Characterization of a recombinant (-)γ-lactamase from Microbacterium hydrocarbonoxydans
1State Key Laboratory of Chemical Resources Engineering, Beijing University of Chemical Technology, Beijing, 100029, People's Republic of China.
Biotechnology Letters
|October 5, 2011
Abstract:
A (-)γ-lactamase, Mhg, from Microbacterium hydrocarbonoxydans was over-expressed in E. coli and was characterized after purification. The maximum activity was at pH 8.0 and 60°C and the half life of Mhg was ~30 min at 75°C. The enzyme was activated by DTT. The catalytic triad of the (-)γ-lactamase is comprised of residues Ser98, Asp230, and His259 and an oxyanion hole was formed by Tyr32 and Met99 according to the alignment results. Under native conditions, the (-)γ-lactamase consists of two 31 kDa homodimers.


