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

Handle URI:
http://hdl.handle.net/10754/622392
Title:
Dual enzymatic dynamic kinetic resolution by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase and Candida antarctica lipase B
Authors:
Karume, Ibrahim; Musa, Musa M.; Bsharat, Odey; Takahashi, Masateru; Hamdan, Samir ( 0000-0001-5192-1852 ) ; El Ali, Bassam
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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Karume I, Musa MM, Bsharat O, Takahashi M, Hamdan SM, et al. (2016) Dual enzymatic dynamic kinetic resolution by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase and Candida antarctica lipase B. RSC Adv 6: 96616–96622. Available: http://dx.doi.org/10.1039/c6ra18895h.
Publisher:
Royal Society of Chemistry (RSC)
Journal:
RSC Adv.
Issue Date:
4-Oct-2016
DOI:
10.1039/c6ra18895h
Type:
Article
ISSN:
2046-2069
Sponsors:
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.
Additional Links:
http://pubs.rsc.org/en/Content/ArticleLanding/2016/RA/C6RA18895H
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorKarume, Ibrahimen
dc.contributor.authorMusa, Musa M.en
dc.contributor.authorBsharat, Odeyen
dc.contributor.authorTakahashi, Masateruen
dc.contributor.authorHamdan, Samiren
dc.contributor.authorEl Ali, Bassamen
dc.date.accessioned2017-01-02T09:28:28Z-
dc.date.available2017-01-02T09:28:28Z-
dc.date.issued2016-10-04en
dc.identifier.citationKarume I, Musa MM, Bsharat O, Takahashi M, Hamdan SM, et al. (2016) Dual enzymatic dynamic kinetic resolution by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase and Candida antarctica lipase B. RSC Adv 6: 96616–96622. Available: http://dx.doi.org/10.1039/c6ra18895h.en
dc.identifier.issn2046-2069en
dc.identifier.doi10.1039/c6ra18895hen
dc.identifier.urihttp://hdl.handle.net/10754/622392-
dc.description.abstractThe 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.en
dc.description.sponsorshipThe 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.en
dc.publisherRoyal Society of Chemistry (RSC)en
dc.relation.urlhttp://pubs.rsc.org/en/Content/ArticleLanding/2016/RA/C6RA18895Hen
dc.titleDual enzymatic dynamic kinetic resolution by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase and Candida antarctica lipase Ben
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalRSC Adv.en
dc.contributor.institutionDepartment of Chemistry, King Fahd University of Petroleum and Minerals, Dhahran, Saudi Arabiaen
kaust.authorTakahashi, Masateruen
kaust.authorHamdan, Samiren
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