Non-enantioselective alcohol dehydrogenases (ADHs) are rarely found in the biocatalysis portfolio. Generally, highly enantioselective ADHs are sought for. Using such ADHs for the oxidation of racemic alcohols generally results in a kinetic resolution of the starting material, which is unfavourable if the ketone represents the product of interest. In the current contribution we report the ADH from Sphingobium yanoikuyae (SyADH) as non-enantioselective ADH for the complete oxidation or rac-heptan-2-ol (representing further 2-alkanols).@en

Enzymatic methods for the oxidation of alcohols are critically reviewed. Dehydrogenases and oxidases are the most prominent biocatalysts, enabling the selective oxidation of primary alcohols into aldehydes or acids. In the case of secondary alcohols, region and/or enantioselective oxidation is possible. In this contribution, we outline the current state-of-the-art and discuss current limitations and promising solutions.

@en