Reactivity and stability improvement of immobilized glucose oxidase.

Abstract

Glucose oxidase (GOD) was immobilized on agrose(a) by diazotization using p(beta-sulfate-ethylfonyl)aniline(SESA) as cross-linking agent, (b) by a new improved glutaraldehyde method and (c) by polyacrylamide entrapment. Results showed that GOD immobilized by the improved glutaraldehyde method had an activity of 10% and 100% higher than that by diazotization and entrapment method respectively. Catalase co-immobilized with GOD on agrose greatly enhanced the stability of GOD. Proteins such as hemoglobin(Hb), bovine serum albumin(BSA) and reducing agent i.e. VitC added during immobilization had the same effect but to a lesser extent.