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

نویسندگان

  • A Jafarian
  • D Abedi
  • MR Fazeli
چکیده مقاله:

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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منابع مشابه

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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عنوان ژورنال

دوره Volume 3  شماره Number 3

صفحات  159- 164

تاریخ انتشار 2010-11-20

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