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Purification and characterization of a novel (−) gamma-lactamase fromMicrobacterium hydrocarbonoxydans

  • Food Microbiology
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Abstract

A (−) gamma-lactamase fromMicrobacterium hydrocarbonoxydans was purified to homogeneity by chromatography methods. SDS-PAGE showed the molecular weight of the enzyme was about 31 kDa. The purified enzyme had a specific activity of 61.3±2.5 U mg−1 for 2-azabicyclo [2.2.1] hept-5-en-3-one [(−) gamma-lactam]. The enantioselectivity factor (E) of the purified enzyme was 9.5±0.8 for unreacted (+) gamma-lactam. TheK m andV max value were 2.3±0.2 mM and 80.0±15.4 U mg−1 respectively. The highest activity was found at 30 °C and pH 8.0. ESIMS mass spectrometry analysis results and N-terminal sequence indicated the (−) gamma-lactamase might be a new enzyme.

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Correspondence to Guojun Zheng.

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These authors contributed equally to this work.

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Wang, J., Guo, X., Zheng, G. et al. Purification and characterization of a novel (−) gamma-lactamase fromMicrobacterium hydrocarbonoxydans . Ann. Microbiol. 59, 345–348 (2009). https://doi.org/10.1007/BF03178337

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  • DOI: https://doi.org/10.1007/BF03178337

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