Lipase-catalysed sequential kinetic resolution of α-lipoic acid

Lipase from Aspergillus sp. WZ002 was employed to kinetically resolve racemicα-lipoic acid by a sequential esterification process. Though the remoteness of this substrate’sstereocentre from the reaction centre provided a significant challenge, the introduction ofsequential kinetic resolution dramatically enhanced the lipase’s enantioselectivity foresterification at the terminal carbonyl group, producing the desired (R)-enantiomer virtuallyenantiomerically pure. The enantiomeric excess of the (R)-enantiomer increased from 52% inthe first step to 92% for in second step.