1. Characterization of an aldo-keto reductase from Thermotoga maritima with high thermostability and a broad substrate spectrum.
- Author
-
Ma YH, Lv DQ, Zhou S, Lai DY, and Chen ZM
- Subjects
- Aldehyde Reductase, Aldo-Keto Reductases, Enzyme Stability, Kinetics, Stereoisomerism, Substrate Specificity, Temperature, Alcohol Oxidoreductases chemistry, Alcohol Oxidoreductases metabolism, Thermotoga maritima enzymology
- 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 %.
- Published
- 2013
- Full Text
- View/download PDF