Chemoenzymatic DKR of tertiary alcohol rac-1

Dynamic kinetic resolution (DKR) of a racemic tertiary alcohol (rac-1) was investigated using lipase CAL-A in combination with a heterogeneous oxovanadium catalyst V-MPS4. In this method, an optically pure ester (R)-2 was produced via simultaneous lipase-catalyzed kinetic resolution and the V-MPS4-catalyzed racemization of unreacted alcohol (S)-1. In this case, the reaction fields of lipase and V-MPS4 were separated with polydimethylsiloxane thimble because the catalytic activity of each of them decreased as a result of mutual deactivation. This table summarizes the effect of native lipase and its double mutant on DKR. Two protocols were carried out, with the addition of lipase and V-MPS4 two and three times during the entire reaction period, and their effects on the conversion were also investigated.