Enhanced activity and stability of <Emphasis Type="SmallCaps">l</Emphasis>-arabinose isomerase by immobilization on aminopropyl glass |
| |
Authors: | Ye-Wang Zhang Marimuthu Jeya Jung-Kul Lee |
| |
Institution: | (1) Department of Chemical Engineering, Konkuk University, Seoul, 143-701, South Korea;(2) Institute of SK-KU Biomaterials, Konkuk University, Seoul, 143-701, South Korea;(3) School of Pharmacy, Jiangsu University, Zhenjiang, 212013, People’s Republic of China; |
| |
Abstract: | Immobilization of Bacillus licheniformis
l-arabinose isomerase (BLAI) on aminopropyl glass modified with glutaraldehyde (4 mg protein g support−1) was found to enhance the enzyme activity. The immobilization yield of BLAI was proportional to the quantity of amino groups
on the surface of support. Reducing particle size increased the adsorption capacity (q
m) and affinity (k
a). The pH and temperature for immobilization were optimized to be pH 7.1 and 33°C using response surface methodology (RSM).
The immobilized enzyme was characterized and compared to the free enzyme. There is no change in optimal pH and temperature
before and after immobilization. However, the immobilized BLAI enzyme achieved 145% of the activity of the free enzyme. Correspondingly,
the catalytic efficiency (k
cat/K
m) was improved 1.47-fold after immobilization compared to the free enzyme. The thermal stability was improved 138-fold (t
1/2 increased from 2 to 275 h) at 50°C following immobilization. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|