Dual enzymatic dynamic kinetic resolution by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase and Candida antarctica lipase B

Ibrahim Karume, Musa M. Musa, Odey Bsharat, Masateru Takahashi, Samir Hamdan, Bassam El Ali

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

The immobilization of Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase (TeSADH) using sol–gel method enables its use to racemize enantiopure alcohols in organic media. Here, we report the racemization of enantiopure phenyl-ring-containing secondary alcohols using xerogel-immobilized W110A TeSADH in hexane rather than the aqueous medium required by the enzyme. We further showed that this racemization approach in organic solvent was compatible with Candida antarctica lipase B (CALB)-catalyzed kinetic resolution. This compatibility, therefore, allowed a dual enzymatic dynamic kinetic resolution of racemic alcohols using CALB-catalyzed kinetic resolution and W110A TeSADH-catalyzed racemization of phenyl-ring-containing alcohols.
Original languageEnglish (US)
Pages (from-to)96616-96622
Number of pages7
JournalRSC Adv.
Volume6
Issue number99
DOIs
StatePublished - 2016

Bibliographical 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 as well as baseline research funding offered to Prof. Hamdan through King Abdullah University of Science and Technology. The authors thank Prof. Claire Vieille, from the Department of Microbiology and Molecular Genetics at Michigan State University, for providing the plasmids of TeSADH.

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