A thermal study on the use of immobilized penicillin G acylase in the formation of 7-amino-3-deacetoxy cephalosporanic acid from cephalosporin G

Jian Liang Pan, Mei-Jywan Syu

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4 Citations (Scopus)

Abstract

Penicillin G acylase (PGA) is an important enzyme for the industrial production of 7-amino-3-deacetoxy cephalosporanic acid (7-ADCA) from cephalosporin G (Ceph-G), and 6-aminopenicillanic acid (6-APA) from penicillin G (Pen-G). These products are used for the manufacture of semi-synthetic cephalosporins and penicillins. In this study, immobilized PGA was utilized to catalyze the conversion of Ceph-G to 7-ADCA. The optimal conditions were found to be an operating temperature of 45°C, 0.2 M phosphate buffer, a substrate concentration of 30 mg cm-3 and a catalyst particle concentration of 0.01 g cm-3 (specific activity of 623.2 U g-1). Up to 45°C the reaction was characterized by an activation energy of 38.66 kJ mol-1. Beyond 57.5°C there was a sharp decline of activity, characterized by a deactivation energy of 235.88 kJ mol-1.

Original languageEnglish
Pages (from-to)1050-1056
Number of pages7
JournalJournal of Chemical Technology and Biotechnology
Volume79
Issue number10
DOIs
Publication statusPublished - 2004 Oct 1

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Chemical Engineering(all)
  • Renewable Energy, Sustainability and the Environment
  • Fuel Technology
  • Waste Management and Disposal
  • Pollution
  • Organic Chemistry
  • Inorganic Chemistry

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