期刊
PROCESS BIOCHEMISTRY
卷 39, 期 12, 页码 2149-2155出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2003.11.010
关键词
catalase; magnesium silicate; covalent immobilization; glutaraldehyde; 3-aminopropionic acid
Bovine liver catalase was immobilized covalently with glutaraldehyde, or glutaraldehyde + 3-aminopropionic acid as a spacer, onto magnesium silicate. The coupling time was determined as 2 h for immobilization. The pH and temperature optima as well as the changes in the kinetics (K-m, V-max, E-a) of the immobilized catalase was observed and discussed. Immobilized catalase preparations showed higher storage stabilities than free catalase. The half-life of free catalase, catalase immobilized via glutaraldehyde and catalase immobilized via glutaraldehyde + spacer were calculated as 2, 55 and 10 days at room temperature and 4, 85 and 107 days at 5 degreesC, respectively. The operational stability of the catalase immobilized via glutaraldehyde was higher than the catalase immobilized via glutaraldehyde + spacer. The remaining activity of the catalase immobilized via glutaraldehyde was about 90% and that of the catalase immobilized via glutaraldeyde + spacer was about 30% after 20 cycles of batch operation. (C) 2003 Elsevier Ltd. All rights reserved.
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