CHARACTERIZATION OF IMMOBILIZED GLUCOSE-OXIDASE CATALASE AND THEIR DEACTIVATION IN A FLUID-BED REACTOR

被引：13

作者：

TARHAN, L ^{[1
]}

TELEFONCU, A ^{[1
]}

机构：

[1] UNIV EGE,FAC SCI,DEPT BIOCHEM,BORNOVA 35100,TURKEY

来源：

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 1990年 / 26卷 / 01期

关键词：

deactivation of GOD and CAT by H[!sub]2[!/sub]O[!sub]2[!/sub; gluconic acid production with GOD-CAT; Immobilization of GOD and CAT on the support; immobilized GOD-CAT; properties of immobilized GOD-CAT;

D O I：

10.1007/BF02798392

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：

2-Amino-4-chloro-s-triazine, a derivative of DEAE-cellulose, and acrolein/styrene copolymer were used as supports for the immobilization of glucose oxidase and catalase after being modified with diaminohexane followed by glutaraldehyde. Immobilization was carried out with optimum glucose oxidase-catalase ratios. The activity variations of the immobilized dual-enzyme systems were investigated in relation to pH and temperature. Time-dependent gluconic acid production resulting from the oxidation of glucose was monitored in a recycling fluid-bed reactor. The deactivation rates of glucose oxidase and catalase were investigated according to the first-order reaction kinetics depending on the presence of the intermediate product H2O2. © 1990 Humana Press Inc.

引用

页码：45 / 57

页数：13

共 20 条

[1] DEACTIVATION OF IMMOBILIZED BEEF LIVER CATALASE BY HYDROGEN-PEROXIDE [J].