Improved beta-lactam acylases and their use as industrial biocatalysts

  • Charles Sio
  • , Wim Quax*
  • *Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

76 Citations (Scopus)

Abstract

Whereas the beta-lactam acylases are traditionally used for the hydrolytic processing of penicillin G and cephalosporin C, new and mutated acylases can be used for the hydrolysis of alternative fermentation products as well as for the synthesis of semisynthetic beta-lactam antibiotics. Three-dimensional structural analyses and site-directed mutagenesis studies have increased the understanding of the catalytic mechanism of these enzymes. The yield of hydrolysis and synthesis has been greatly improved by process design, including immobilization of the enzyme and the use of alternative reaction media. Significant advances have also been made in the resolution of racemic mixtures by means of stereoselective acylation/hydrolysis using beta-lactam acylases
Original languageEnglish
Pages (from-to)349-355
Number of pages7
JournalCurrent Opinion in Biotechnology
Volume15
Issue number4
DOIs
Publication statusPublished - 2004

Keywords

  • PENICILLIN-G ACYLASE
  • ACID ESTER HYDROLASE
  • SITE-DIRECTED MUTAGENESIS
  • N-TERMINAL HYDROLASE
  • SUBSTRATE-SPECIFICITY
  • CEPHALOSPORIN ACYLASE
  • ENZYMATIC-SYNTHESIS
  • 7-AMINOCEPHALOSPORANIC ACID
  • AUTOPROTEOLYTIC ACTIVATION
  • ACETOBACTER-TURBIDANS

Cite this