Racemization of enantiopure alcohols is the key step to accomplish a dynamic kinetic resolution, and thus overcome the intrinsic drawback of 50 % yield with high enantioselectivity that is associated with kinetic resolution. Herein, the concurrent use of I86A and W110G mutants of Thermoanaerobacter pseudoethanolicus secondary alcohol dehydrogenase (TeSADH) in racemization of enantiopure phenyl-ring-containing alcohols is reported. The efficiency of this bienzymatic racemization approach is also compared with that reported previously using W110G TeSADH and is marginally more efficient.
|Original language||English (US)|
|Number of pages||4|
|State||Published - Dec 6 2021|
Bibliographical noteKAUST Repository Item: Exported on 2022-05-25
Acknowledgements: The author gratefully acknowledges funding by Deanship of Scientific Research (DSR) at King Fahd University of Petroleum and Minerals (KFUPM), project number DF191007. The author also thanks Professor Claire Vieille, from the Department of Microbiology and Molecular Genetics and Department of Biochemistry and Molecular Biology at Michigan State University, for providing the plasmid of TeSADH, and Professor Samir M. Hamdan, from the Division of Biological and Environmental Sciences and Engineering at King Abdullah University of Science and Technology, for providing purified TeSADH mutants.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.