Performance of chloroperoxidase stabilization in mesoporous sol-gel glass using in situ glucose oxidase peroxide generation

被引：32

作者：

Borole, A ^{[1
]}

Dai, S ^{[1
]}

Cheng, CL ^{[1
]}

Rodriguez, M ^{[1
]}

Davison, BH ^{[1
]}

机构：

[1] Oak Ridge Natl Lab, Oak Ridge, TN 37831 USA

来源：

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 2004年 / 113卷 / 1-3期

关键词：

sol-gel glass; chloroperoxidase; glucose oxidase; acetonitrile; horseradish peroxidase; thermostability;

D O I：

10.1385/ABAB:113:1-3:273

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A unique mesoporous sol-gel glass possessing a highly ordered porous structure (with three pore sizes of about 50, 150, and 200 A diameter) was used as a support material for immobilization of the enzyme chloroperoxidase (CPO). CPO was bound onto the glass via a bifunctional ligand, trimethoxysilylpropanal. In situ production of the cosubstrate, H2O2, was achieved using glucose oxidase. Solvent stability in acetonitrile mixtures was enhanced when a pore size larger than the size of CPO was used (i.e., 200 A). From these results, it appears that the glass-enzyme complex developed through the present work can be used as high-performance biocatalysts for various chemical-processing applications, particularly in harsh conditions.

引用

页码：273 / 285

页数：13

共 47 条

[1] Aqueous sol-gel process for protein encapsulation [J].