Journal
CHEMICAL COMMUNICATIONS
Volume 53, Issue 68, Pages 9454-9457Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7cc05377k
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Funding
- Max-Planck-Society
- LOEWE cluster SynChemBio
- Generalitat de Catalunya [2015-FI-B-00165]
- Spanish MINECO [BES-2015-074964, CTQ2014-59212-P]
- European Community [PCIG14-GA-2013-630978]
- European Research Council (ERC) under European Union's Horizon research and innovation programme [ERC-2015-StG-679001]
- [RYC-2014-16846]
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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.
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