JPS59169491A - Stabilization of enzyme - Google Patents
Stabilization of enzymeInfo
- Publication number
- JPS59169491A JPS59169491A JP4155383A JP4155383A JPS59169491A JP S59169491 A JPS59169491 A JP S59169491A JP 4155383 A JP4155383 A JP 4155383A JP 4155383 A JP4155383 A JP 4155383A JP S59169491 A JPS59169491 A JP S59169491A
- Authority
- JP
- Japan
- Prior art keywords
- enzyme
- phospholipid
- ethanol
- water
- 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
Links
Landscapes
- Enzymes And Modification Thereof (AREA)
Abstract
Description
【発明の詳細な説明】
本発明は酵素の安定化法に関し、より詳細には、酵素を
リン脂質で被覆処理することを特徴とする酵素の安定化
法に関する。DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a method for stabilizing an enzyme, and more particularly, to a method for stabilizing an enzyme characterized by coating the enzyme with a phospholipid.
従来、グロテアーゼ、アミラーゼ、リパーゼ等の酵素が
蛋白質、澱粉、脂肪等の汚れの除去に有効であるとして
洗剤等の分野に広く使用されている。然るにこれらの酵
素は、蛋白質等の高分子汚染物に作用[2て、これを低
分子化して水に対する溶解度を増加させるという機能を
有するものであるが、アルカリ性洗浄剤と併用しこれら
高分子を完全に分解することは不可能であるために、過
炭酸ソーダ、過ホウ酸ナトリウム等と併用して使用に供
されている。Conventionally, enzymes such as grotease, amylase, and lipase have been widely used in the field of detergents and the like because they are effective in removing stains such as proteins, starches, and fats. However, these enzymes have the function of acting on macromolecular contaminants such as proteins [2] and reducing their molecular weight to increase their solubility in water. Since it is impossible to completely decompose it, it is used in combination with sodium percarbonate, sodium perborate, etc.
然しなからこれらの酵素を上記酸化漂白性の物質と併用
する場合には、その保存時或いは使用に際して酵素自体
が酸化されて所望の酵素活性が得られないという欠点を
有L7ている。However, when these enzymes are used in combination with the above-mentioned oxidative bleaching substances, they have the disadvantage that the enzymes themselves are oxidized during storage or use, making it impossible to obtain the desired enzyme activity.
即ち、本発明は、リン脂質で酵素の被覆処理を行うこと
により、該酵素に対して酸化安定性を付与せしめ、過炭
酸ソーダ等の過酸化化合物との併用によるも、その酵素
活性が失われないという特徴を有するものである。That is, the present invention imparts oxidative stability to the enzyme by coating the enzyme with phospholipid, and the enzyme activity is not lost even when used in combination with a peroxide compound such as sodium percarbonate. It has the characteristic that there is no
本発明において酵素の被覆処理に使用するリン脂質とは
、複合脂質の一つであシ、これには、グリセリン、脂肪
酸、リン酸から成るホスファチジン酸、ホスファチジル
グリセリン、及びカルシオリピンのようなもの、更に構
成成分として含窒素原子団を有するホスファチジルコリ
ン、ホスファチジルエタノールアミン、ホスファチジル
セリン或いは脂肪酸の代わりに1個のアルデヒドを有す
るプラスマロゲン類、また脂肪酸1個しかないリゾホス
ホリピド類、リゾプラスマロゲン等があシ、特にレシチ
ン(ホスファチジルコリ/)、七ノアリン(ホスファチ
ジルセリン)等が好適に使用し得る。The phospholipid used in the enzyme coating treatment in the present invention is one of complex lipids, and includes phosphatidic acid, phosphatidylglycerin, and calciolipin, which are composed of glycerin, fatty acids, and phosphoric acid; Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, which have a nitrogen-containing atomic group as a constituent, plasmalogens which have one aldehyde instead of a fatty acid, and lysophospholipids, lysoplasmogens, which have only one fatty acid, etc., especially Lecithin (phosphatidylcoli/), heptanoline (phosphatidylserine), and the like can be suitably used.
聾だこのリン脂質は、一般に酸化され易く、従って酵素
の被覆処理に使用した場合に酸化防止剤として働き、例
えばこの被覆酵素を過炭酸ソーダの如き過酸化化合物と
混合使用した場合に、過炭酸ソーダの分解によシ生じた
酸素が有効に遮断される結果として、酵素活性の失活が
有効に防止されるという効果が達成される。Deaf phospholipids are generally easily oxidized and therefore act as antioxidants when used in enzyme coatings. For example, when this coated enzyme is mixed with a peroxide compound such as soda percarbonate, As a result of effectively blocking oxygen generated by the decomposition of soda, the effect of effectively preventing deactivation of enzyme activity is achieved.
またこのリン脂質は一般に水溶性乃至水分散性であると
ともにそれ自体界面活性的な効果を有しているために、
この被覆酵素を洗剤、詠白剤等の使用に供した場合に格
別の常置が生じないばかりかむしろ蛋白質等の汚れに該
酵素が選択的に作用してこれらの汚れの分解が行われる
ために洗浄性が向上するという利点を有している。In addition, this phospholipid is generally water-soluble or water-dispersible and has a surfactant effect itself.
When this coated enzyme is used in detergents, whitening agents, etc., not only does it not cause permanent retention, but rather the enzyme acts selectively on stains such as proteins and decomposes these stains. It has the advantage of improved cleanability.
本発明において使用する酵素としては、プロテアーゼ、
リパーゼ、アミラーゼ等の任意の酵素を使用し得るが、
蛋白質分解酵素、特にアルカリ性プロテアーゼが好適に
使用し得る。またこの酵素はそれ単体のみならず、ポリ
エチレングリコール等の潤滑剤、塩化ナトリウム、硫酸
ナトリウム、トリポリリン酸5ナトリウム、ビロリン酸
4ナトリウム又は対応するカリウム塩、セルロース粉末
、澱粉粉末、セルロース誘導体、澱粉分解生成物、澱粉
誘導体、ゼラチン、カゼイン、脱脂乳粉末、ポリビニル
アルコール、ポリビニルピロリドン等の充填剤乃至は結
合剤等と混合或いは担持されていてもよい。Enzymes used in the present invention include protease,
Any enzyme can be used, such as lipase, amylase, etc.
Proteolytic enzymes, especially alkaline proteases, can be preferably used. In addition, this enzyme is produced not only by itself but also by lubricants such as polyethylene glycol, sodium chloride, sodium sulfate, pentasodium tripolyphosphate, tetrasodium birophosphate or the corresponding potassium salt, cellulose powder, starch powder, cellulose derivatives, and starch decomposition products. It may be mixed with or supported on fillers or binders such as starch derivatives, gelatin, casein, skim milk powder, polyvinyl alcohol, and polyvinylpyrrolidone.
被覆処理は、前述したリン脂質をエタノール或いは水/
エタノール等のアルコール系溶媒に溶解せしめ、これを
回転ミル中で酵素単体或いは市販の担体に担持された酵
素と混合し、次いで乾燥することにより容易に行なわれ
る。勿論、リン脂質溶液を上記酵素にスプレー噴霧等に
より処理してもよい。In the coating treatment, the above-mentioned phospholipids are coated with ethanol or water/
This can be easily carried out by dissolving the enzyme in an alcoholic solvent such as ethanol, mixing it with the enzyme alone or with the enzyme supported on a commercially available carrier in a rotary mill, and then drying. Of course, the phospholipid solution may be treated with the above enzyme by spraying or the like.
また被覆処理に際して酵素とリン脂質とは、使用酵素及
びリン脂質の種類によっても異なるが、通常100:0
.5乃至100:100、特に100:1乃至100:
50の量比で配合することが望せしい。上記範囲よりも
リン脂質の量が少ないと所望の酸化安定性が得られず、
例えば過炭酸ンーダ等の過酸化化合物との混合により酵
素活性が失活する。また上記範囲よりリン脂質の量が多
くとも格別の利点はなく、経済的には不利となる。In addition, during coating treatment, the ratio of enzyme and phospholipid is usually 100:0, although it varies depending on the type of enzyme and phospholipid used.
.. 5 to 100:100, especially 100:1 to 100:
It is desirable to mix them in an amount ratio of 50%. If the amount of phospholipid is less than the above range, the desired oxidative stability cannot be obtained,
For example, the enzyme activity is deactivated by mixing with a peroxide compound such as percarbonate. Further, even if the amount of phospholipid is greater than the above range, there is no particular advantage and it is economically disadvantageous.
また被覆処理に使用する酵素或いは担体保持酵素はそれ
自体粉末でも粒状でもよく、例えば酵素単体或いはポリ
ビニルピロリドン等の安定剤含油酵素を若干量の水とと
もに押出成形した酵素ベレットを粒状化したものが、熱
水並びに冷水に溶解し易く好適に使用し得る。The enzyme or carrier-retaining enzyme used in the coating treatment may itself be in the form of powder or granules; for example, enzyme pellets obtained by extruding a single enzyme or an oleaginous enzyme with a stabilizer such as polyvinylpyrrolidone together with a small amount of water may be used. It is easily soluble in hot water as well as cold water and can be suitably used.
本発明方法により安定化された酵素は、酸化安定性に優
れ、例えば過炭酸ソーダ、過ホウ酸ナトリウム等の過酸
化化合物と併用しても、その保存時或いは使用に際【〜
で酵素活性が失活することなく、洗剤、漂白剤等の分野
に極めて有用である。The enzymes stabilized by the method of the present invention have excellent oxidative stability, and even when used in combination with peroxide compounds such as sodium percarbonate and sodium perborate, the enzymes stabilized during storage or use.
It is extremely useful in the fields of detergents, bleaches, etc., without losing its enzyme activity.
本発明を次の例で説明する。The invention is illustrated by the following example.
試料の調製
酵素としてプロチン/Is(大和化成製 アルカリ性プ
ロテアーゼ)を使用し、各種被覆処理剤と混合し、脱イ
オン水をこの混合物中に入れ攪拌した後、脱イオン水と
等量のエタノールを添加し、次いでこの混合物を減圧乾
燥して粉末化し、この粉末を過炭酸ソーダ(5Na、t
CO,” 2H,O□、P Cと呼ぶ〕と混合し、試料
粉末とした。Sample preparation: Protin/Is (alkaline protease manufactured by Daiwa Kasei) is used as the enzyme, mixed with various coating agents, deionized water is added to this mixture, stirred, and then ethanol is added in the same amount as the deionized water. Then, this mixture was dried under reduced pressure to powder, and this powder was mixed with sodium percarbonate (5Na, t
CO, ``2H,O□, PC'' was mixed to prepare a sample powder.
各試料粉末の配合条件等は第1表に示す通りである。The blending conditions for each sample powder are as shown in Table 1.
第1表
実施例1、
上記により調製した各試料粉末をガラスビン中に入れ、
37Cの恒温槽中に保存し、酵素活性の経時変化を測定
した。Table 1 Example 1 Each sample powder prepared as above was placed in a glass bottle,
It was stored in a constant temperature bath at 37C, and changes in enzyme activity over time were measured.
その結果を第2表に示す3、
尚、酵素活性の測定は、カゼイン−Folin法を用い
た。The results are shown in Table 2.3 The enzyme activity was measured using the casein-Folin method.
第2表
この結果より本発明に従いリン脂質で酵素の被覆処理を
行ったものは、過炭酸ソーダと混合した塙合にも、酵素
活性の失活が有効に防止されていることが理解される。Table 2 From the results, it can be seen that in the enzyme coated with phospholipid according to the present invention, deactivation of the enzyme activity is effectively prevented even when mixed with sodium percarbonate. .
実施例2゜
実施例1で使用した各試料を使用し、各保存時において
蛋白質汚染布による浸漬テストを行った6汚染布として
は、EMPAl 16蛋白質汚染布(成分:牛乳、血液
及びシナインク、付着量60TtI/S’布)を使用し
2、各試料粉体(過炭酸ソーダ22含有する量)を常温
の脱イオン水20 o meに溶解後、上記汚染布を浸
漬して汚れの除去率を測定1.た。Example 2 Using each sample used in Example 1, a soaking test was carried out with a protein-contaminated cloth at each time of storage.The 6-contaminated cloth was EMPAl 16-protein-contaminated cloth (components: milk, blood, cinnamon, adhesion). After dissolving each sample powder (containing 22% of sodium percarbonate) in 20 ml of deionized water at room temperature, the contaminated cloth was immersed to determine the stain removal rate. Measurement 1. Ta.
尚、浸漬温度け50r、浸漬時間は2時間である。第6
表にその結果を示す。The immersion temperature was 50 r, and the immersion time was 2 hours. 6th
The results are shown in the table.
第6表
特許出願人 ダスキンフランチャイズ株式会社手 続
補 正 書(自発)
昭和58年6月17日
特許庁長官 若杉和夫殿
1、 事件の表示
特願昭58−41553号
2、 発明の名称
酵素の安定化法
3 補正をする渚
事件との関係 特許出願人
4、代理人〒105
5、 補正命令の目利
な し
6、 補正の対象
明細書の発明の詳細な説明の欄
7、 補正の内容
(1) 明細書第5頁8行に「安定剤含油」とあるを
、 「安定剤含有」と訂正する。Table 6 Patent Applicant Duskin Franchise Co., Ltd. Procedural Amendment (Voluntary) June 17, 1980 Director General of the Patent Office Mr. Kazuo Wakasugi1, Indication of Case Patent Application No. 58-415532, Name of Invention Enzyme Stabilization Law 3 Relationship with the Nagisa case to be amended Patent applicant 4, agent 〒105 5, No indication of order for amendment 6, Column 7 for detailed explanation of the invention in the specification to be amended, Contents of the amendment (1) On page 5, line 8 of the specification, the phrase "contains oil stabilizer" should be corrected to "contains stabilizer."
以上that's all
Claims (1)
安定化法。A method for stabilizing enzymes characterized by coating enzymes with phospholipids.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP4155383A JPS59169491A (en) | 1983-03-15 | 1983-03-15 | Stabilization of enzyme |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP4155383A JPS59169491A (en) | 1983-03-15 | 1983-03-15 | Stabilization of enzyme |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS59169491A true JPS59169491A (en) | 1984-09-25 |
JPH0127719B2 JPH0127719B2 (en) | 1989-05-30 |
Family
ID=12611614
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP4155383A Granted JPS59169491A (en) | 1983-03-15 | 1983-03-15 | Stabilization of enzyme |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPS59169491A (en) |
Cited By (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH04234985A (en) * | 1990-12-18 | 1992-08-24 | Shin Nippon Kagaku Kogyo Kk | Production of dustless enzymic powder |
EP0826375A2 (en) * | 1996-08-28 | 1998-03-04 | Solvay Pharmaceuticals GmbH | Use of complex lipids as stabilizing additives for pharmaceutical preparations of digestive enzymes |
US9198871B2 (en) | 2005-08-15 | 2015-12-01 | Abbott Products Gmbh | Delayed release pancreatin compositions |
US10072256B2 (en) | 2006-05-22 | 2018-09-11 | Abbott Products Gmbh | Process for separating and determining the viral load in a pancreatin sample |
US10704037B2 (en) | 2005-07-29 | 2020-07-07 | Abbott Products Gmbh | Processes for the manufacture and use of pancreatin |
US11266607B2 (en) | 2005-08-15 | 2022-03-08 | AbbVie Pharmaceuticals GmbH | Process for the manufacture and use of pancreatin micropellet cores |
Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS4921090A (en) * | 1972-06-15 | 1974-02-25 |
-
1983
- 1983-03-15 JP JP4155383A patent/JPS59169491A/en active Granted
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS4921090A (en) * | 1972-06-15 | 1974-02-25 |
Cited By (10)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH04234985A (en) * | 1990-12-18 | 1992-08-24 | Shin Nippon Kagaku Kogyo Kk | Production of dustless enzymic powder |
EP0826375A2 (en) * | 1996-08-28 | 1998-03-04 | Solvay Pharmaceuticals GmbH | Use of complex lipids as stabilizing additives for pharmaceutical preparations of digestive enzymes |
JPH1077236A (en) * | 1996-08-28 | 1998-03-24 | Solvay Pharmaceut Gmbh | Stabilizing additive in water-soluble medicine preparation of digestive enzyme mixture containing lipase and protease, preparation containing the same additive and kit for producing the same digestive enzyme mixture |
US5993806A (en) * | 1996-08-28 | 1999-11-30 | Solvay Pharmaceuticals Gmbh | Method of stabilizing pharmaceutical preparations comprising digestive enzyme mixtures |
EP0826375A3 (en) * | 1996-08-28 | 2002-08-14 | Solvay Pharmaceuticals GmbH | Use of complex lipids as stabilizing additives for pharmaceutical preparations of digestive enzymes |
JP4593697B2 (en) * | 1996-08-28 | 2010-12-08 | ゾルファイ ファーマスーティカルズ ゲゼルシャフト ミット ベシュレンクテル ハフツング | Stabilized additive in water-soluble pharmaceutical preparation of lipase and protease-containing digestive enzyme mixture, preparation containing the additive and kit for producing digestive enzyme mixture |
US10704037B2 (en) | 2005-07-29 | 2020-07-07 | Abbott Products Gmbh | Processes for the manufacture and use of pancreatin |
US9198871B2 (en) | 2005-08-15 | 2015-12-01 | Abbott Products Gmbh | Delayed release pancreatin compositions |
US11266607B2 (en) | 2005-08-15 | 2022-03-08 | AbbVie Pharmaceuticals GmbH | Process for the manufacture and use of pancreatin micropellet cores |
US10072256B2 (en) | 2006-05-22 | 2018-09-11 | Abbott Products Gmbh | Process for separating and determining the viral load in a pancreatin sample |
Also Published As
Publication number | Publication date |
---|---|
JPH0127719B2 (en) | 1989-05-30 |
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