JPH02286074A - Two-layered membrane - Google Patents
Two-layered membraneInfo
- Publication number
- JPH02286074A JPH02286074A JP11093689A JP11093689A JPH02286074A JP H02286074 A JPH02286074 A JP H02286074A JP 11093689 A JP11093689 A JP 11093689A JP 11093689 A JP11093689 A JP 11093689A JP H02286074 A JPH02286074 A JP H02286074A
- Authority
- JP
- Japan
- Prior art keywords
- membrane
- reaction
- enzyme
- treated
- lytic
- 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
- 239000012528 membrane Substances 0.000 title claims abstract description 50
- 238000006243 chemical reaction Methods 0.000 claims abstract description 26
- 102000004190 Enzymes Human genes 0.000 claims abstract description 22
- 108090000790 Enzymes Proteins 0.000 claims abstract description 22
- 101000925662 Enterobacteria phage PRD1 Endolysin Proteins 0.000 claims abstract description 11
- 238000000034 method Methods 0.000 abstract description 9
- 239000000919 ceramic Substances 0.000 abstract description 7
- 102000007698 Alcohol dehydrogenase Human genes 0.000 abstract description 6
- 108010021809 Alcohol dehydrogenase Proteins 0.000 abstract description 6
- 102000005369 Aldehyde Dehydrogenase Human genes 0.000 abstract description 6
- 108020002663 Aldehyde Dehydrogenase Proteins 0.000 abstract description 6
- 238000001179 sorption measurement Methods 0.000 abstract description 5
- 239000000126 substance Substances 0.000 abstract description 5
- 108091005804 Peptidases Proteins 0.000 abstract description 4
- 238000000926 separation method Methods 0.000 abstract description 4
- 239000004365 Protease Substances 0.000 abstract description 3
- 102000035195 Peptidases Human genes 0.000 abstract description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 abstract description 2
- 239000007795 chemical reaction product Substances 0.000 abstract 1
- 238000010030 laminating Methods 0.000 abstract 1
- 230000035515 penetration Effects 0.000 abstract 1
- 235000019833 protease Nutrition 0.000 abstract 1
- 235000019419 proteases Nutrition 0.000 abstract 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 20
- 229940088598 enzyme Drugs 0.000 description 19
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 15
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 9
- 239000000243 solution Substances 0.000 description 7
- 238000001914 filtration Methods 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 210000000170 cell membrane Anatomy 0.000 description 4
- 210000002421 cell wall Anatomy 0.000 description 4
- 230000002101 lytic effect Effects 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 3
- 210000004027 cell Anatomy 0.000 description 3
- 239000011550 stock solution Substances 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- 239000004382 Amylase Substances 0.000 description 2
- 108010065511 Amylases Proteins 0.000 description 2
- 102000013142 Amylases Human genes 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 108010022172 Chitinases Proteins 0.000 description 2
- 102000012286 Chitinases Human genes 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 108090001060 Lipase Proteins 0.000 description 2
- 239000004367 Lipase Substances 0.000 description 2
- 102000004882 Lipase Human genes 0.000 description 2
- 108010059820 Polygalacturonase Proteins 0.000 description 2
- 235000019418 amylase Nutrition 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 108010093305 exopolygalacturonase Proteins 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 235000019421 lipase Nutrition 0.000 description 2
- 239000011259 mixed solution Substances 0.000 description 2
- 238000010992 reflux Methods 0.000 description 2
- 102100032487 Beta-mannosidase Human genes 0.000 description 1
- 108010059892 Cellulase Proteins 0.000 description 1
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- BLRPTPMANUNPDV-UHFFFAOYSA-N Silane Chemical compound [SiH4] BLRPTPMANUNPDV-UHFFFAOYSA-N 0.000 description 1
- -1 acetylmuramidase Proteins 0.000 description 1
- 108010047754 beta-Glucosidase Proteins 0.000 description 1
- 102000006995 beta-Glucosidase Human genes 0.000 description 1
- 108010055059 beta-Mannosidase Proteins 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 108010002430 hemicellulase Proteins 0.000 description 1
- 229940059442 hemicellulase Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 230000009965 odorless effect Effects 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000001612 separation test Methods 0.000 description 1
- 229910000077 silane Inorganic materials 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000007039 two-step reaction Methods 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- 108010082737 zymolyase Proteins 0.000 description 1
Landscapes
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Separation Using Semi-Permeable Membranes (AREA)
- Filtering Materials (AREA)
- Laminated Bodies (AREA)
Abstract
Description
【発明の詳細な説明】
（産業上の利用分野）
本発明は反応と分離とを−ステップで行わせることがで
きる二層膜に関するものである。DETAILED DESCRIPTION OF THE INVENTION (Industrial Application Field) The present invention relates to a two-layer membrane capable of performing reaction and separation in two steps.
（従来の技術）
セラミック膜等の表面に反応用酵素を付着させておき、
この膜体に原液を通過させて反応用酵素の作用により生
体反応を行わせ、目的とする生成物を得るための反応膜
は従来から知られている。(Conventional technology) A reaction enzyme is attached to the surface of a ceramic membrane, etc.
Reaction membranes for producing a desired product by passing a stock solution through this membrane body to cause a biological reaction to occur under the action of a reaction enzyme have been conventionally known.
しかしこのような反応膜はすぐに目詰まりを生じて濾過
流量が低下するため、必要な濾過量を得るためには必要
膜面積が大きくなり、イニシャルコスト、ランニングコ
ストが増大するという欠点があった。However, such reaction membranes quickly become clogged and the filtration flow rate decreases, so in order to obtain the required filtration amount, the required membrane area becomes large, which has the disadvantage of increasing initial costs and running costs. .
（発明が解決しようとする課題）
本発明は上記したような従来の問題点を解決して、反応
と分離とを−ステップで行わせることができ、また目詰
まりを防止して安定した反応を継続させることができる
二層膜を提供するために完成されたものである。(Problems to be Solved by the Invention) The present invention solves the above-mentioned conventional problems, allows reaction and separation to be performed in one step, and prevents clogging to ensure stable reaction. It was completed to provide a two-layer membrane that can be continued.
（！ＩＢを解決するための手段）
上記の課題を解決するためになされた本発明は、膜体の
表面と内部のいずれか一方又は双方に、溶菌酵素と反応
用酵素とを積層吸着したことを特徴とするものである。(Means for Solving !IB) The present invention, which has been made to solve the above problems, consists of stacking and adsorbing a lytic enzyme and a reaction enzyme on either or both of the surface and interior of a membrane. It is characterized by:
以下に本発明を図面を参照しつつ更に詳細に説明する。The present invention will be explained in more detail below with reference to the drawings.
第１図は本発明の二層膜を模式的に示した断面図であり
、（１）は膜体、（２）はその表面と内部のいずれか一
方又は双方に積層吸着された溶菌酵素、（３）は膜体（
１）の内部に吸着された反応用酵素である。FIG. 1 is a cross-sectional view schematically showing the two-layer membrane of the present invention, in which (1) is a membrane body, (2) is a lytic enzyme laminated and adsorbed on either or both of the surface and inside thereof; (3) is a membrane body (
1) is the reaction enzyme adsorbed inside.
膜体（１）の種類は特に限定されるものではないが、セ
ラミック膜を使用することが好ましい、溶菌酵素として
は、目詰まりの原因となる菌体の細胞壁や細胞膜を溶か
すことができるものが用いられるが、その溶菌作用は相
手の国体によって特異的に決まるものである。即ち、細
菌に対してはペクチナーゼ、プロテアーゼ、に−アセチ
ルムラミダーゼ、リゾチーム、リパーゼ、アミラーゼ、
キチナーゼ等の溶菌酵素が使用される。また真菌類に対
しては、グルカナーゼ、マンナナーゼ、プロテアーゼ、
β−グルコシダーゼ、セルラーゼ、リパーゼ、アミラー
ゼ、キチナーゼ、ペクチナーゼ、ヘミセルラーゼ、キシ
ラナーゼ等の溶菌酵素を使用すればよい、また反応用酵
素としては目的とする反応により種々の酵素が選択され
るが、例えばエタノールから酢酸を製造する場合には、
アルコールデヒドロゲナーゼとアルデヒドデヒドロゲナ
ーゼを使用すればよい、 このような溶菌酵素や反応用
酵素を膜体（１）に吸着させるには、膜体く１）を化学
物質で処理後、酵素を共有結合によりその化学物質に結
合させる化学的吸着法や、膜体（１）を酵素の水溶液に
浸漬するか、膜体（１）に酵素の水溶液を圧入する物理
的吸着法を取ることができる。なお、物理的吸着法を取
る場合には、酵素の水溶液の濃度は高いほど好ましく、
また酵素の安定化を図るために他の蛋白質等を酵素の水
溶液に溶かしてもよい。The type of membrane (1) is not particularly limited, but it is preferable to use a ceramic membrane.As for the lytic enzyme, one that can dissolve the cell walls and cell membranes of bacterial cells that cause clogging is recommended. However, its lytic action is determined specifically by the host country. That is, for bacteria, pectinase, protease, acetylmuramidase, lysozyme, lipase, amylase,
Lytic enzymes such as chitinase are used. In addition, for fungi, glucanases, mannanases, proteases,
Lytic enzymes such as β-glucosidase, cellulase, lipase, amylase, chitinase, pectinase, hemicellulase, and xylanase may be used. Various enzymes may be selected depending on the desired reaction, such as ethanol. When producing acetic acid from
Alcohol dehydrogenase and aldehyde dehydrogenase can be used. In order to adsorb such lytic enzymes and reaction enzymes to the membrane body (1), after treating the membrane body (1) with a chemical substance, the enzymes can be attached to the membrane body through covalent bonds. A chemical adsorption method in which the enzyme is bonded to a chemical substance or a physical adsorption method in which the membrane body (1) is immersed in an aqueous enzyme solution or an aqueous enzyme solution is pressurized into the membrane body (1) can be used. In addition, when using the physical adsorption method, the higher the concentration of the enzyme aqueous solution, the better.
Further, in order to stabilize the enzyme, other proteins etc. may be dissolved in the aqueous solution of the enzyme.
（作用）
このように構成された本発明の二層膜は、膜体（１）に
原液を通過させて反応用酵素（３）の作用により反応を
行わせるとともに、膜体（１）自体を濾過体として反応
液の分離を行うものであり、従来の反応用酵素のみを吸
着固定させた膜では分離の際には菌体の細胞壁や細胞膜
の破片等が膜体（１）の表面に付着して目詰まりが発止
し易いのであるが、本発明においては膜体（１）の表面
又は内部に積層吸着されている溶菌酵素（２）がこの細
胞壁や細胞膜を溶かすので目詰まりを生じに＜＜、次の
実施例に示される通り膜の寿命を従来の膜に比較して大
幅に延ばすことができる。(Function) The two-layer membrane of the present invention configured as described above allows a stock solution to pass through the membrane body (1) to cause a reaction by the action of the reaction enzyme (3), and also allows the membrane body (1) itself to react. It is used as a filter to separate the reaction solution, and with conventional membranes that adsorb and immobilize only reaction enzymes, the cell walls of bacterial cells and fragments of cell membranes adhere to the surface of the membrane body (1) during separation. However, in the present invention, the lytic enzyme (2) layered and adsorbed on the surface or inside of the membrane body (1) dissolves this cell wall and cell membrane, so clogging does not occur. <<As shown in the following example, the life of the membrane can be significantly extended compared to conventional membranes.
（実施例）
次にグルコースをサツカロマイセス−セレビシェ（Ｓａ
ｃ’ｃｈａｒｏｓｙｃｅｓ−ｃｅｒｅｖｉｉｉａｅ）協
会７号菌を用いてエタノールに変換し、アルコールデヒ
ドロゲナーゼとアルデヒドデヒドロゲナーゼを使用して
酢酸を製造する二段反応についての実施例を示す。(Example) Next, glucose was added to Satucharomyces cerevisiae (Sa
An example of a two-step reaction in which ethanol is converted to ethanol using B. c'charosyces-cereviiiiae) and acetic acid is produced using alcohol dehydrogenase and aldehyde dehydrogenase.
「二層膜の製造方法」
まずセラミック膜（平均孔径０．２＃、膜面積５０ｃｊ
）を６００ｍ ｌのトルエンに浸漬させ、沸騰石を添加
後マントルヒーターを用いて還流しながら加熱した。ト
ルエンが沸騰後、６０−Ｅのシラン剤（信越化学社製、
Ｔ−アミノプロピルトリエトキシシラン）を添加し、４
時間還流を行いながら加熱した０反応後この溶媒を捨て
、トルエン臭がなくなるまでセラミック膜をアセトンで
洗浄した。"Method for manufacturing a two-layer membrane" First, a ceramic membrane (average pore diameter 0.2#, membrane area 50cj
) was immersed in 600 ml of toluene, and after adding boiling stones, it was heated under reflux using a mantle heater. After the toluene boils, add 60-E silane agent (manufactured by Shin-Etsu Chemical Co., Ltd.).
T-aminopropyltriethoxysilane) and 4
After the reaction was heated under reflux for a period of time, the solvent was discarded, and the ceramic membrane was washed with acetone until the toluene odor disappeared.
このように゛処理したセラミック膜をエタノール中に浸
漬後、真空ポンプを用いて脱気を行ない、純水で洗浄し
、１％グルタルアルデヒド１５０■ｌを添加し、室温で
２時間静置した。その後、セラミック膜を無臭になるま
で純水で洗浄し、次の二つの方法で処理した。After immersing the thus treated ceramic membrane in ethanol, it was degassed using a vacuum pump, washed with pure water, 150 liters of 1% glutaraldehyde was added, and left standing at room temperature for 2 hours. Thereafter, the ceramic membrane was washed with pure water until it became odorless and treated using the following two methods.
０１０％アルコールデヒドロゲナーゼと１０％アルデヒ
ドデヒドロゲナーゼの混合液に２４時間浸漬後、純水で
洗浄する。After being immersed in a mixed solution of 10% alcohol dehydrogenase and 10% aldehyde dehydrogenase for 24 hours, it is washed with pure water.
■支持層を下にして１０％アルコールデヒドロゲナーゼ
と１０％アルデヒドデヒドロゲナーゼの混合液に２４時
間半分浸すように浸漬後、純水で洗浄し、その後活性層
を下にして１０％ザイモリエース溶液に２４時間半分浸
すように浸漬後、純水で洗浄した。- After immersing in a mixed solution of 10% alcohol dehydrogenase and 10% aldehyde dehydrogenase for half of 24 hours with the support layer facing down, wash with pure water, then soak in a 10% Zymolyase solution for half of 24 hours with the active layer facing down. After soaking, it was washed with pure water.
このように■、■の二通りの方法で処理した膜を使用し
、次の試験を行った。The following tests were conducted using the membranes treated in two ways (1) and (2).
「反応及び分離試験」
実容量３１の醗酵槽にグルコース１８％、酵母エキス２
％となるように調整された墳地を入れ、サツカロマイセ
ス−セレビシェ（Ｓａｃｃｈａｒｏｇ＋ｙｃｅｓ−ｃａ
ｒｅｖｉｓｉａｅ） Ｉａ会７号菌を接種し、１ｖｖｓ
の空気量で４〜６日間培養を行った。エタノール濃度が
９％（−ハ）以上（収率９５％以上）に達した時点より
Ｎ＾Ｄを最終濃度１％以上になるように添加した。その
後醗酵槽から４１／■ｉｎで培養液を引き抜き、クロス
フロー式で前記した二通りの方法で処理した膜に通して
反応酵素であるアルコールデヒドロゲナーゼとアルデヒ
ドデヒドロゲナーゼによりエタノールを酢酸に変喚させ
ると同時に濾過させ、原液（Ｉ４縮液） は醗酵槽に戻
す連続濾過培養を滞留時間９６時間で行った。"Reaction and separation test" Glucose 18%, yeast extract 2
Insert the mound adjusted to %, and add Saccharomyces-cereviche
revisiae) inoculated with Ia group 7 bacteria, 1vvs.
Culture was performed for 4 to 6 days with an air volume of . From the time when the ethanol concentration reached 9% (-c) or more (yield 95% or more), N^D was added to give a final concentration of 1% or more. After that, the culture solution was drawn out from the fermentation tank at 41/cm, and passed through a membrane treated with the two methods described above using a cross-flow method to simultaneously convert ethanol into acetic acid using the reaction enzymes alcohol dehydrogenase and aldehyde dehydrogenase. After filtration, the stock solution (I4 condensate) was returned to the fermenter for continuous filtration culture with a residence time of 96 hours.
その結果、いずれの膜を用いても濾液中の生成酢酸量は
培養液中のエタノールの９５％以上が変換された量とな
り、未反応のエタノール濃度は培養液中のエタノール濃
度の５％以下になった。またその際の透過流量を経時的
に測定したところ、第２図に示されるとおりとなった。As a result, no matter which membrane was used, the amount of acetic acid produced in the filtrate was such that more than 95% of the ethanol in the culture solution was converted, and the concentration of unreacted ethanol was less than 5% of the ethanol concentration in the culture solution. became. Moreover, when the permeation flow rate at that time was measured over time, it was as shown in FIG. 2.
第２図から明らかなように、溶菌酵素を固定化した■の
膜は溶菌酵素のない■の膜に比較して約１．４倍の透過
流量を示した。またエタノールから酢酸への反応性はい
ずれの膜を用いても差は認められなかった。As is clear from FIG. 2, the membrane No. 2 on which the lytic enzyme was immobilized showed a permeation flow rate about 1.4 times that of the membrane No. 2 without the lytic enzyme. Furthermore, no difference was observed in the reactivity from ethanol to acetic acid regardless of which membrane was used.
（発明の効果）
本発明は以上に説明したように、目詰まりの原因となる
菌体の細胞壁や細胞膜を溶かすことができる溶菌酵素を
吸着させたことにより濾過の際の目詰まりを防止するこ
とができ、長時間にわたり高い透過流量を維持すること
ができる。よって本発明は安定した反応を継続させるこ
とができる二層膜、として、産業の発展に寄与するとこ
ろは極めて大きいものがある。(Effects of the Invention) As explained above, the present invention prevents clogging during filtration by adsorbing a lytic enzyme that can dissolve the cell walls and cell membranes of bacterial cells that cause clogging. It is possible to maintain a high permeation flow rate for a long period of time. Therefore, the present invention greatly contributes to the development of industry as a two-layer membrane that can continue a stable reaction.
第１図は本発明の酵素固定膜を模式的に示す断面図、第
２図は実施例における透過流量の経時的変化を示すグラ
フである。
（１） ｊ ＩＩ！体、（２）：溶菌酵素、（３）二反
応用酵素。FIG. 1 is a cross-sectional view schematically showing the enzyme-immobilized membrane of the present invention, and FIG. 2 is a graph showing changes in permeation flow rate over time in Examples. (1) j II! body, (2): lytic enzyme, (3) enzyme for two reactions.
Claims (1)
菌酵素（２）と反応用酵素（３）とを積層吸着したこと
を特徴とする二層膜。A two-layer membrane characterized in that a lytic enzyme (2) and a reaction enzyme (3) are laminated and adsorbed on either or both the surface and interior of a membrane body (1).
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1110936A JP2728932B2 (en) | 1989-04-28 | 1989-04-28 | Two-layer membrane |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1110936A JP2728932B2 (en) | 1989-04-28 | 1989-04-28 | Two-layer membrane |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH02286074A true JPH02286074A (en) | 1990-11-26 |
| JP2728932B2 JP2728932B2 (en) | 1998-03-18 |
Family
ID=14548342
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP1110936A Expired - Lifetime JP2728932B2 (en) | 1989-04-28 | 1989-04-28 | Two-layer membrane |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP2728932B2 (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1998004334A1 (en) * | 1996-07-25 | 1998-02-05 | Nikki-Universal Co., Ltd. | Air cleaning filter |
| CN102786709A (en) * | 2012-07-18 | 2012-11-21 | 北京理工大学 | Waterproof permeable material having antibacterial function, and its preparation method |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6430584A (en) * | 1987-07-25 | 1989-02-01 | Ngk Insulators Ltd | Carrier for immobilizing organism catalyst |
-
1989
- 1989-04-28 JP JP1110936A patent/JP2728932B2/en not_active Expired - Lifetime
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6430584A (en) * | 1987-07-25 | 1989-02-01 | Ngk Insulators Ltd | Carrier for immobilizing organism catalyst |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1998004334A1 (en) * | 1996-07-25 | 1998-02-05 | Nikki-Universal Co., Ltd. | Air cleaning filter |
| CN102786709A (en) * | 2012-07-18 | 2012-11-21 | 北京理工大学 | Waterproof permeable material having antibacterial function, and its preparation method |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2728932B2 (en) | 1998-03-18 |
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