Original scientific paper

Immobilization of Glucose Oxidase on a Novel Crosslinked Chitosan Support Grafted with L-Lysine Spacers

L. C. Dong ; School of Chemistry & Chemical Engineering, Chongqing University, Chongqing, 400044, P. R. China
G. Wang ; School of Chemistry & Chemical Engineering, Chongqing University, Chongqing, 400044, P. R. China
Y. Xiao ; Department of Chemical Engineering, Tsinghua University, Beijing, P. R. China
Y. Xu ; School of Chemistry & Chemical Engineering, Chongqing University, Chongqing, 400044, P. R. China
X. Zhou ; School of Chemistry & Chemical Engineering, Chongqing University, Chongqing, 400044, P. R. China
H. Jiang ; School of Chemistry & Chemical Engineering, Chongqing University, Chongqing, 400044, P. R. China
Q. Luo ; Kansas Polymer Research Center, Business and Technology Institute, Pittsburg State University, Pittsburg, Kansas 66762, USA

Abstract

A novel L-lysine modified semi-crosslinked chitosan resin (LMCCR) was synthesized and demonstrated to be a promising enzyme support by studying the enzymatic properties of glucose oxidases (GODs) immobilized on it. The prepared LMCCR beads have large specific surface and excellent chemical stability. The insertion of flexible L-lysine spacers between chitosan backbone and the immobilized GODs (I-GODs) increases the enzymes’ activity and improves their affinity towards the substrate. Repetitive uses demonstrated that the LMCCR-immobilized GODs have excellent operational stability and reusability.
Moreover, the enzyme activity at varied temperatures and pH indicated that the GODs immobilized on LMCCR have good thermostability and pH stability.

Keywords

Enzyme support; chitosan; L-lysine; enzyme immobilization; glucose oxidase; flexible spacers

Hrčak ID:

71966

URI

https://hrcak.srce.hr/71966

Publication date:

2.10.2011.

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