Kinetic resolution of glyceraldehyde using an aldehyde dehydrogenase from Deinococcus geothermalis DSM 11300 combined with electrochemical cofactor recycling

Glyceraldehyde and glyceric acid are both valuable chiral starting materials. Aldehyde dehydrogenases (ALDHs) accept a broad scope of endo- and exogenous aldehydes, such as glyceraldehyde, and convert them into the corresponding carboxylic acid. Here we present cloning, overexpression and kinetic data on two ALDHs from Escherichia coli BL21 and Deinococcus geothermalis. The two ALDHs have a similar substrate scope and favor short to medium chain aldehydes, both oxidize glyceraldehyde to glyceric acid. The ALDH variant of D. geothermalis shows the higher specific activity towards glyceraldehyde and has an elevated activity optimum compared with the BL21 enzyme. The ALDH of G. geothermalis was also applied to conduct a kinetic resolution of glyceraldehyde with electrochemical cofactor recycling.

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► Cloning, overexpression and kinetic data of E. coli and D. geothermalis ALDH.
► Both ALDHs favor short to medium chain aldehydes.
► D. geothermalis ALDH: thermostable, higher vmax towards glyceraldehyde.
► Kinetic resolution of glyceraldehyde with electrochemical cofactor recycling.