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Characterization of a thermostable short-chain alcohol dehydrogenase from the hyperthermophilic archaeon thermococcus sibiricus

Applied and Environmental Microbiology (2010) 76(12) 4096-4098
DOI: 10.1128/AEM.02797-09
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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. Copyright © 2010, American Society for Microbiology. All Rights Reserved.

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Stekhanova, T. N., Mardanov, A. V., Bezsudnova, E. Y., Gumerov, V. M., Ravin, N. V., Skryabin, K. G., & Popov, V. O. (2010). Characterization of a thermostable short-chain alcohol dehydrogenase from the hyperthermophilic archaeon thermococcus sibiricus. Applied and Environmental Microbiology, 76(12), 4096–4098. https://doi.org/10.1128/AEM.02797-09

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