JPH0111A - Manufacturing method for refined cosmetic raw materials - Google Patents
Manufacturing method for refined cosmetic raw materialsInfo
- Publication number
- JPH0111A JPH0111A JP62-155232A JP15523287A JPH0111A JP H0111 A JPH0111 A JP H0111A JP 15523287 A JP15523287 A JP 15523287A JP H0111 A JPH0111 A JP H0111A
- Authority
- JP
- Japan
- Prior art keywords
- hydrolyzed
- molecular weight
- proteins
- cosmetics
- derivatives
- 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
- 239000002537 cosmetic Substances 0.000 title claims description 23
- 239000002994 raw material Substances 0.000 title claims description 8
- 238000004519 manufacturing process Methods 0.000 title claims description 6
- 102000004169 proteins and genes Human genes 0.000 claims description 33
- 108090000623 proteins and genes Proteins 0.000 claims description 33
- 238000000108 ultra-filtration Methods 0.000 claims description 17
- 239000012528 membrane Substances 0.000 claims description 15
- 238000001914 filtration Methods 0.000 claims description 6
- 239000000243 solution Substances 0.000 description 15
- 238000000034 method Methods 0.000 description 10
- 238000001556 precipitation Methods 0.000 description 8
- 102000008186 Collagen Human genes 0.000 description 7
- 108010035532 Collagen Proteins 0.000 description 7
- 239000007864 aqueous solution Substances 0.000 description 7
- 229920001436 collagen Polymers 0.000 description 7
- 239000000047 product Substances 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000007787 solid Substances 0.000 description 4
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 3
- 102000011782 Keratins Human genes 0.000 description 3
- 108010076876 Keratins Proteins 0.000 description 3
- 125000003277 amino group Chemical group 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 230000003301 hydrolyzing effect Effects 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 238000003860 storage Methods 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
- 102000016942 Elastin Human genes 0.000 description 2
- 108010014258 Elastin Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 244000068988 Glycine max Species 0.000 description 2
- 235000010469 Glycine max Nutrition 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 241000209140 Triticum Species 0.000 description 2
- 235000021307 Triticum Nutrition 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 235000020224 almond Nutrition 0.000 description 2
- 230000000052 comparative effect Effects 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
- 239000000706 filtrate Substances 0.000 description 2
- 125000001453 quaternary ammonium group Chemical group 0.000 description 2
- -1 rechuculin Proteins 0.000 description 2
- 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 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
- 235000011437 Amygdalus communis Nutrition 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 241000287828 Gallus gallus Species 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
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000004365 Protease Substances 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
- 150000007513 acids Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 230000002862 amidating effect Effects 0.000 description 1
- 150000003863 ammonium salts Chemical class 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
- 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
- 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
- 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
- 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
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229960001322 trypsin Drugs 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Abstract
(57)【要約】本公報は電子出願前の出願データであるた
め要約のデータは記録されません。(57) [Summary] This bulletin contains application data before electronic filing, so abstract data is not recorded.
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 Application Field] The present invention relates to a method for producing a hydrolyzed protein or a derivative thereof which is used as a raw material in cosmetics, from which potentially insolubilized components have been removed.
[従来の技術・発明が解決しようとする問題点化粧料に
間合される加水分解、蛋白質として1、 、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 the Prior Art and Inventions] As hydrolyzed proteins used in cosmetics, 1. Proteins 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へ解物、また植物起源のものの
具体例としては、大豆1、 ・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)゛
。゛
これら化粧料に台用゛蕊加水分解蛋白質は、通 ゛さ
れているが、固体のばあいでも化粧料に配合 。Specific examples of the animal-derived products include hydrolyzates of proteins such as collagen, elastin, rechuculin, keratin, silk, milk, and chicken eggs, and specific examples of the plant-derived products include soybean 1, wheat, and corn. ,
Hydrolysates of proteins such as almonds are known (see JP-A-62-53909). Hydrolyzed proteins are commonly used in these cosmetics, but they are also incorporated into cosmetics even in solid form.
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、長期側保存して、も透明で、曇
り、にごり、沈澱な(!:′oi ’。When used, it is often used as an aqueous solution. These aqueous solutions maintain the uniformity of cosmetics and increase their commercial value, so they remain transparent, cloudy, cloudy, and precipitated even after long-term storage.
じないことが必要で凪る゛。さらにこれを配合し゛た化
粧料においても1.とくにその化粧料が透明 −なy品
下あるばあいには、4長“期間、透明Fあることが要求
される。“
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、製造時に濾過された際には透明なもの
でも、1〜6力月程度保存すれば曇り、にごりなどが生
じ、6力月〜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。I need something to calm down. Furthermore, in cosmetics containing this, 1. Particularly in cases where the cosmetic is a transparent product, it is required to remain transparent for a long period of time. Even if it is clear when filtered, it becomes cloudy or cloudy if stored for 1 to 6 months, and often forms a precipitate if stored for 6 months to 1 year or more, making it difficult to use as a raw material for cosmetics. Its commercial value has also declined, and there are restrictions on its inclusion in cosmetics.
このようなにごり、沈澱などが生じる現象は、−m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 of cloudiness, precipitation, etc. is more pronounced as the average molecular weight of the hydrolyzed protein is larger, and that it is more pronounced for proteins originating from vegetable proteins and keratin than for those originating from collagen, etc. There is.
このにごり、沈澱などは濾過すればその時点では透明に
なるが、1〜6力月経過すればまた発生し、再び濾過し
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。This cloudiness and precipitate become transparent when filtered, but they reappear after 1 to 6 months, and even after filtration, they reappear, and there is no limit to this, and fundamentally they remain transparent for a long time. It is very difficult to produce hydrolyzed proteins or derivatives thereof.
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
解決しうるちのばかりではなく、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 problems such as cloudiness and precipitation, hydrolyzed proteins are converted into derivatives, for example, hydrolyzed proteins are converted into quaternary ammonium derivatives by reaction with 3-chloro-2-hydroxypropyltrimethylammonium salt. The reality is that even in the cases where such methods are used, they are not necessarily able to solve the above-mentioned problems, and they do not always produce sufficiently satisfactory effects.
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分解酵素により加水分解する方法
が知られている。Note that as a method of hydrolyzing natural proteins, methods of hydrolyzing with acid, alkali, or proteolytic enzyme are 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
、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の限外濾過膜でン濾
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に関する。[Means for Solving the Problems] The present invention has been made in order to solve the problems such as stubborn cloudiness and precipitation that occur when hydrolyzed proteins or derivatives thereof as described above are stored as an aqueous solution. A method for producing a purified cosmetic raw material, which comprises filtering a solution of a hydrolyzed protein and/or its derivative through an ultrafiltration membrane having a molecular weight cutoff of 2000 to 200,000 to remove potentially insolubilized components. Regarding.
[実施例]
本発明における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
として使用しうるちのである限りとくに限定はない。[Example] The hydrolyzed protein and its derivative solution in the present invention refers to a hydrolyzed protein and its derivative solution that has been conventionally used as a cosmetic raw material, and as long as it can be used as a cosmetic raw material. There are no particular limitations.
このような加水分解蛋白質およびその誘導体溶液の具体
例としては、[従来の技術・発明が解決しようとする問
題点コの項に記載したような動物性や植物性の蛋白質の
加水分解物およびその誘導体の溶液があげられる。加水
分解蛋白質の誘導体溶液の前記以外の例としては、たと
えばイソステアリン酸でアミド化した加水分解コラーゲ
ンのごとき加水分解蛋白質のアミノ基を脂肪酸でアミド
化したもの、たとえばグリシジルアンモニウム塩と加水
分解コラーゲンとを反応させてできる誘導体のごときア
ミノ基の水素原子を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82−8401号公報参照)。Specific examples of such solutions of hydrolyzed proteins and their derivatives include animal and vegetable protein hydrolysates and their Examples include solutions of derivatives. Examples of derivative solutions of hydrolyzed proteins other than those mentioned above include solutions in which the amino groups of hydrolyzed proteins are amidated with fatty acids, such as hydrolyzed collagen amidated with isostearic acid, such as glycidylammonium salts and hydrolyzed collagen. Examples include solutions such as ammonium salt derivatives made by reacting the hydrogen atoms of amino groups with quaternary ammonium-forming agents.
(See Japanese Patent Publication No. 82-8401).
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、さらにはペプシン、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 above-mentioned solutions of hydrolyzed proteins and their derivatives are usually produced by hydrolyzing animal or vegetable proteins using acids, alkalis, or proteolytic enzymes derived from various bacteria such as pepsin, papain, and trypsin. Furthermore, 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)その誘導体を一度濾過したものを、
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、−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、pH1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ン濾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
外濾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、これは通常の濾
過(たとえば濾過助剤とン戸紙によるン濾過)によって
も除去できる。The potential insolubilized components referred to herein refer to hydrolyzed proteins and/or derivatives thereof that have been filtered once;
When transparent cosmetics are manufactured and stored as they are or mixed into cosmetics, they become insolubilized over time and cause cloudiness and precipitation. As a result of the research conducted by the present inventors, this component mainly consists of high molecular weight components that were not sufficiently decomposed by hydrolysis; It has been found that it is a component that This insolubilization phenomenon is
The mechanism is complex and has not been fully elucidated, as it is affected by storage time, temperature, pH average molecular weight, presence of other components, etc., but in any case, a solution of hydrolyzed protein and/or its derivatives is Filtration may remove many potentially insolubilized components. Of course, this ultrafiltration also removes visible insoluble components (components visible as cloudiness, precipitates, etc.), which can also be removed by conventional filtration (e.g. filtration with a filter aid and filter paper). .
本発明に使用する限外ン濾過膜の分画分子量(排除限界
分子量)は2,000〜200,000のものであり、
10,000〜too、ooo程度のものがとくに好ま
しい。なお限外ン濾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ン濾過膜の概念に
含まれるものである。The ultrafiltration membrane used in the present invention has a molecular weight cutoff (exclusion limit molecular weight) of 2,000 to 200,000,
10,000 to about too, ooo is particularly preferable. Note that even if the membrane is not called an ultrafiltration membrane, a membrane having the above molecular weight cut-off is included in the concept of an ultrafiltration membrane in the present invention.
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、限外を
濾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、
限外濾過物の不溶物析出安定性などを見て適した限外濾
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 2,000, the passing time will be long, the yield will be low, and the ultrafiltrate will have a sticky feel. Furthermore, if the molecular weight cutoff exceeds 200,000, the removal of latent insoluble components will not be sufficient. In practice, for each hydrolyzed protein and/or its derivatives, the passage rate, yield,
It is preferable to select and use a suitable ultrafiltration membrane based on the stability of insoluble matter precipitation in the ultrafiltrate.
限外濾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、通常限外濾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 are no particular limitations on the material constituting the ultrafiltration membrane, and examples include materials normally used to form ultrafiltration membranes, such as polysulfone, polyacrylonitrile, polyethylene polymers, hydrophilic polyolefins, cellulose, and cellulose acetate. Any material may be used without limitation, but if an aqueous solvent is used, a hydrophilic material is preferred.
限外ン濾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 ultrafiltration membrane is not particularly limited, and various shapes such as a flat membrane, 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濾過膜を
通過させ、そののち誘導体にしてもよく、誘導体にして
から限外濾過膜を通過させてもよい。When removing potentially insolubilized components from a solution of a hydrolyzed protein derivative, the hydrolyzed protein solution may be passed through an ultrafiltration membrane and then converted into a derivative; You may let them.
限外ン濾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、1〜5 k
g4・Gのごとき条件が採用される。There are no particular limitations on the conditions for ultrafiltration; normal conditions,
For example, hydrolyzed protein and/or at a concentration of 40% (wt%) or less, preferably 10 to 30%
The derivative solution was heated at a temperature of 50 to 60°C or less for 1 to 5 k.
Conditions such as g4・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
難くなりを効であるが、限外濾過していない乾燥固体を
溶解させてから限外濾過しても同様の効果かえられる。When hydrolyzed proteins and/or their derivatives are supplied to the market to be incorporated into cosmetics, they are often in the form of dry solids (powders); If the method of the present invention is carried out in the dry solid state, it will be easier to dissolve the dry solid when it is made into a solution, and the insoluble matter will be less likely to be produced. A similar effect can be achieved by ultrafiltration.
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。Cosmetics in the present invention may be included in cosmetics, quasi-drugs, or pharmaceuticals as defined in the Pharmaceutical Affairs Law, and are included in the concept of cosmetics in the present invention as long as they are preparations used for cosmetics. It will 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 explained 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濾過
助剤(珪藻上)とび紙とを使用して濾過し、平均分子置
駒4000の透明な加水分解蛋白質の水溶液(a度20
%)をえた。えられた水溶液を温度30℃、圧力3 k
g4で第1表に示す6種の限外濾過膜を用いて限外濾過
し、6種の限外濾過液をえた。Examples 1 to 5 and Comparative Examples 1 to 2 Defatted soybean flour was hydrolyzed in water with an enzyme and then filtered using a filter aid (on diatom) and a piece of paper to obtain a transparent hydrolyzed product with an average molecular weight of 4000. Protein aqueous solution (A degree 20
%) was obtained. The resulting aqueous solution was heated at a temperature of 30°C and a pressure of 3k.
g4 was subjected to ultrafiltration using six types of ultrafiltration membranes shown in Table 1 to obtain six types of ultrafiltrate.
えられた水溶液および限外濾過液それぞれの濃度、製造
直後、1力月後および6力月後の色調(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 resulting aqueous solution and ultrafiltrate were examined for their respective concentrations, color tone (Gardner number) immediately after production, one month later, and six months later, and transparency (visual observation). The results are shown in Table 1.
[以下余白コ
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力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 below, it can be seen that the products produced by the method of the present invention do not develop cloudiness or precipitation even after storage for 6 months, and have a light color tone, which is excellent.
実施例6および比較例3
下記A−Hの加水分解蛋白質およびその誘導体の159
6水性溶液それぞれの通常濾過物を、実施例3で用いた
限外ン濾過膜(分画分子量50.000)を使用して、
温度25℃、圧力3.5kg 4で限外ン濾過した。え
られた限外浄過液および通常濾過物それぞれの製造直後
、1力月後および6力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
ップにバラボラトリース社製)を0.3%添加した。Example 6 and Comparative Example 3 Hydrolyzed proteins of A-H below and their derivatives 159
The normal filtrate of each of the 6 aqueous solutions was filtered using the ultrafiltration membrane (molecular weight cut off: 50.000) used in Example 3.
Ultrafiltration was performed at a temperature of 25° C. and a pressure of 3.5 kg. The transparency of the obtained ultrafiltrate and conventional filtrate was compared immediately after production, after 1 month, and after 6 months. The results are shown in Table 2. In addition, 0.3% of Fenonip (manufactured by Balabora Reese Co., Ltd.) was added to all samples as a preservative.
A:加水分解コラーゲン(平均分子ffi 10.00
0)B:加水分解ケラチン(平均分子ffi 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Q 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
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m eoo)[以下余白]
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 ffi 10.00
0) B: Hydrolyzed keratin (average molecular ffi 200)
C: Hydrolyzed elastin (average molecular weight 3000) D = Hydrolyzed silk (average molecular weight Q 1000) E: Hydrolyzed wheat protein (average molecular weight 150) F: Hydrolyzed almond protein (average molecular weight 2000) G: Hydrolyzed collagen of A A quaternary ammonium derivative synthesized by reacting 3-chloro-2-hydroxypropyltrimethylammonium chloride with 3-chloro-2-hydroxypropyltrimethylammonium chloride (the amino group of hydrolyzed collagen with an average molecular weight H:A is converted into a triethanolamine salt by amidating coconut oil fatty acid) 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ほとんどのば
あい1週間から6力月の間に、わすかな曇りを生じるも
のから明らかな沈澱を生じるものまで程度の差こそあれ
透明性が失われる。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] Solutions of hydrolyzed proteins and/or derivatives thereof that are not obtained by the method of the present invention will become slightly cloudy within one week to six months in most cases, even if they are initially transparent. Transparency is lost to varying degrees from those that produce obvious precipitation. This phenomenon also occurs when it is blended into transparent cosmetics.
しかし、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力月)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, cosmetic raw materials obtained by removing potentially insolubilized components from hydrolyzed protein and/or derivative solutions by the method of the present invention remain transparent without clouding or precipitation even after a long period of time (for example, 6 months). It is. Moreover, the color tone is clearly lighter and superior than that of a sample to which the method of the present invention is not applied.
Claims (1)
分画分子量2000〜200,000の限外ろ過膜でろ
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 method for producing a purified cosmetic raw material, which comprises filtering a solution of a hydrolyzed protein and/or its derivative through an ultrafiltration membrane having a molecular weight cutoff of 2,000 to 200,000 to remove potentially insolubilized components.
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 true JPH0111A (en) | 1989-01-05 |
| JPH0729899B2 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
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