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Issue 99, 2016, Issue in Progress
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Dual enzymatic dynamic kinetic resolution by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase and Candida antarctica lipase B

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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.

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

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Publication details

The article was received on 25 Jul 2016, accepted on 30 Sep 2016 and first published on 04 Oct 2016


Article type: Paper
DOI: 10.1039/C6RA18895H
RSC Adv., 2016,6, 96616-96622

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

    I. Karume, M. M. Musa, O. Bsharat, M. Takahashi, S. M. Hamdan and B. El Ali, RSC Adv., 2016, 6, 96616
    DOI: 10.1039/C6RA18895H

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