Kinetic resolution of pipecolic acid using partially-purified lipase from Aspergillus niger

Enzyme-catalyzed hydrolysis facilitated the efficient kinetic resolution of pipecolic acid esters, which were used to synthesize biologically active peptides, alkaloids and immunosuppresants such as FK506. Lipase obtained from Aspergillus niger, had an apparent molecular weight of 32 kDa, and contributed to the enantioselective hydrolysis of octylpipecolate.