Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolutionElectronic supplementary information (ESI) available. See DOI: 10.1039/c7cc05377k

The long-standing problem of achieving high activity of a thermophilic enzyme at low temperatures and short reaction times with little tradeoff in thermostability has been solved by directed evolution, an alcohol dehydrogenase found in hot springs serving as the catalyst in enantioselective ketone r...

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Bibliographic Details
Main Authors Li, Guangyue, Maria-Solano, Miguel A, Romero-Rivera, Adrian, Osuna, Sílvia, Reetz, Manfred T
Format Journal Article
LanguageEnglish
Published 22.08.2017
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Summary:The long-standing problem of achieving high activity of a thermophilic enzyme at low temperatures and short reaction times with little tradeoff in thermostability has been solved by directed evolution, an alcohol dehydrogenase found in hot springs serving as the catalyst in enantioselective ketone reductions. 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).
Bibliography:10.1039/c7cc05377k
Electronic supplementary information (ESI) available. See DOI
ISSN:1359-7345
1364-548X
DOI:10.1039/c7cc05377k