Synthesis of cephalexin in ethylene glycol with glyoxyl-agarose immobilised penicillin acylase: Temperature and pH optimisation

Andrés Illanes, Zaida Cabrera, LORENA EVELYN WILSON SOTO, Carolina Aguirre

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

The synthesis of cephalexin with glyoxyl-agarose immobilised penicillin acylase (GAPA) in 50% (v/v) ethylene glycol at 90 mM acyl donor was optimised in terms of pH and temperature, using molar yield as objective function. Yield was substantially increased by the presence of the cosolvent and stability was also higher than in aqueous medium. pH and temperature optima were 7.0 and 28°C and maximum yield was 96%, substantially higher than previously obtained with a commercial biocatalyst. The operational stability of the biocatalyst was determined as a half-life of 135 h at 28°C. Synthesis of cephalexin at low temperatures is being studied to determine if the increase in biocatalyst stability will outweigh the longer times and higher enzyme loads required. Optimisation is still to be conducted at higher substrate concentrations. Reduction in acyl donor excess is advisable but it will reduce yield.

Original languageEnglish
Pages (from-to)111-117
Number of pages7
JournalProcess Biochemistry
Volume39
Issue number1
DOIs
StatePublished - 30 Sep 2003
Externally publishedYes

Keywords

  • Cephalexin
  • Enzymatic synthesis
  • Organic cosolvent
  • Penicillin acylase
  • β-Lactam antibiotics

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