Author/Authors :
Abedi, Daryoush Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan , Jafarian, Abbas Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan , Fazeli , Mohammad Reza Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran
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
Keywords :
Penicillin G acylase , E. Coli , Cross-linked Enzyme Aggregates , Ampicillin
