Kinetic resolution of secondary alcohols with commercial lipases : Application to rootworm sex pheromone synthesis.

The relative rates of enzyme-catalyzed esterification of the enantiomers of 2-octanol with various acids were determined for several commercial lipases. Interesterifications and hydrolyses of racemic 2-octanol esters catalyzed by these enzymes were also examined. Novo'sMucor miehei lipase exhibited considerable enantioselectivity and was therefore employed to prepare 8-methyl-2-decanols with high configurational purity at the carbinol carbon. Esters of these alcohols had been previously identified as sexually attractive to several rootworm (Diabrotica) species, and the stereochemistry of those esters had been shown to be critical to the attraction. The enzymatic resolution provides a convenient method to obtain such esters in a desired state of configurational purity.