optimization of enzymatic synthesis of ampicillin using cross-linked aggregates of penicillin g acylase
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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.
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Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase
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). Compare...
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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). Compare...
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Journal title:
iranian journal of pharmaceutical researchجلد ۲۰۰۴، شماره ۷، صفحات ۱۵۹-۱۶۴
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