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American Society for Microbiology, Applied and Environmental Microbiology, 12(76), p. 4096-4098, 2010

DOI: 10.1128/aem.02797-09

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Characterization of a Thermostable Short-Chain Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Thermococcus sibiricus

Journal article published in 2010 by Tatiana N. Stekhanova, Andrey V. Mardanov, Ekaterina Y. Bezsudnova, Vadim M. Gumerov ORCID, Nikolai V. Ravin, Konstantin G. Skryabin, Vladimir O. Popov
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

ABSTRACT Short-chain alcohol dehydrogenase, encoded by the gene Tsib_0319 from the hyperthermophilic archaeon Thermococcus sibiricus , was expressed in Escherichia coli , purified and characterized as an NADPH-dependent enantioselective oxidoreductase with broad substrate specificity. The enzyme exhibits extremely high thermophilicity, thermostability, and tolerance to organic solvents and salts.