JPH0127719B2 - - Google Patents
Info
- Publication number
- JPH0127719B2 JPH0127719B2 JP58041553A JP4155383A JPH0127719B2 JP H0127719 B2 JPH0127719 B2 JP H0127719B2 JP 58041553 A JP58041553 A JP 58041553A JP 4155383 A JP4155383 A JP 4155383A JP H0127719 B2 JPH0127719 B2 JP H0127719B2
- Authority
- JP
- Japan
- Prior art keywords
- enzyme
- phospholipid
- water
- enzymes
- enzyme activity
- 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
Links
- 102000004190 Enzymes Human genes 0.000 claims description 41
- 108090000790 Enzymes Proteins 0.000 claims description 41
- 150000003904 phospholipids Chemical class 0.000 claims description 13
- 238000000034 method Methods 0.000 claims description 6
- 238000002156 mixing Methods 0.000 claims description 4
- 230000000087 stabilizing effect Effects 0.000 claims description 4
- 230000001476 alcoholic effect Effects 0.000 claims description 2
- 238000001035 drying Methods 0.000 claims description 2
- 239000002904 solvent Substances 0.000 claims description 2
- 229940088598 enzyme Drugs 0.000 description 37
- 230000000694 effects Effects 0.000 description 11
- 238000000576 coating method Methods 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- 239000011248 coating agent Substances 0.000 description 7
- -1 peroxide compound Chemical class 0.000 description 7
- 239000000843 powder Substances 0.000 description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- VTIIJXUACCWYHX-UHFFFAOYSA-L disodium;carboxylatooxy carbonate Chemical compound [Na+].[Na+].[O-]C(=O)OOC([O-])=O VTIIJXUACCWYHX-UHFFFAOYSA-L 0.000 description 6
- 229940045872 sodium percarbonate Drugs 0.000 description 6
- 239000004744 fabric Substances 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 108091005804 Peptidases Proteins 0.000 description 3
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 3
- 239000008367 deionised water Substances 0.000 description 3
- 229910021641 deionized water Inorganic materials 0.000 description 3
- 235000014113 dietary fatty acids Nutrition 0.000 description 3
- 239000000194 fatty acid Substances 0.000 description 3
- 229930195729 fatty acid Natural products 0.000 description 3
- 150000004665 fatty acids Chemical class 0.000 description 3
- 238000007654 immersion Methods 0.000 description 3
- 230000001590 oxidative effect Effects 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- TZCPCKNHXULUIY-RGULYWFUSA-N 1,2-distearoyl-sn-glycero-3-phosphoserine Chemical compound CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)OC[C@H](N)C(O)=O)OC(=O)CCCCCCCCCCCCCCCCC TZCPCKNHXULUIY-RGULYWFUSA-N 0.000 description 2
- 239000004382 Amylase Substances 0.000 description 2
- 102000013142 Amylases Human genes 0.000 description 2
- 108010065511 Amylases Proteins 0.000 description 2
- 108091005658 Basic proteases Proteins 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- ZWZWYGMENQVNFU-UHFFFAOYSA-N Glycerophosphorylserin Natural products OC(=O)C(N)COP(O)(=O)OCC(O)CO ZWZWYGMENQVNFU-UHFFFAOYSA-N 0.000 description 2
- 102000004882 Lipase Human genes 0.000 description 2
- 108090001060 Lipase Proteins 0.000 description 2
- 239000004367 Lipase Substances 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 235000019418 amylase Nutrition 0.000 description 2
- 239000007844 bleaching agent Substances 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 230000009849 deactivation Effects 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
- 235000019421 lipase Nutrition 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 2
- 235000019419 proteases Nutrition 0.000 description 2
- 229960001922 sodium perborate Drugs 0.000 description 2
- MWNQXXOSWHCCOZ-UHFFFAOYSA-L sodium;oxido carbonate Chemical compound [Na+].[O-]OC([O-])=O MWNQXXOSWHCCOZ-UHFFFAOYSA-L 0.000 description 2
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 2
- PORPENFLTBBHSG-MGBGTMOVSA-N 1,2-dihexadecanoyl-sn-glycerol-3-phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(O)=O)OC(=O)CCCCCCCCCCCCCCC PORPENFLTBBHSG-MGBGTMOVSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- CFWRDBDJAOHXSH-SECBINFHSA-N 2-azaniumylethyl [(2r)-2,3-diacetyloxypropyl] phosphate Chemical compound CC(=O)OC[C@@H](OC(C)=O)COP(O)(=O)OCCN CFWRDBDJAOHXSH-SECBINFHSA-N 0.000 description 1
- 241000723347 Cinnamomum Species 0.000 description 1
- JZNWSCPGTDBMEW-UHFFFAOYSA-N Glycerophosphorylethanolamin Natural products NCCOP(O)(=O)OCC(O)CO JZNWSCPGTDBMEW-UHFFFAOYSA-N 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000017803 cinnamon Nutrition 0.000 description 1
- 239000012459 cleaning agent Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- ZGSPNIOCEDOHGS-UHFFFAOYSA-L disodium [3-[2,3-di(octadeca-9,12-dienoyloxy)propoxy-oxidophosphoryl]oxy-2-hydroxypropyl] 2,3-di(octadeca-9,12-dienoyloxy)propyl phosphate Chemical compound [Na+].[Na+].CCCCCC=CCC=CCCCCCCCC(=O)OCC(OC(=O)CCCCCCCC=CCC=CCCCCC)COP([O-])(=O)OCC(O)COP([O-])(=O)OCC(OC(=O)CCCCCCCC=CCC=CCCCCC)COC(=O)CCCCCCCC=CCC=CCCCCC ZGSPNIOCEDOHGS-UHFFFAOYSA-L 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 239000010200 folin Substances 0.000 description 1
- 125000002485 formyl group Chemical class [H]C(*)=O 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 230000001050 lubricating effect 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
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- 238000009896 oxidative bleaching Methods 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 150000008104 phosphatidylethanolamines Chemical class 0.000 description 1
- 235000011007 phosphoric acid Nutrition 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- XAEFZNCEHLXOMS-UHFFFAOYSA-M potassium benzoate Chemical compound [K+].[O-]C(=O)C1=CC=CC=C1 XAEFZNCEHLXOMS-UHFFFAOYSA-M 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- FQENQNTWSFEDLI-UHFFFAOYSA-J sodium diphosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])([O-])=O FQENQNTWSFEDLI-UHFFFAOYSA-J 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- 238000005507 spraying Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 235000019818 tetrasodium diphosphate Nutrition 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-I triphosphate(5-) Chemical compound [O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O UNXRWKVEANCORM-UHFFFAOYSA-I 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
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。
従来、プロテアーゼ、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
染物に作用して、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。
然しなが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している。
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。
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り、これには、グ
リセリン、脂肪酸、リン酸から成るホスフアチジ
ン酸、ホスフアチジルグリセリン、及びカルジオ
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アチジルコリン、ホスフア
チジルエタノールアミン、ホスフアチジルセリン
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
り、特にレシチン（ホスフアチジルコリン）、セ
フアリン（ホスフアチジルセリン）等が好適に使
用し得る。
またこのリン脂質は、一般に酸化され易く、従
つ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り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。
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、標白剤等
の使用に供した場合に格別の弊害が生じないばか
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。
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
等の潤滑性、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、ピロリン酸４ナト
リウム又は対応するカリウム塩、等の充填剤と混
合されていてもよい。
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。
また被覆処理に際して酵素とリン脂質とは、重
量基準で100：１乃至100：50の量比で使用され
る。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、例えば過炭酸ソーダ等
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。
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有
酵素を若干量の水とともに押出成形した酵素ペレ
ツ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。
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
時或いは使用に際して酵素活性が失活することな
く、洗浄、漂白剤等の分野に極めて有用である。
本発明を次の例で説明する。
試料の調製
酵素としてプロチンAS（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撹拌した
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（3Na2CO3・2H2O2、PCと呼
ぶ）と混合し、試料粉末とした。
各試料粉末の配合条件等は第１表に示す通りで
ある。
[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. Conventionally, enzymes such as protease, 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, converting them into lower molecules, and increasing their solubility in water. Since it is impossible to decompose it into other substances, it is used in combination with sodium percarbonate, sodium perborate, etc. 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. 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 The phospholipid used in the enzyme coating treatment in the present invention is one of complex lipids, and includes phosphatidic acid, phosphatidylglycerin, and cardiolipin, which are composed of glycerin, fatty acids, and phosphoric acid; Furthermore, 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 which have only one fatty acid, Lysoplus. Among them, lecithin (phosphatidylcholine), cephalin (phosphatidylserine), etc. can be preferably used. In addition, this phospholipid is generally easily oxidized, and therefore acts as an antioxidant when used for coating enzymes. 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. In addition, this phospholipid is generally water-soluble or water-dispersible, and has a surfactant effect itself, so when this coated enzyme is used in detergents, whitening agents, etc., it has a special effect. Not only does it not cause any harmful effects, it has the advantage that the enzyme selectively acts on stains such as proteins and decomposes these stains, resulting in improved cleaning performance. As the enzyme used in the present invention, any enzyme such as protease, lipase, amylase, etc. can be used, and proteolytic enzymes, particularly alkaline protease, can be preferably used. In addition, this enzyme is not only used alone, but also by lubricating substances such as polyethylene glycol, sodium chloride, sodium sulfate,
It may also be mixed with fillers such as pentasodium tripolyphosphate, tetrasodium pyrophosphate or the corresponding potassium salt. The coating treatment can be easily carried out by dissolving the above-mentioned phospholipid in an alcoholic solvent such as ethanol or water/ethanol, mixing this with the enzyme alone or with the enzyme supported on a commercially available carrier in a rotary mill, and then drying. It will be held in Of course, the phospholipid solution may be treated with the above enzyme by spraying or the like. Further, during the coating treatment, the enzyme and phospholipid are used in a weight ratio of 100:1 to 100:50. When the amount of phospholipid is less than the above range, the desired oxidative stability cannot be obtained, and the enzyme activity is deactivated by mixing with a peroxide compound such as sodium percarbonate. Further, even if the amount of phospholipid is greater than the above range, there is no particular advantage and it is economically disadvantageous. The enzyme or carrier-retaining enzyme used in the coating process may itself be in the form of powder or granules; for example, enzyme pellets obtained by extruding an enzyme alone or an enzyme containing 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. The enzyme stabilized by the method of the present invention has excellent oxidative stability, and even when used in combination with peroxide compounds such as sodium percarbonate and sodium perborate, the enzyme activity will not be deactivated during storage or use. It is extremely useful in fields such as cleaning and bleaching agents. The invention is illustrated by the following example. Preparation of sample Protin AS (alkaline protease manufactured by Daiwa Kasei) was used as the enzyme, mixed with various coating treatment agents, deionized water was added to this mixture, stirred, and then ethanol of the same amount as deionized water was added. Next, this mixture was dried under reduced pressure to powder, and this powder was mixed with sodium percarbonate (3Na 2 CO 3 .2H 2 O 2 , referred to as PC) to obtain a sample powder. The blending conditions for each sample powder are as shown in Table 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、37℃の恒温槽中に保存し、酵素活性の経
時変化を測定した。
その結果を第２表に示す。
尚、酵素活性の測定は、カゼイン−Folin法を
用いた。[Table] Example 1 Each sample powder prepared as described above was placed in a glass bottle and stored in a constant temperature bath at 37°C, and changes in enzyme activity over time were measured. The results are shown in Table 2. Note that the enzyme activity was measured using the casein-Folin method.
【表】
この結果より本発明に従いリン脂質で酵素の被
覆処理を行つたものは、過炭酸ソーダと混合した
場合にも、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。
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つ
た。
汚染布としては、EMPA116蛋白質汚染布（成
分：牛乳、血液及びシナインク、付着量60mg／ｇ
布）を使用し、各試料粉体と（過炭酸ソーダ２ｇ
含有する量）を常温の脱イオン水200mlに溶解後、
上記汚染布を浸漬して汚れの除去率を測定した。
尚、浸漬温度は50℃、浸漬時間は２時間であ
る。第３表にその結果を示す。[Table] From these 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. Example 2 Using each sample used in Example 1, a immersion test with a protein-contaminated cloth was conducted at each time of storage. The contaminated cloth was EMPA116 protein contaminated cloth (ingredients: milk, blood, and cinnamon ink, adhesion amount 60 mg/g).
cloth), and each sample powder and (2 g of soda percarbonate)
After dissolving the amount contained in 200ml of deionized water at room temperature,
The stain removal rate was measured by soaking the contaminated cloth. The immersion temperature was 50°C and the immersion time was 2 hours. Table 3 shows the results.
Claims (1)
でこの溶液を酵素と混合し乾燥することから成る
酵素の安定化方法であつて、前記酵素とリン脂質
とは100：１乃至100：50の重量比で使用されるこ
とを特徴とする酵素の安定化方法。1. A method for stabilizing an enzyme, which comprises dissolving a phospholipid in an alcoholic solvent, then mixing this solution with an enzyme and drying, the enzyme and the phospholipid having a weight ratio of 100:1 to 100:50. A method for stabilizing an enzyme, characterized in that it is used in.
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 JPS59169491A (en) | 1984-09-25 |
| JPH0127719B2 true 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) |
Families Citing this family (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 |
| DE19724845A1 (en) * | 1996-08-28 | 1998-03-05 | Solvay Pharm Gmbh | Use of complex lipids as stabilizing additives for pharmaceutical preparations of digestive enzyme mixtures |
| CN101233229B (en) | 2005-07-29 | 2013-05-01 | 雅培实验室有限公司 | Processes for the manufacture of sterilized pancreatin powder |
| US11266607B2 (en) | 2005-08-15 | 2022-03-08 | AbbVie Pharmaceuticals GmbH | Process for the manufacture and use of pancreatin micropellet cores |
| 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 |
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 |
Also Published As
| Publication number | Publication date |
|---|---|
| JPS59169491A (en) | 1984-09-25 |
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