Effects of Inhibitors on the Catalysis and Immobilization of Cephalosporin C Acylase

Sa？etak Numerous compounds, including weak bases (e.g., glucosamine, ethylenediamine, and pyridine) and weak acids (e.g., bicarbonate, acetate, propionate, and butyrate), were found to inhibit the catalysis of cephalosporin C acylase (CCA), which is a recombinant enzyme expressed in E. coli. Additionally, the protective effect of the inhibitors on free and immobilized CCA against heat treatment was investigated. The inhibitors were added to increase recovery of the activity of the enzyme immobilized by covalent attachment to an epoxy support. The activities of immobilized CCA obtained in the presence of acetate or bicarbonate were 99.2±2.5 U g–1 and 94.1±3.0 U g–1, respectively, which were 31.7 % and 25 % higher, respectively, than that of the control. In addition, the immobilized CCA exhibited improved thermostability. The half-life of immobilized CCA obtained in the presence of acetate or bicarbonate increased by 190 % and 120 %, respectively, compared to that of immobilized CCA obtained in the absence of an inhibitor. This work is licensed under a Creative Commons Attribution 4.0 International License