JPH02150281A - Enzyme-containing membrane and production thereof - Google Patents
Enzyme-containing membrane and production thereofInfo
- Publication number
- JPH02150281A JPH02150281A JP30316588A JP30316588A JPH02150281A JP H02150281 A JPH02150281 A JP H02150281A JP 30316588 A JP30316588 A JP 30316588A JP 30316588 A JP30316588 A JP 30316588A JP H02150281 A JPH02150281 A JP H02150281A
- Authority
- JP
- Japan
- Prior art keywords
- enzyme
- synthetic polymer
- organic solvent
- membrane
- solvent
- 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.)
- Pending
Links
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 50
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 50
- 239000012528 membrane Substances 0.000 title claims abstract description 21
- 238000004519 manufacturing process Methods 0.000 title claims description 4
- 229920001059 synthetic polymer Polymers 0.000 claims abstract description 20
- 239000003960 organic solvent Substances 0.000 claims abstract description 9
- BYEAHWXPCBROCE-UHFFFAOYSA-N 1,1,1,3,3,3-hexafluoropropan-2-ol Chemical compound FC(F)(F)C(O)C(F)(F)F BYEAHWXPCBROCE-UHFFFAOYSA-N 0.000 claims abstract description 5
- 238000005266 casting Methods 0.000 claims abstract description 5
- 229920000728 polyester Polymers 0.000 claims abstract description 5
- 239000004952 Polyamide Substances 0.000 claims abstract description 4
- 229920002647 polyamide Polymers 0.000 claims abstract description 4
- 239000000758 substrate Substances 0.000 claims abstract description 4
- YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 claims description 9
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 claims description 8
- 238000002156 mixing Methods 0.000 claims description 8
- 239000012046 mixed solvent Substances 0.000 claims description 7
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 claims description 6
- BOSAWIQFTJIYIS-UHFFFAOYSA-N 1,1,1-trichloro-2,2,2-trifluoroethane Chemical compound FC(F)(F)C(Cl)(Cl)Cl BOSAWIQFTJIYIS-UHFFFAOYSA-N 0.000 claims description 2
- RHQDFWAXVIIEBN-UHFFFAOYSA-N Trifluoroethanol Chemical compound OCC(F)(F)F RHQDFWAXVIIEBN-UHFFFAOYSA-N 0.000 claims description 2
- 239000000203 mixture Substances 0.000 claims 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims 1
- 239000002904 solvent Substances 0.000 abstract description 10
- 238000000034 method Methods 0.000 abstract description 4
- 235000013305 food Nutrition 0.000 abstract description 2
- 230000002459 sustained effect Effects 0.000 abstract description 2
- 239000003814 drug Substances 0.000 abstract 1
- 230000003578 releasing effect Effects 0.000 abstract 1
- 229940088598 enzyme Drugs 0.000 description 40
- 230000000694 effects Effects 0.000 description 22
- 239000000243 solution Substances 0.000 description 14
- 102000016943 Muramidase Human genes 0.000 description 5
- 108010014251 Muramidase Proteins 0.000 description 5
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 229960000274 lysozyme Drugs 0.000 description 5
- 239000004325 lysozyme Substances 0.000 description 5
- 235000010335 lysozyme Nutrition 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 230000003187 abdominal effect Effects 0.000 description 4
- 229920005615 natural polymer Polymers 0.000 description 4
- 108010010803 Gelatin Proteins 0.000 description 3
- 239000004677 Nylon Substances 0.000 description 3
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 3
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 3
- 229920000159 gelatin Polymers 0.000 description 3
- 239000008273 gelatin Substances 0.000 description 3
- 235000019322 gelatine Nutrition 0.000 description 3
- 235000011852 gelatine desserts Nutrition 0.000 description 3
- 229920001778 nylon Polymers 0.000 description 3
- 238000013268 sustained release Methods 0.000 description 3
- 239000012730 sustained-release form Substances 0.000 description 3
- 229960005356 urokinase Drugs 0.000 description 3
- 150000001298 alcohols Chemical class 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 239000005357 flat glass Substances 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- VZGDMQKNWNREIO-UHFFFAOYSA-N tetrachloromethane Chemical compound ClC(Cl)(Cl)Cl VZGDMQKNWNREIO-UHFFFAOYSA-N 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 102000009123 Fibrin Human genes 0.000 description 1
- 108010073385 Fibrin Proteins 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- 229920002302 Nylon 6,6 Polymers 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 229920002873 Polyethylenimine Polymers 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108090001109 Thermolysin Proteins 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 238000007605 air drying Methods 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000000679 carrageenan Substances 0.000 description 1
- 229920001525 carrageenan Polymers 0.000 description 1
- 235000010418 carrageenan Nutrition 0.000 description 1
- 229940113118 carrageenan Drugs 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 229940096384 chicken egg white lysozyme Drugs 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000012050 conventional carrier Substances 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 108010017131 high fluorescent intermediate II Proteins 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 238000000465 moulding Methods 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 239000008057 potassium phosphate buffer Substances 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229960001322 trypsin Drugs 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- UHVMMEOXYDMDKI-JKYCWFKZSA-L zinc;1-(5-cyanopyridin-2-yl)-3-[(1s,2s)-2-(6-fluoro-2-hydroxy-3-propanoylphenyl)cyclopropyl]urea;diacetate Chemical compound [Zn+2].CC([O-])=O.CC([O-])=O.CCC(=O)C1=CC=C(F)C([C@H]2[C@H](C2)NC(=O)NC=2N=CC(=CC=2)C#N)=C1O UHVMMEOXYDMDKI-JKYCWFKZSA-L 0.000 description 1
Landscapes
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Abstract
Description
【発明の詳細な説明】
（産業上の利用分野）
本発明は酵素含有膜およびその製造法に関し、特にヘキ
サフロロイソプロパノール（ＨＦＩＩ））に溶解する合
成高分子と酵素とを混合溶解し、キャスティング成型す
る方法に関する。Detailed Description of the Invention (Industrial Application Field) The present invention relates to an enzyme-containing membrane and a method for producing the same, and in particular, it involves mixing and dissolving an enzyme and a synthetic polymer soluble in hexafluoroisopropanol (HFII), and casting-molding the membrane. Regarding how to.
（従来の技術）
従来酵素包括用担体としては、合成高分子としてポリア
クリルアミド、ポリビニルアルコールまたは天然高分子
として寒天、カラーギナン、コラーゲン等さらにはポリ
エチレンイミンの使用（特開昭６２−２９４０８４）な
どが用いられている。(Prior art) Conventional carriers for entrapping enzymes include synthetic polymers such as polyacrylamide and polyvinyl alcohol, natural polymers such as agar, carrageenan, and collagen, as well as polyethyleneimine (Japanese Unexamined Patent Publication No. 62-294084). It is being
これらの素材をゲル化させる方法は化学反応、放射線、
熱、光重合等の厳しい条件で行われている。そのため触
媒の残留、酵素活性の低下等の問題が生ずる。Methods for gelling these materials include chemical reactions, radiation,
It is carried out under harsh conditions such as heat and photopolymerization. This causes problems such as residual catalyst and decreased enzyme activity.
（発明が解決しようとする問題点）
本発明は以上のような従来技術における問題点を解決し
、酵素含有膜として合成高分子および酵素両者を可溶化
し、しかも低沸点の有機溶媒であるＨＦＩＰを溶媒とし
て用いることにより酵素包括化が効率的に行われること
を見出し本発明に到達したものである。(Problems to be Solved by the Invention) The present invention solves the problems in the prior art as described above, and uses HFIP, which is an organic solvent with a low boiling point, to solubilize both a synthetic polymer and an enzyme as an enzyme-containing membrane. The present invention was achieved by discovering that enzyme entrapment can be carried out efficiently by using the compound as a solvent.
（問題点を解決するための手段）
本発明は酵素含有膜およびその製造法に係わり、酵素含
有膜の製造は酵素／ＨＦＩＰ溶液と合成高分子／ＨＦＩ
Ｐ溶液とを混合攪拌した溶液を平滑なガラス平板、金属
板、または合成高分子板上にキャスティング成型し、酵
素を合成高分子に含有させることにより行われる。(Means for Solving the Problems) The present invention relates to an enzyme-containing membrane and a method for producing the same.
This is carried out by casting a solution obtained by mixing and stirring a P solution onto a flat glass plate, metal plate, or synthetic polymer plate, and incorporating the enzyme into the synthetic polymer.
酵素／合成高分子の製膜は酵素と合成高分子のＨＦＩＰ
混合溶液をＨＦＩＰ不溶性の平板上に流延した後、風乾
、真空乾燥して行われる。Enzyme/synthetic polymer film formation is HFIP of enzyme and synthetic polymer.
The mixed solution is cast on an HFIP-insoluble plate, and then air-dried and vacuum-dried.
本発明に用いられる合成高分子はＨＦＩＰ可溶性のナイ
ロンに代表されるポリアミドまたはポリエステルで、■
−１０重量％の濃度にｓｉｌして用いる。酵素はＨＦＩ
Ｐに溶解した場合不活性化されない酵素類、例えばシス
チン結合を有するリゾチーム、トリプシン、キモトリプ
シン、トロンビン、ウロキナーゼ、パパイン、サーモラ
イシンまたはりボヌクレアーゼＡ等を用いることができ
る。またこれらの酵素２種類以上を混合して用いること
もできる。酵素溶液の濃度は１−１００ｍｇ／ｍｌの範
囲で用いることができる。さらにゼラチン、アルブミン
等の天然高分子を配合することにより合成高分子／酵素
の相溶性を高めることも可能である。この場合水中での
強度を保つため合成高分子に対する天然高分子の配合比
率は３５重量％以下にすることが好ましい。The synthetic polymer used in the present invention is polyamide or polyester represented by HFIP-soluble nylon;
It is used at a concentration of -10% by weight. The enzyme is HFI
Enzymes that are not inactivated when dissolved in P, such as lysozyme having a cystine bond, trypsin, chymotrypsin, thrombin, urokinase, papain, thermolysin or ribonuclease A, can be used. Furthermore, two or more of these enzymes can also be used in combination. The concentration of the enzyme solution can be used in the range of 1-100 mg/ml. Furthermore, by blending natural polymers such as gelatin and albumin, it is also possible to improve the compatibility of the synthetic polymer/enzyme. In this case, in order to maintain strength in water, the blending ratio of natural polymer to synthetic polymer is preferably 35% by weight or less.
また、酵素／合成高分子の配合比はいかなる比率でも混
合しうるが、水中での強度保持の問題から３０重量％以
下にすることが好ましい。Further, the enzyme/synthetic polymer may be mixed at any ratio, but it is preferably 30% by weight or less from the viewpoint of maintaining strength in water.
ＨＦＩＰは高価な溶媒であることから他の溶媒を混合添
加してＨＦＩＰの使用量を減少させることも可能である
。この場合混合溶媒は塩化メチレン、クロロホルムまた
は四塩化炭素等の塩素系溶媒、トリフロロトリクロロエ
タンまたはトリフロロエタノール等のフッ素系溶媒、イ
ンプロパツールまたはブタノール等のアルコール類の中
から選ばれる。混合溶媒の配合比は酵素の不溶化を防ぐ
ために５−２５容積％、好ましくは５−１０容積％以下
である。またブタノール等のアルコール類の過剰な添加
は膜の強度低下を招くので好ましくない。Since HFIP is an expensive solvent, it is also possible to reduce the amount of HFIP used by mixing and adding other solvents. In this case, the mixed solvent is selected from chlorinated solvents such as methylene chloride, chloroform or carbon tetrachloride, fluorinated solvents such as trifluorotrichloroethane or trifluoroethanol, and alcohols such as impropatol or butanol. The blending ratio of the mixed solvent is 5-25% by volume, preferably 5-10% by volume or less in order to prevent insolubilization of the enzyme. Further, excessive addition of alcohols such as butanol is not preferable because it causes a decrease in the strength of the membrane.
製膜は室温において合成高分子／酵素溶液または合成高
分子／天然高分子／酵素溶液を平滑なガラス平板、金属
板またはポリスチレン板等の上に流延した後、風乾して
得られその膜厚は特に制約はないが、通常０．１〜５０
０μｍ程度のものが得られる。なお、溶媒の完全な除去
のためには真空乾燥を行うことが望ましい。Film formation is performed by casting a synthetic polymer/enzyme solution or a synthetic polymer/natural polymer/enzyme solution onto a flat glass plate, metal plate, polystyrene plate, etc. at room temperature, and then air drying. There are no particular restrictions, but it is usually 0.1 to 50.
A thickness of about 0 μm can be obtained. Note that vacuum drying is preferably performed in order to completely remove the solvent.
このようにして製膜された酵素含有膜例えばナイロン／
リゾチームは水中において酵素活性を９０時間以上にわ
たり保持する。また、これら酵素活性は緩衝液中比較的
初期の５−７５分に放出されるが、その後も徐々に緩衝
液中の酵素活性は上昇する。この活性上昇速度の調整は
添加溶媒の種類、濃度を変えることにより可能である。The enzyme-containing membrane produced in this way, for example, nylon/
Lysozyme retains enzymatic activity in water for over 90 hours. Furthermore, although these enzyme activities are released relatively early in the buffer solution, 5 to 75 minutes, the enzyme activities in the buffer solution gradually increase thereafter. The rate of increase in activity can be adjusted by changing the type and concentration of the added solvent.
例えば添加溶媒による効果は、１０容量％を加えた場合
にはｎ−ブタノールでは酵素の除放性活性率は９０時間
後には４０％以上となり、クロロホルムでは３％程度で
ある。また、５容量％の場合にはいずれの混合溶媒でも
除放性活性率はＨＦＩＰ単独製膜よりも低下する。For example, the effect of the added solvent is that when n-butanol is added in an amount of 10% by volume, the enzyme sustained release activity rate is 40% or more after 90 hours, and it is about 3% in chloroform. Moreover, in the case of 5% by volume, the sustained release activity rate is lower than that in film formation using HFIP alone in any mixed solvent.
本発明の酵素含有膜は以上の特質から酵素フィルムある
いは酵素徐放性膜への応用が有効である。Due to the above characteristics, the enzyme-containing membrane of the present invention can be effectively applied to an enzyme film or a sustained enzyme release membrane.
以下本発明を実施例により説明するがこれらによって限
定されるものではない。The present invention will be explained below with reference to Examples, but is not limited thereto.
実施例１
濃度１００■／ｄのナイロン６６（デュポン社製）／Ｈ
ＦＩＰ溶液０．２ａｔｆｆｉおよび１０■／−のニワト
リ卵白リゾチーム（シグマ社製）／ＨＦＩＰ溶液０．１
＋ｔｌｌとを混合攪拌し、ガラス平板上に流延後風乾、
真空乾燥してリゾチーム含有膜（膜厚４０〜７０μｍ）
を調製した。この膜を一部切り出し、１／１５Ｍリン酸
カリウム緩衝液（ｐ Ｈ６，２４）中に浸漬した。活性
は経時的に緩衝液をサンプリングし、酵素活性基質とし
てＭ １ｅｒｏｅｏｅｃｕｓＩｙｓｏａｅｉｋｔｔｃｕ
ｓ （シグマ社ｍりを用い、分光光度計によりＡ ４
５０の初期変化率よりもとめた。Example 1 Nylon 66 (manufactured by DuPont)/H with a concentration of 100 μ/d
FIP solution 0.2 atffi and 10/- chicken egg white lysozyme (manufactured by Sigma)/HFIP solution 0.1
+tll mixed and stirred, cast on a glass plate, air-dried,
Vacuum dry to form a lysozyme-containing film (film thickness 40-70 μm)
was prepared. A portion of this membrane was cut out and immersed in 1/15M potassium phosphate buffer (pH 6,24). The activity was determined by sampling the buffer over time and using M1eroeoecusIysoaeikttcu as the enzyme active substrate.
s (A4 by spectrophotometer using Sigma Corporation mri)
It was determined based on the initial rate of change of 50.
その結果を第１図に示す。ここで放出活性率は仕込酵素
活性に対するサンプルの実測活性の比率（％）を示す。The results are shown in FIG. Here, the release activity rate indicates the ratio (%) of the measured activity of the sample to the charged enzyme activity.
実施例２
実施例１と同様にしてリゾチーム含有膜を製膜した。た
だし混合溶媒としてＨＦ Ｉ Ｐに対し塩化メチレン（
Ｉｌｈｌ）、クロロホルム（階２）またはｎ−ブタノー
ル（患３）を各々５．１０または２５容積％合成高分子
／酵素溶液に添加し、製膜を行った。得られた膜は１／
ｉ ５Ｍリン酸カリウム（ｐ Ｈ６，２４）緩衝液に腹
切片を浸漬後、経時的に放出されてくる３８時間後の酵
素活性を測定した。その結果を第２図に示す。Example 2 A lysozyme-containing membrane was formed in the same manner as in Example 1. However, as a mixed solvent, methylene chloride (
Film formation was carried out by adding 5.10 or 25% by volume of synthetic polymer/enzyme solution to 5.10 or 25 volume % of synthetic polymer/enzyme solution, respectively. The obtained film was 1/
i After immersing the abdominal section in 5M potassium phosphate (pH 6,24) buffer, the enzyme activity released over time was measured 38 hours later. The results are shown in FIG.
実施例３
濃度１００ｍｇ／ａｄのゼラチン（ナカライテック社製
）溶液０．１ｄ、１００■／ｄのポリエステル溶液０．
２−および１０ｍｇ／ｍｌ！のりゾチーム溶液０．１−
を混合攪拌し、実施例１と同様にして製膜を行った。こ
の腹切片を蒸留水で充分洗浄後さらに蒸留水中に４℃で
２晩浸漬した。その後膜切片を取り出し真空乾燥した後
、酵素活性を測定した。腹切片の酵素残存活性は仕込リ
ゾチーム活性に対して０．９％であった。一方ゼラチン
無添加の場合の残存活性は０．６％であった。Example 3 0.1 d of gelatin (manufactured by Nacalai Tech) solution with a concentration of 100 mg/ad, and 0.1 d of a polyester solution with a concentration of 100 mg/d.
2- and 10 mg/ml! Norizozyme solution 0.1-
were mixed and stirred, and film formation was performed in the same manner as in Example 1. After thoroughly washing the abdominal section with distilled water, it was further immersed in distilled water at 4°C for 2 nights. Thereafter, the membrane sections were taken out and dried under vacuum, and then the enzyme activity was measured. The residual enzyme activity in the abdominal section was 0.9% of the charged lysozyme activity. On the other hand, the residual activity when no gelatin was added was 0.6%.
実施例４
実施例１と同様に濃度１００■／ｄのナイロン溶液０．
２ｍおよび３０００ Ｕ ／ ｄのウロキナーゼ（ミド
リ十字社製）溶液０．１ｄとを混合攪拌し、実施例１と
同様にしてｉ膜を行った。この腹切片についてフィブリ
ン平板法により酵素活性を測定した。その結果、仕込ウ
ロキナーゼ活性に対し約１７１０の活性が認められた。Example 4 As in Example 1, a nylon solution with a concentration of 100 μ/d was used.
2 m and 0.1 d of 3000 U/d urokinase (Midori Juji Co., Ltd.) solution were mixed and stirred, and i-filming was performed in the same manner as in Example 1. The enzyme activity of this abdominal section was measured by fibrin plate method. As a result, an activity of about 1710 was observed compared to the urokinase activity of the preparation.
（発明の効果）
本発明の酵素含有膜は、簡便な方法で安価に効率よく目
的の酵素含有膜を製造することができると共に、従来の
酵素フィルムにない酵素徐放性膜としての利用ができる
ため食品工業、医薬への応用に有効である。(Effects of the Invention) The enzyme-containing membrane of the present invention allows the desired enzyme-containing membrane to be produced efficiently at low cost using a simple method, and can also be used as a sustained-release enzyme membrane, which is not available in conventional enzyme films. Therefore, it is effective for food industry and pharmaceutical applications.
第１図は酵素含有膜の放出活性率の経時変化を、第２図
は混合溶媒含有率に対する放出活性率を示したものであ
る。
第１図
第２図
溶媒含有率（％）FIG. 1 shows the change over time in the release activity rate of the enzyme-containing membrane, and FIG. 2 shows the release activity rate with respect to the mixed solvent content. Figure 1 Figure 2 Solvent content (%)
Claims (1)
スティング成型した酵素含有膜。 ２）合成高分子がポリアミドまたはポリエステルである
請求項１記載の酵素含有膜。 ３）有機溶媒がヘキサフロロイソプロパノールまたはヘ
キサフロロイソプロパノールとクロロホルムまたは塩化
メチレン等のハロゲン系有機溶剤あるいはトリフロロト
リクロロエタン、トリフロロエタノール等のフッ素系有
機溶媒との混合溶媒、またはヘキサフロロイソプロパノ
ールとｎ−ブタノール等のアルコール系有機溶剤との混
合溶媒である請求項１記載の酵素含有膜。 ４）ポリアミドまたはポリエステルからなる合成高分子
を有機溶媒に溶解したのち、酵素を溶解混合し基板上で
キャスティングすることを特徴とする酵素含有膜の製造
方法。[Claims] 1) An enzyme-containing membrane formed by dissolving and mixing an enzyme and a synthetic polymer in an organic solvent and then casting the mixture. 2) The enzyme-containing membrane according to claim 1, wherein the synthetic polymer is polyamide or polyester. 3) The organic solvent is hexafluoroisopropanol, a mixed solvent of hexafluoroisopropanol and a halogenated organic solvent such as chloroform or methylene chloride, or a fluorinated organic solvent such as trifluorotrichloroethane or trifluoroethanol, or hexafluoroisopropanol and n-butanol. The enzyme-containing membrane according to claim 1, which is a mixed solvent with an alcohol-based organic solvent such as . 4) A method for producing an enzyme-containing film, which comprises dissolving a synthetic polymer made of polyamide or polyester in an organic solvent, dissolving and mixing the enzyme, and casting the mixture on a substrate.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP30316588A JPH02150281A (en) | 1988-11-30 | 1988-11-30 | Enzyme-containing membrane and production thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP30316588A JPH02150281A (en) | 1988-11-30 | 1988-11-30 | Enzyme-containing membrane and production thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH02150281A true JPH02150281A (en) | 1990-06-08 |
Family
ID=17917668
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP30316588A Pending JPH02150281A (en) | 1988-11-30 | 1988-11-30 | Enzyme-containing membrane and production thereof |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH02150281A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003106671A1 (en) * | 2002-06-14 | 2003-12-24 | Baxter International Inc. | Membranes impregnated with cross-linked enzyme crystals and use thereof |
| CN112853764A (en) * | 2021-03-08 | 2021-05-28 | 南京工业大学 | Chemical pretreatment method for improving enzyme degradation efficiency of waste polyester cloth |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5014580A (en) * | 1973-05-07 | 1975-02-15 |
-
1988
- 1988-11-30 JP JP30316588A patent/JPH02150281A/en active Pending
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5014580A (en) * | 1973-05-07 | 1975-02-15 |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003106671A1 (en) * | 2002-06-14 | 2003-12-24 | Baxter International Inc. | Membranes impregnated with cross-linked enzyme crystals and use thereof |
| CN112853764A (en) * | 2021-03-08 | 2021-05-28 | 南京工业大学 | Chemical pretreatment method for improving enzyme degradation efficiency of waste polyester cloth |
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