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Expression, purification and characterization of a thermostable leucine dehydrogenase from the halophilic thermophile Laceyella sacchari

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Abstract

Objective

A potential thermotolerant l-leucine dehydrogenase from Laceyella sacchari (Ls-LeuDH) was over-expressed in E. coli, purified and characterized.

Results

Ls-LeuDH had excellent thermostability with a specific activity of 183 U/mg at pH 10.5 and 25 °C. It retained a high activity in 200 mM carbonate buffer from pH 9.5 to 11. The optimal temperature for Ls-LeuDH was 60 °C.

Conclusion

It is the first time that a thermostable and highly active LeuDH originating from L. sacchari has been characterized. It may be useful for medical and pharmaceutical applications.

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Acknowledgments

This research was financially supported by the State Key Basic Research and Development Plan of China (2009CB724700) and PCSIRT (IRT_14R28) and PAPD. We thank Dr Songi Han for carefully reading the manuscript.

Supporting Information

Supplementary Fig. 1—Kinetics analysis of the reaction catalyzed by Ls-LeuDH.

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Authors and Affiliations

  1. College of Biotechnology and Pharmaceutical Engineering, Nanjing Technology University, Nanjing, 211800, People’s Republic of China

    Wenjun Zhu, Yan Li, Honghua Jia, Ping Wei, Hua Zhou & Min Jiang

Authors
  1. Wenjun Zhu
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  2. Yan Li
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  3. Honghua Jia
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  4. Ping Wei
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  5. Hua Zhou
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  6. Min Jiang
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Corresponding author

Correspondence to Honghua Jia.

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Zhu, W., Li, Y., Jia, H. et al. Expression, purification and characterization of a thermostable leucine dehydrogenase from the halophilic thermophile Laceyella sacchari . Biotechnol Lett 38, 855–861 (2016). https://doi.org/10.1007/s10529-016-2053-z

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  • DOI: https://doi.org/10.1007/s10529-016-2053-z

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