Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/3355
標題: Interactions of Enzymes with Polymer-Intercalated Montmorillonites and their Effects Enzymatic Activities
酵素與高分子插層蒙脫土之交互作用及酵素活性探討
作者: 王健銘
Wang, Jing-Ming
關鍵字: 蒙脫土
montmorillonite
高分子改質蒙脫土
胰蛋白酶
過氧化氫酶
插層
脫層
MMT/POP2000
MMT/POP4000
trypsin
catalase
intercalation
exfoliation
出版社: 化學工程學系
摘要: In this study, the interactions of trypsin and catalase with Na+-MMT and POP intercalated MMT were investigated. Intercalation of trypsin into the galleries of Na+-MMT and MMT/POP2000 was successfully achieved. The adsorption/intercalation amount of trypsin in MMT/POP2000 was found 2.4-fold higher than that in Na+-MMT although both of their d-spacings maintained at 5.7 nm. It was observed that the POP molecules originally residing within the galleries of MMT was replaced and released during the trypsin intercalation. Both the surface adsorption and intercalation of trypsin on MMT was significantly influenced by pH, the greatest total adsorption being observed at pH 4.0. The enzymatic activity of trypsin intercalated within galleries of MMT/POP200 was well preserved irrespective of the amount of its total adsorption. However, the enzymatic activity was highly reduced as the low concentration of trypsin was employed in its incubating with Na+-MMT. Interaction of catalase with MMT/POP2000 and MMT/POP4000, however, led to exfoliation of the clay layered structure. Nevertheless, the enzymes adsorption on MMT/POP2000 and MMT/POP4000 was 4-time higher than that on Na+-MMT. Significant effects of pH on the adsorption of catalase were similarly observed. The layered structure of MMT was only maintained with interacting catalase at pH 11.0. The enzymatic activity of catalase was highly reduced by its adsorption on either Na+-MMT or MMT/POP surfaces probably due to the conformational changes of the enzyme as a result of its extensive interactions with clay.
於本研究中,利用胰蛋白酶(trypsin)及過氧化氫酶(catalase)與天然蒙脫土(Na+-MMT)及兩種不同之高分子改質之蒙脫土(MMT/POP2000及MMT/POP4000)進行吸附/插層之程序。Trypsin於Na+-MMT及MMT/POP2000皆可成功進行插層,但MMT/POP2000之吸附/插層量相對於Na+-MMT則高出了2.4倍。由粉末式X光繞射儀(XRPD)可知,trypsin進入蒙脫土的層間插層後,其層間為5.7 nm;由POP2000的釋放量得知,trypsin吸附/插層MMT/POP2000時與層間之POP2000發生置換以進入MMT/POP2000的層間。不同的pH吸附環境對trypsin的吸附/插層量具有影響(於pH 4.0時,吸附/插層量最大),且對於trypsin插層與否也具有影響。少量的trypsin吸附/插層於MMT/POP2000時即具有酵素活性;但大量的trypsin吸附/插層於Na+-MMT時才具有酵素活性。 Catalase吸附MMT/POP2000及MMT/POP4000時蒙脫土會發生脫層反應。Catalase對於MMT/POP2000及MMT/POP4000的最大吸附量為Na+-MMT的4倍。不同的pH吸附環境下,對於catalase的吸附量及吸附現象皆有影響(pH環境為4.0時,catalase具有最大之吸附量;於pH 11.0時,不會發生脫層反應)。catalase吸附於Na+-MMT及MMT/POP4000時,蛋白質將不具有酵素活性。
URI: http://hdl.handle.net/11455/3355
Appears in Collections:化學工程學系所

文件中的檔案:

取得全文請前往華藝線上圖書館



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.