Optimization of enzymatic synthesis of ampicillin using cross-linked aggregates of penicillin G acylase

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 26 [6-APAPGME] substrate ratio