Characterization of an aldo–keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum |
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Authors: | Yuan-Hui Ma Dan-Qing Lv Shuo Zhou Dun-Yue Lai Zhen-Ming Chen |
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Institution: | 1. Lab of Biocatalysis, Hangzhou Normal University, 402-Building D, 1378 West Wenyi Road, Hangzhou, 311121, China 2. College of Life and Environmental Sciences, Hangzhou Normal University, 16 Xuelin Street, Hangzhou, 310036, China
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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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