Difference in Enzyme Activity and Conformation of Glucose Oxidase Before and After Purification


Autoria(s): 戴国亮; 李津如; 江龙
Data(s)

2002

Resumo

EEnzyme activity of commercial glucose oxidase was enhanced after purification through a strong anionic exchange resin. In order to get a better insight into this phenomenon, surface pressure–area ( –A) isotherms and surface pressure–time ( –t) isotherms was used to study the interaction and the absorption at different pH values of the subphases between octadecylamine and glucose oxidase purified by a styrene system quaternary ammonium type strongly basic anionic exchange resin. Circular dichroism (CD), electrophoresis and enzyme activity measurements were conducted to study these phenomena. A preliminary hypothesis has been suggested to explain why the enzyme activity of purified glucose oxidase was higher than that of the commercial one. © 2002 Elsevier Science B.V. All rights reserved.

Identificador

http://dspace.imech.ac.cn/handle/311007/16857

http://www.irgrid.ac.cn/handle/1471x/1501

Idioma(s)

英语

Palavras-Chave #力学
Tipo

期刊论文