Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase

Musa M. Musa; Robert S. Phillips; Maris Laivenieks; Claire Vieille; Masateru Takahashi; Samir Hamdan

doi:10.1039/c3ob27415b

Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase

Musa M. Musa, Robert S. Phillips, Maris Laivenieks, Claire Vieille, Masateru Takahashi, Samir Hamdan

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33 Scopus citations

Abstract

Controlled racemization of enantiopure phenyl-ring-containing secondary alcohols is achieved in this study using W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus (W110A TeSADH) and in the presence of the reduced and oxidized forms of its cofactor nicotinamide-adenine dinucleotide. Racemization of both enantiomers of alcohols accepted by W110A TeSADH, not only with low, but also with reasonably high, enantiomeric discrimination is achieved by this method. Furthermore, the high tolerance of TeSADH to organic solvents allows TeSADH-catalyzed racemization to be conducted in media containing up to 50% (v/v) of organic solvents. © 2013 The Royal Society of Chemistry.

Original language	English (US)
Pages (from-to)	2911
Journal	Organic & Biomolecular Chemistry
Volume	11
Issue number	17
DOIs	https://doi.org/10.1039/c3ob27415b
State	Published - 2013

ASJC Scopus subject areas

Biochemistry
Organic Chemistry
Physical and Theoretical Chemistry

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10.1039/c3ob27415b

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@article{b5eb3e42b64547e7b48168e8d4e62367,

title = "Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase",

abstract = "Controlled racemization of enantiopure phenyl-ring-containing secondary alcohols is achieved in this study using W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus (W110A TeSADH) and in the presence of the reduced and oxidized forms of its cofactor nicotinamide-adenine dinucleotide. Racemization of both enantiomers of alcohols accepted by W110A TeSADH, not only with low, but also with reasonably high, enantiomeric discrimination is achieved by this method. Furthermore, the high tolerance of TeSADH to organic solvents allows TeSADH-catalyzed racemization to be conducted in media containing up to 50% (v/v) of organic solvents. {\textcopyright} 2013 The Royal Society of Chemistry.",

author = "Musa, {Musa M.} and Phillips, {Robert S.} and Maris Laivenieks and Claire Vieille and Masateru Takahashi and Samir Hamdan",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: The authors acknowledge the support provided by King Abdulaziz City for Science and Technology (KACST) through the Science and Technology Unit at King Fahd University of Petroleum and Minerals (KFUPM) for funding this work through project no. 11-BIO1666-04 as part of the National Science, Technology and Innovation Plan.",

year = "2013",

doi = "10.1039/c3ob27415b",

language = "English (US)",

volume = "11",

pages = "2911",

journal = "Organic & Biomolecular Chemistry",

issn = "1477-0520",

publisher = "Royal Society of Chemistry",

number = "17",

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TY - JOUR

T1 - Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase

AU - Musa, Musa M.

AU - Phillips, Robert S.

AU - Laivenieks, Maris

AU - Vieille, Claire

AU - Takahashi, Masateru

AU - Hamdan, Samir

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: The authors acknowledge the support provided by King Abdulaziz City for Science and Technology (KACST) through the Science and Technology Unit at King Fahd University of Petroleum and Minerals (KFUPM) for funding this work through project no. 11-BIO1666-04 as part of the National Science, Technology and Innovation Plan.

PY - 2013

Y1 - 2013

N2 - Controlled racemization of enantiopure phenyl-ring-containing secondary alcohols is achieved in this study using W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus (W110A TeSADH) and in the presence of the reduced and oxidized forms of its cofactor nicotinamide-adenine dinucleotide. Racemization of both enantiomers of alcohols accepted by W110A TeSADH, not only with low, but also with reasonably high, enantiomeric discrimination is achieved by this method. Furthermore, the high tolerance of TeSADH to organic solvents allows TeSADH-catalyzed racemization to be conducted in media containing up to 50% (v/v) of organic solvents. © 2013 The Royal Society of Chemistry.

AB - Controlled racemization of enantiopure phenyl-ring-containing secondary alcohols is achieved in this study using W110A secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus (W110A TeSADH) and in the presence of the reduced and oxidized forms of its cofactor nicotinamide-adenine dinucleotide. Racemization of both enantiomers of alcohols accepted by W110A TeSADH, not only with low, but also with reasonably high, enantiomeric discrimination is achieved by this method. Furthermore, the high tolerance of TeSADH to organic solvents allows TeSADH-catalyzed racemization to be conducted in media containing up to 50% (v/v) of organic solvents. © 2013 The Royal Society of Chemistry.

UR - http://hdl.handle.net/10754/562489

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U2 - 10.1039/c3ob27415b

DO - 10.1039/c3ob27415b

M3 - Article

C2 - 23525226

SN - 1477-0520

VL - 11

SP - 2911

JO - Organic & Biomolecular Chemistry

JF - Organic & Biomolecular Chemistry

IS - 17

ER -

Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase

Abstract

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