Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase

authors:

avatar Daryoush Abedi 1 , * , avatar Mohammad Reza Fazeli 2 , avatar Abbas Jafarian 1

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran
Iranian Journal of Pharmaceutical Research: Vol.3, issue 3; 159-164
published online: November 20, 2010
article type: Research Article
received: January 01, 2004
accepted: May 01, 2004
DOI: https://doi.org/10.22037/ijpr.2010.594

how to cite: Abedi D, Fazeli M R, Jafarian A. Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase. Iran J Pharm Res. 2004;3(3):e128215. https://doi.org/10.22037/ijpr.2010.594.

Abstract

Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compared with PGA-450, this immobilized enzyme showed a high synthesis activity. The optimum conditions for synthetic activity was at pH 6, 25°C and 2:6 (6-APA:PGME) substrate ratio.