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

11 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

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