Thermal and Operational Characteristics of Glutaryl-7-aminocephalosporanic acid Acylase Immobilized on Silica Gel Modified by Epoxide Silanization |
| |
Authors: | Jung Soo Lim Seung Won Park Seung Wook Kim |
| |
Institution: | (1) Department of Chemical and Biological Engineering, Korea University, 1, Anam-dong, 136-701 Sungbuk-ku, Seoul, Korea;(2) Food Ingredient Division, CJ Foods R&D, CJ Corp., 636, Guro-dong, 152-050 Guro-gu, Seoul, Korea |
| |
Abstract: | Summary In this study, an investigation was performed into the thermal and operational characteristics of glutaryl-7-aminocephalosporanic
acid (GL-7-ACA) acylase (EC 3.5.1.-) immobilized on silica gel that had been modified by epoxide silanization. The pH values
for the optimum activity of free and immobilized GL-7-ACA acylase were almost the same. However, the pH-dependent activity
profile for the immobilized GL-7-ACA acylase is considerably expanded. Both free and immobilized enzymes generally had the
highest activity at 50 °C. In thermodynamic studies, it was found that immobilization using epoxide silanization made GL-7-ACA
acylase thermodynamically stable. In the results of repeated batch production of 7-ACA, 89.0 and 83.5% of the 7-ACA produced
at the initial cycle were maintained after 20 times of recycle at 25 °C and 30 °C, respectively. Hence it was suggested that
mass production of 7-ACA at 25 °C using immobilized GL-7-ACA acylase by epoxide silanization would be possible on a large
scale. |
| |
Keywords: | Epoxide silanization GL-7-ACA Acylase immobilization repeated batch reaction thermodynamics |
本文献已被 SpringerLink 等数据库收录! |
|