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  Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution

Li, G., Maria-Solano, M. A., Romero-Rivera, A., Osuna, S., & Reetz, M. T. (2017). Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution. Chemical Communications, 53(68), 9454-9457. doi:10.1039/C7CC05377K.

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 Creators:
Li, Guangyue1, 2, Author           
Maria-Solano, Miguel A.3, Author
Romero-Rivera, Adrian3, Author
Osuna, Silvia3, Author
Reetz, Manfred T.1, 2, Author           
Affiliations:
1Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445588              
2Philipps-Universität Marburg, Fachbereich Chemie, ou_persistent22              
3Institut de Química Computacional i Catàlisi and Department de Química, Universitat de Girona, Carrer Maria Aurèlia Capmany 6, Girona 17003, Spain , ou_persistent22              

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 Abstract: 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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Language(s): eng - English
 Dates: 2017-08-012017-08-042017-09-04
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C7CC05377K
 Degree: -

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Title: Chemical Communications
  Other : Chem. Commun.
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 53 (68) Sequence Number: - Start / End Page: 9454 - 9457 Identifier: ISSN: 1359-7345
CoNE: https://pure.mpg.de/cone/journals/resource/954928495413