Racemization of Enantiopure Alcohols Using Two Mutants of Thermoanaerobacter pseudoethanolicus Secondary Alcohol Dehydrogenase

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Abstract

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 languageEnglish
Pages (from-to)13261-13264
Number of pages4
JournalChemistrySelect
Volume6
Issue number46
DOIs
StatePublished - 13 Dec 2021

Bibliographical note

Publisher Copyright:
© 2021 Wiley-VCH GmbH

Keywords

  • Alcohol dehydrogenases
  • biocatalysis
  • enantiopure alcohols
  • racemization

ASJC Scopus subject areas

  • General Chemistry

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