Study on the activity and stability of urease immobilized via a saccharide–concanavalin A binding
In this study, urease was immobilized on chitosan beads via a saccharide-concanavalin A binding. Similarly, the covalent immobilization of urease using glutaraldehyde was also studied for comparison. The aim of the study was to compare the two immobilization method in terms of their optimum temperature, thermal stability, optimum pH and pH stability and also, Michaelis constant(Km) of two immobilized enzyme was compared with each other. The Michaelis constant(Km) for the immobilized urease via affinity bonds was disclosed to be 11.76 mM by Lineweaver-Burk plot, and the highest activity was allowed at 77℃ and pH 5-6. Besides, this immobilized enzyme exhibits good thermal and pH stability. The obtained results are much better compared to the free enzyme and the covalent immobilization of urease using glutaraldehyde. Hence, immobilization of urease via affinity bonds could therefore be a versatile tool for immobilization of proteins and would have great promise in clinical as well as industrial use.
Urease Immobilization Concanavalin A
ZHOU Jian-qin CHEN Shao-hua Ye Lin Li Wen Jiang Xia
School of Pharmacy Soochow University Suzhou, China
国际会议
上海
英文
990-993
2008-05-16（万方平台首次上网日期，不代表论文的发表时间）