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A comparative study of various hydrolases enables the identification of two hydrolases, Lipase from Candida rugosa (CRL) and cholesterol esterase (CE), exhibiting enantioselectivity in the hydrolysis of pendant acetates in chiral phosphines and phosphine oxides. Both hydrolases exhibit efficient enantioselectivity toward the phosphine oxide ArPhMeP double bond O. Resolution of this phosphine oxide by CRL produces an enantiomerically-enriched starting acetate and a product alcohol, which on stereospecific reduction produces both enantiomers of phosphine ArPhMeP.

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.

X-ray crystallography was used to determine the mechanism by which lipase from Candida rugosa differentiates between enantiomers of menthol. This mechanism may elucidate the structural features in lipases that are associated with enantiorecognition. Phosphonates were covalently linked to the active site serene to imitate the transition state for menthyl ester hydrolysis.

The scissile fatty acyl sequence of the Candida rugosa lipase-inhibitor complex is bound in a hydrophobic channel. The bound lipid has a 'tuning fork' shape. The tetrahedral intermediates of the acylation step centralizes oxyanion hole components and indicates ester hydrolysis. The stereochemistry of ester hydrolysis is same in all lipases.