1. Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution
- Author
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Miguel A. Maria-Solano, Sílvia Osuna, Manfred T. Reetz, Adrian Romero-Rivera, and Guangyue Li
- Subjects
Ketone ,Catalitzadors ,010402 general chemistry ,01 natural sciences ,Catalysis ,Enzyme Stability ,Materials Chemistry ,Organic chemistry ,Cinètica enzimàtica ,Thermostability ,Alcohol dehydrogenase ,chemistry.chemical_classification ,Catalysts ,biology ,010405 organic chemistry ,Thermophile ,Enzyme kinetics ,Cinètica química ,Alcohol Dehydrogenase ,Temperature ,Metals and Alloys ,Enantioselective synthesis ,Stereoisomerism ,General Chemistry ,Ketones ,Directed evolution ,humanities ,0104 chemical sciences ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,Chemical kinetics ,Enzyme ,chemistry ,Biocatalysis ,Ceramics and Composites ,biology.protein ,Directed Molecular Evolution - Abstract
Turn cool off and stay active: the thermostable alcohol dehydrogenase TbSADH originating from the hot springs of Yellow Stone Park was successfully subjected to directed evolution for inducing high activity at ambient temperatures and enabling short reaction times with minimal tradeoff in thermostability. Reversed enantioselectivity was also evolved (99% ee).
- Published
- 2017
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