Overproduction and purification of the Aeromonas hydrophila CphA metallo-β-lactamase expressed in Escherichia coli

Maria Hernandez Villadares, Moreno Galleni, Jean Marie Frère, Antonio Felici, Mariagrazia Perilli, Nicola Franceschini, Gian Maria Rossolini, Arduino Oratore, Gianfranco Amicosante

Research output: Contribution to journalArticle

Abstract

The Aeromonas hydrophila CphA metallo-β-lactamase was overexpressed in a soluble secreted form in Escherichia coli using a T7 RNA polymerase-based expression system, and a simple protocol based on a single cation-exchange chromatographic step was developed, which is suitable for rapid purification of the overexpressed enzyme from E. coli lysates. A yield of up to 30 μg of purified enzyme per milliliter of culture was obtained. The purified enzyme preparation showed properties identical to those previously reported in the literature.

Original languageEnglish
Pages (from-to)253-256
Number of pages4
JournalMicrobial Drug Resistance
Volume2
Issue number2
Publication statusPublished - 1996

ASJC Scopus subject areas

  • Immunology
  • Microbiology
  • Microbiology (medical)
  • Pharmacology

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    Villadares, M. H., Galleni, M., Frère, J. M., Felici, A., Perilli, M., Franceschini, N., Rossolini, G. M., Oratore, A., & Amicosante, G. (1996). Overproduction and purification of the Aeromonas hydrophila CphA metallo-β-lactamase expressed in Escherichia coli. Microbial Drug Resistance, 2(2), 253-256.