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 language | English |
|---|---|
| Pages (from-to) | 13261-13264 |
| Number of pages | 4 |
| Journal | ChemistrySelect |
| Volume | 6 |
| Issue number | 46 |
| DOIs | |
| State | Published - 13 Dec 2021 |
Bibliographical note
Publisher Copyright:© 2021 Wiley-VCH GmbH
Keywords
- Alcohol dehydrogenases
- biocatalysis
- enantiopure alcohols
- racemization
ASJC Scopus subject areas
- General Chemistry