固定化葡萄糖氧化酶的反应活性和稳定性提升

Reactivity and stability improvement of immobilized glucose oxidase.

作者信息

Li L X, Chen C Z, Yu Y T

机构信息

Institute for Molecular Biology, Nankai University, Tianjin Peoples Republic of China.

出版信息

Biomater Artif Cells Artif Organs. 1989;17(2):183-8.

PMID:2505874

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.

摘要

使用对（β-硫酸乙酯砜基）苯胺（SESA）作为交联剂，通过重氮化反应将葡萄糖氧化酶（GOD）固定在琼脂糖（a）上；采用一种新的改良戊二醛法（b）；以及通过聚丙烯酰胺包埋法（c）。结果表明，通过改良戊二醛法固定的GOD活性分别比重氮化法和包埋法固定的GOD活性高10%和100%。过氧化氢酶与GOD共固定在琼脂糖上可大大提高GOD的稳定性。在固定过程中添加的蛋白质如血红蛋白（Hb）、牛血清白蛋白（BSA）和还原剂即维生素C也有相同效果，但程度较小。