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.
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Acknowledgment
This work was supported by Youth Fund of State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences and Open fund of State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences.
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Yang, M., Gao, Q., Wu, S. et al. Characterization of a recombinant (−)γ-lactamase from Microbacterium hydrocarbonoxydans . Biotechnol Lett 34, 275–279 (2012). https://doi.org/10.1007/s10529-011-0758-6
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DOI: https://doi.org/10.1007/s10529-011-0758-6