Chloroperoxidase on periodic mesoporous organosilanes: Immobilization and reuse

被引:96
|
作者
Hudson, S.
Cooney, J.
Hodnett, B. K.
Magner, E.
机构
[1] Univ Limerick, Mat & Surface Sci Inst, Limerick, Ireland
[2] Univ Limerick, Dept Chem & Environm Sci, Limerick, Ireland
关键词
D O I
10.1021/cm070180c
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Six mesoporous materials functionalized with amine groups were developed and screened as potential supports for chloroperoxidase (CPO). A periodic mesoporous organosilane (PMO PA-40) with pore entrances large enough to allow the enzyme entry inside the pores was found to be the best support. When CPO was immobilized onto this material, it could be reused 20 times with retention of activity. On materials with little mesoporous structure and/or pore entrances too narrow to allow the enzyme entry to the channels, immobilized CPO rapidly lost activity upon reuse. Similarly, postsynthetic amino functionalization of a pure silica mesoporous material did not yield a stable biocatalyst.
引用
收藏
页码:2049 / 2055
页数:7
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