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

• Published in: RSC Advances
• Main Authors: Karume, Ibrahim, Musa, Musa M., Bsharat, Odey, Takahashi, Masateru, Hamdan, Samir, El Ali, Bassam
• Other Authors: Biological and Environmental Sciences and Engineering (BESE) Division, Bioscience Program, Department of Chemistry, King Fahd University of Petroleum and Minerals, Dhahran, Saudi Arabia
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: Royal Society of Chemistry (RSC) 2016
• Subjects: Antarc*; Antarctica
• Online Access: http://hdl.handle.net/10754/622392; https://doi.org/10.1039/c6ra18895h

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. 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.