Abstract
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 over-expressed 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.
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