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Characterization of an aldo–keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum

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Abstract

A novel aldo–keto reductase gene, Tm1743, from Thermotoga maritima was overexpressed in Escherichia coli. The enzyme displayed the highest activity at 90 °C and at pH 9. It retained 63 % of its activity after 15 h at 85 °C. The enzyme also could tolerate (up to 10 % v/v) acetonitrile, ethanol and 2-propanol with slightly increased activities. Methanol, DMSO and acetone decreased activity slightly. Furthermore, Tm1743 exhibited broad substrate specificity towards various keto esters, ketones and aldehydes, with relative activities ranging from 2 to 460 % compared to the control. Its optimum substrate, 2,2,2-trifluoroacetophenone, was asymmetrically reduced in a coupled NADPH-regeneration system with an enantioselectivity of 99.8 % and a conversion of 98 %.

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Acknowledgments

This work was supported by a project (20101131N06) from the Science & Technology Department of Hangzhou, China.

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Authors and Affiliations

  1. Lab of Biocatalysis, Hangzhou Normal University, 402-Building D, 1378 West Wenyi Road, Hangzhou, 311121, China

    Yuan-Hui Ma, Dan-Qing Lv, Shuo Zhou, Dun-Yue Lai & Zhen-Ming Chen

  2. College of Life and Environmental Sciences, Hangzhou Normal University, 16 Xuelin Street, Hangzhou, 310036, China

    Yuan-Hui Ma

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  1. Yuan-Hui Ma
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  2. Dan-Qing Lv
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  3. Shuo Zhou
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  4. Dun-Yue Lai
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Correspondence to Zhen-Ming Chen.

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Ma, YH., Lv, DQ., Zhou, S. et al. Characterization of an aldo–keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum. Biotechnol Lett 35, 757–762 (2013). https://doi.org/10.1007/s10529-013-1141-6

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  • DOI: https://doi.org/10.1007/s10529-013-1141-6

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