of collagen origin.
このにごり、沈澱などは過すればその時点では透明に
なるが、１〜６カ月経過すればまた発生し、再び過し
てもまた発生し、際限がなく、根本的に長期間透明を維
持しうる加水分解蛋白質またはその誘導体を製造するこ
とは非常に困難である。If there is turbidity, precipitation, etc., it becomes transparent at that time, but it will occur again after 1 to 6 months, and it will occur again even if it passes again, there is no end, and basically it remains transparent for a long time. It is very difficult to produce a hydrolyzed protein or its derivative.
このようなにごり、沈澱などの問題を解決するために加
水分解蛋白質をその誘導体に変えたもの、たとえば加水
分解蛋白質を３−クロロ−２−ヒドロキシプロピルトリ
メチルアンモニウム塩との反応によって４級アンモニウ
ム誘導体にしたもののばあいにも、必ずしも前記問題を
解決しうるのばかりではなく、充分満足のいく効果のえ
られるものではないのが実状である。In order to solve the problems such as turbidity and precipitation, hydrolyzed protein is changed to its derivative, for example, hydrolyzed protein is converted into a quaternary ammonium derivative by reaction with 3-chloro-2-hydroxypropyltrimethylammonium salt. However, the fact is that not only can the problem be solved, but the satisfactory effect cannot be obtained.
なお、天然の蛋白質を加水分解させる方法としては、
酸、アルカリまたは蛋白質酵素により加水分解する方法
が知られている。As a method of hydrolyzing natural proteins,
A method of hydrolyzing with an acid, an alkali or a protein enzyme is known.
［問題点を解決するための手段］ 本発明は前記のごとき加水分解蛋白質またはその誘導体
を水性溶液として保存したばあいに生じる頑固なにご
り、沈澱などの問題を解決するためになされたものであ
り、大豆、小麦またはケラチンの加水分解蛋白質および
（または）その誘導体溶液を分画分子量2000〜200,000
の限外過膜で過し、潜在的不溶化成分を除去するも
とを特徴とする精製された化粧料原料の製法に関する。[Means for Solving Problems] The present invention has been made to solve the problems such as stubborn turbidity and precipitation that occur when the hydrolyzed protein or its derivative as described above is stored as an aqueous solution. , Soybean, wheat or keratin hydrolyzed protein and / or its derivative solution fractionated molecular weight 2000-200,000
The method for producing a purified cosmetic raw material, which is characterized by removing a latent insolubilized component after passing through the ultra-permeation membrane.
［実施例］ 本発明における大豆、小麦またはケラチンの加水分解蛋
白質およびその誘導体溶液とは、従来より化粧料原料と
して使用されている大豆、小麦またはケラチンの加水分
解蛋白質およびその誘導体溶液のことであり、化粧料原
料として使用しうるものである限りとくに限定はない。[Examples] The hydrolyzed protein of soybean, wheat or keratin and its derivative solution in the present invention means the hydrolyzed protein of soybean, wheat or keratin and its derivative solution which have been conventionally used as a raw material for cosmetics. There is no particular limitation as long as it can be used as a cosmetic raw material.
大豆、小麦またはケラチンの加水分解蛋白質の誘導体溶
液の例としては、加水分解蛋白質のアミノ基をイソステ
アリン酸のごとき脂肪酸でアミド化したもの、たとえば
加水分解蛋白質のアミノ基の水素原子をグリシジルアン
モニウム塩のごとき４級アンモニウム化剤と反応させて
できるアンモニウム塩誘導体などの溶液があげられる
（特公昭62−8401号公報参照）。Examples of the hydrolyzed protein derivative solution of soybean, wheat or keratin include those obtained by amidating the amino group of hydrolyzed protein with a fatty acid such as isostearic acid, for example, the hydrogen atom of the amino group of hydrolyzed protein of glycidyl ammonium salt. Examples thereof include solutions of ammonium salt derivatives formed by reacting with a quaternary ammonium agent (see Japanese Examined Patent Publication No. 62-8401).
上記のごとき加水分解蛋白質やその誘導体溶液は、通
常、酸やアルカリ、さらにはペブシン、パパイン、トリ
プシンなどの各種菌起源の蛋白分解酵素により動物性や
植物性の蛋白質を常法により加水分解することにより、
さらにはえられた加水分解物を４級化などすることによ
りえられる。The hydrolyzed protein or its derivative solution as described above is usually prepared by hydrolyzing an animal or plant protein by a conventional method with a proteolytic enzyme of various fungal origin such as acid, alkali, pepsin, papain or trypsin. Due to
Further, it can be obtained by quaternizing the obtained hydrolyzate.
本明細書にいう潜在的な不溶化成分とは、加水分解蛋白
質および（または）その誘導体を一度過したものを、
そのまままたは化粧料に配合して透明な化粧料を製造し
て保存しておくと、経時的に不溶化して曇りや沈澱など
の原因になる成分のことである。本発明者らの研究の結
果、この成分は主として加水分解によって充分分解しな
かった分子量の高い成分からなり、一時的に水を主体と
する溶媒に溶解しても会合などにより経時的に不溶化す
る成分であることが判明している。この不溶化現象は、
保存の時間、温度、pH、平均分子量、他成分の存在など
によって影響され、そのしくみは複雑で充分解明されて
いないが、いずれにしても加水分解蛋白質および（また
は）その誘導体の溶液を限外過することにより潜在的
不溶化成分の多くを除去しうる。もちろん、この限外
過によって顕在不溶成分（曇り、沈澱などとして目に見
える成分）も同時に除去しうるが、これは通常の過
（たとえば過助剤と紙による過）によっても除去
できる。The term “potential insolubilizing component” as used herein means a substance which has once passed through a hydrolyzed protein and / or its derivative,
It is a component which becomes insoluble over time and causes clouding or precipitation when a transparent cosmetic is manufactured and stored as it is or in a cosmetic composition. As a result of the research conducted by the present inventors, this component is mainly composed of a component having a high molecular weight that was not sufficiently decomposed by hydrolysis, and even if it is temporarily dissolved in a solvent mainly composed of water, it becomes insoluble over time due to association or the like. It is known to be an ingredient. This insolubilization phenomenon is
The mechanism is complicated and not fully clarified because it is affected by storage time, temperature, pH, average molecular weight, presence of other components, etc., but in any case, the solution of hydrolyzed protein and / or its derivative is limited. Most of the potentially insolubilized components can be removed by passing. Of course, this ultrafiltration can simultaneously remove the apparently insoluble components (the components visible as haze, precipitation, etc.), but they can also be removed by the usual excess (for example, with a super-auxiliary agent and paper).
本発明に使用する限外過膜の分画分子量（排除限界分
子量）は2,000〜200,000のものであり、10,000〜100,00
0程度のものがとくに好ましい。なお限外過膜と称し
ていなくても上記分画分子量を有する膜は本発明におけ
る限外過膜の概念に含まれるものである。The molecular weight cut-off (exclusion limit molecular weight) of the ultrapermeabilizer used in the present invention is 2,000 to 200,000, and 10,000 to 100,00.
Those of about 0 are particularly preferable. It should be noted that a membrane having the above-mentioned molecular weight cut-off is included in the concept of "ultra-supermembrane" in the present invention even though it is not called "ultra-supermembrane".
前記分画分子量が2000未満のように小さくなり過ぎる
と、通過時間が長く収率が低下するとともに、限外過
物の感触がねばりの小さいものになる。また分画分子量
が200,000をこえると、潜在不溶成分の除去が充分でな
くなる。実際には個々の加水分解蛋白質および（また
は）その誘導体について、通過速度、収率、限外過物
の不溶物析出安定性などを見て適した限外過膜を選ん
で使用するのが好ましい。If the molecular weight cutoff is too small, such as less than 2000, the passage time will be long and the yield will be low, and the feel of the ultrapure product will be less sticky. When the molecular weight cutoff exceeds 200,000, the latent insoluble component is not sufficiently removed. In practice, it is preferable to select and use an appropriate ultrafiltration membrane for each hydrolyzed protein and / or its derivative in view of the passage rate, yield, stability of insoluble matter precipitation of ultrafiltration products, etc. .
限外過膜を構成する材質にはとくに限定はなく、たと
えばポリスルホン、ポリアクリロニトリル、ポリエチレ
ン系ポリマー、親水性ポリオレフィン、セルローズ、酢
酸セルローズなど、通常限外過膜を形成するのに使用
される材質であれば限定なく使用しうるが、水系の溶媒
を使用するばあいには親水性の材質であるのが好まし
い。There is no particular limitation on the material constituting the ultra-supermembrane, for example, polysulfone, polyacrylonitrile, polyethylene-based polymer, hydrophilic polyolefin, cellulose, cellulose acetate, etc., which are usually used for forming the ultra-supermembrane. Any material can be used without limitation, but when an aqueous solvent is used, it is preferably a hydrophilic material.
限外過膜の形状にもとくに限定はなく、たとえば平
膜、プリーツ、スパイラル、チューブ、中空糸など、各
種形状のものが使用されうる。The shape of the ultrapermeable membrane is not particularly limited, and various shapes such as flat membranes, pleats, spirals, tubes and hollow fibers can be used.
加水分解蛋白質の誘導体溶液の潜在的不溶化成分を除去
するばあい、加水分解蛋白質溶液の状態で限外過膜を
通過させ、そののち誘導体にしてもよく、誘導体にして
から限外過膜を通過させてもよい。When removing the potential insolubilized components of the hydrolyzed protein derivative solution, the hydrolyzed protein solution may be passed through the ultrapermeabilization membrane and then made into a derivative, or after being made into a derivative, passed through the ultrahypermembrane. You may let me.
限外過の条件にはとくに限定はなく、通常の条件、た
とえば40％（重量％、以下、同様）以下、好ましくは10
〜30％の濃度の加水分解蛋白質および（または）その誘
導体溶液を50〜60℃以下の温度、１〜5kg/cm2・Ｇのご
とき条件が採用される。There is no particular limitation on the conditions of the ultra-passage, and normal conditions such as 40% (wt%, hereinafter, the same) or less, preferably 10
Conditions of a hydrolyzed protein and / or its derivative solution having a concentration of -30% at a temperature of 50-60 ° C or less and 1-5 kg / cm 2 · G are adopted.
化粧料に配合するための加水分解蛋白質および（また
は）その誘導体が市場に供給されるばあい、乾燥固体
（粉末）の形状のものも多いが、このばあいには乾燥固
形化する前の溶液状態で本発明の方法を実施しておけ
ば、乾燥固体を溶液にする際に溶解させやすく、不溶分
が生じ難くなり有効であるが、限外過していない乾燥
固体を溶解させてから限外過しても同様の効果がえら
れる。When a hydrolyzed protein and / or its derivative for incorporation into cosmetics is supplied to the market, it is often in the form of a dry solid (powder), but in this case, it is a solution before being dried and solidified. If the method of the present invention is carried out in a state, it is effective when the dried solid is dissolved into a solution, and insoluble matter is less likely to occur, which is effective. The same effect can be obtained even if you go outside.
本発明における化粧料とは、薬事法にいう化粧品、医薬
部外品、医薬品のいずれに含まれるものであってもよ
く、化粧に使用する調合品である限り本発明の化粧料の
概念に含まれる。The cosmetics in the present invention may be contained in any of cosmetics, quasi drugs, and pharmaceuticals referred to in the Pharmaceutical Affairs Law, and are included in the concept of the cosmetics of the present invention as long as they are preparations used for makeup. Be done.
つぎに本発明の方法を実施例に基づき、さらに詳細に説
明する。Next, the method of the present invention will be described in more detail based on examples.
実施例１〜５および比較例１〜２ 脱脂大豆粉を水中で酵素によって加水分解したのち過
助剤（珪藻土）と紙とを使用して過し、平均分子量
約4000の透明な加水分解蛋白質の水溶液（濃度20％）を
えた。えられた水溶液を温度30℃、圧力3kg/cm2で第１
表に示す６種の限外過膜を用いて限外過し、６種の
限外過液をえた。Examples 1 to 5 and Comparative Examples 1 to 2 Defatted soybean flour was hydrolyzed with an enzyme in water, and then passed through a super-auxiliary agent (diatomaceous earth) and paper to obtain a transparent hydrolyzed protein having an average molecular weight of about 4000. An aqueous solution (concentration 20%) was obtained. The obtained aqueous solution is firstly heated at a temperature of 30 ° C and a pressure of 3 kg / cm 2 .
Ultrafiltration was performed using the 6 types of ultrapermeability membranes shown in the table, and 6 types of ultrapermeability were obtained.
えられた水溶液および限外過液それぞれの濃度、製造
直後、１カ月後および６カ月後の色調（ガードナーナン
バー）、ならびに透明性（目視観察）を調べた。結果を
第１表に示す。The concentration of each of the obtained aqueous solution and ultrafiltration solution, the color tone (Gardner number) immediately after the production, and one month and six months later, and the transparency (visual observation) were examined. The results are shown in Table 1.
第１表の結果から、本発明の方法により製造したものは
６カ月間保存後も曇りや沈澱が生じず、色調も淡く、優
れていることがわかる。 From the results shown in Table 1, it can be seen that the product manufactured by the method of the present invention is excellent in that it does not cause clouding or precipitation even after being stored for 6 months and has a light color tone.
実施例６〜７、参考例１〜６および比較例３〜10 下記Ａ〜Ｈの加水分解蛋白質およびその誘導体の15％水
性溶液それぞれの通常過物を、実施例３で用いた限外
過膜（分画分子量50,000）を使用して、温度25℃、圧
力3.5kg/cm2で限外過した。えられた限外過液およ
び通常過物それぞれの製造直後、１カ月後および６カ
月後の透明性を比較した。結果を第２表に示す。なお全
サンプルに防腐剤としてフェノニップ（ニパラボラトリ
ース社製）を0.3％添加した。Examples 6 to 7, Reference Examples 1 to 6 and Comparative Examples 3 to 10 The ultrafiltration membranes used in Example 3 were the usual impurities of each of the following 15% aqueous solutions of hydrolyzed proteins of A to H and their derivatives. (Fraction molecular weight 50,000) was used, and the temperature was 25 ° C. and the pressure was 3.5 kg / cm 2 . The obtained ultraperfusate and normal perfusate were compared in transparency immediately after the production, after 1 month, and after 6 months. The results are shown in Table 2. In addition, 0.3% of phenonip (manufactured by Nipara Laboratories) was added as a preservative to all samples.
A:加水分解コラーゲン（平均分子量10,000） B:加水分解ケラチン（平均分子量200） C:加水分解エラスチン（平均分子量3000） D:加水分解シルク（平均分子量1000） E:加水分解小麦蛋白質（平均分子量150） F:加水分解アーモンド蛋白質（平均分子量2000） G:Aの加水分解コラーゲンに３−クロロ−２−ヒドロキ
シプロピルトリメチルアンモニウムクロライドを反応さ
せて合成した４級アンモニウム誘導体（平均分子量1200
0） H:Aの加水分解コラーゲンのアミノ基をヤシ油脂肪酸ア
ミド化し、トリエタノールアミン塩としたもの（平均分
子量600） 第２表の結果からも本発明の方法が有効であることがわ
かる。A: Hydrolyzed collagen (average molecular weight 10,000) B: Hydrolyzed keratin (average molecular weight 200) C: Hydrolyzed elastin (average molecular weight 3000) D: Hydrolyzed silk (average molecular weight 1000) E: Hydrolyzed wheat protein (average molecular weight 150) ) F: hydrolyzed almond protein (average molecular weight 2000) G: quaternary ammonium derivative synthesized by reacting 3-chloro-2-hydroxypropyltrimethylammonium chloride with hydrolyzed collagen (average molecular weight 1200
0) Amino group of H: A hydrolyzed collagen was converted to coconut oil fatty acid amid to form triethanolamine salt (average molecular weight 600) The results in Table 2 also show that the method of the present invention is effective.
［発明の効果］ 本発明の方法によらない大豆、小麦またはケラチンの加
水分解蛋白質および（または）その誘導体溶液は、初め
透明であっても１カ月で少し沈澱し、６カ月で多量に沈
澱する。この現象は透明化粧料に配合したばあいにも生
ずる。[Effects of the Invention] The hydrolyzed protein solution of soybean, wheat or keratin and / or its derivative solution which is not produced by the method of the present invention slightly precipitates in one month and a large amount in 6 months even if it is initially transparent. . This phenomenon also occurs when blended with transparent cosmetics.
しかし、大豆、小麦またはケラチンの加水分解蛋白質お
よび（または）その誘導体溶液から本発明の方法により
潜在的不溶化成分を除去した化粧料原料は、長期間（た
とえば６カ月）経過後も曇り、沈澱などを生じることな
く透明である。そのうえ、その色調も本発明の方法を適
用しないものと比べて明らかに淡色であり、優れてい
る。However, the cosmetic raw material obtained by removing the potential insolubilizing component from the solution of hydrolyzed protein of soybean, wheat or keratin and / or its derivative by the method of the present invention becomes cloudy or precipitates even after a long time (for example, 6 months). It is transparent without causing. Moreover, its color tone is also clearly lighter than that to which the method of the present invention is not applied, which is excellent.
Claims (1)
質及び（または）その誘導体溶液を分画分子量2000〜20
0,000の限外濾過膜で濾過し、潜在的不溶化成分を除去
することを特徴とする精製された化粧料原料の製法。1. A soybean, wheat or keratin hydrolyzed protein and / or its derivative solution is fractionated to a molecular weight of 2000 to 20.
A method for producing a purified cosmetic raw material, which comprises filtering a latent insolubilized component by filtration through an ultrafiltration membrane of 0000.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP62155232A JPH0729899B2 (en) | 1987-06-22 | 1987-06-22 | Manufacturing method of purified cosmetic ingredients |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP62155232A JPH0729899B2 (en) | 1987-06-22 | 1987-06-22 | Manufacturing method of purified cosmetic ingredients |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JPS6411A JPS6411A (en) | 1989-01-05 |
| JPH0111A JPH0111A (en) | 1989-01-05 |
| JPH0729899B2 true JPH0729899B2 (en) | 1995-04-05 |
Family
ID=15601420
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP62155232A Expired - Fee Related JPH0729899B2 (en) | 1987-06-22 | 1987-06-22 | Manufacturing method of purified cosmetic ingredients |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0729899B2 (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0528321Y2 (en) * | 1988-09-30 | 1993-07-21 | ||
| EP0457565B1 (en) * | 1990-05-18 | 1997-07-30 | Morinaga Milk Industry Co., Ltd. | Milk-protein hydrolyzates and compositions for use as hair and skin treating agent |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS506704A (en) * | 1973-05-30 | 1975-01-23 | ||
| FR2538683B3 (en) * | 1982-12-30 | 1985-12-13 | Goemar Lab Sa | HIGH NUTRITIVE VALUE BEVERAGES CONTAINING CERTAIN ALGAE EXTRACTS AND CORRESPONDING ADDITIVES |
| JPS6236308A (en) * | 1985-08-12 | 1987-02-17 | Kishiyuu Sangyo Kk | Cosmetic compounded with liquid composition containing hydrolyzed sericin |
| JPS62185100A (en) * | 1986-02-10 | 1987-08-13 | Ichimaru Fuarukosu Kk | Casein for compounding to cosmetic and cosmetic containing same |
| JPS62221612A (en) * | 1986-03-25 | 1987-09-29 | Mikimoto Seiyaku Kk | Production of cosmetic material |
-
1987
- 1987-06-22 JP JP62155232A patent/JPH0729899B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6411A (en) | 1989-01-05 |
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