Title of article :
Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase
Author/Authors :
Abedi, Daryoush 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 , Jafarian, Abbas Department of Pharmaceutical Biotechnology - Faculty of Pharmacy and Pharmaceutical Sciences - Isfahan University of Medical Sciences, Isfahan
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
Journal title :
Astroparticle Physics
