Efficient resolution of a chiral alcohol (RS)-HMPC by enzymatic transesterification with vinyl acetate using surfactant-modified lipase

Abstract A synthetic surfactant, didodecyl N - d -glucono- l -glutamate (DGG), was used for modification of Pseudomonas sp. lipase (Lipase PS) to prepare optically pure ( S )-4-hydroxy-3-mehtyl-2-(2-propenyl)-2-cyclopenten-1-one (( S )-HMPC) in a solvent-free system. In the enzymatic transesterification reaction, vinyl acetate was employed both as an acyl donor and as a reaction medium. The DGG-modified lipase showed different Machaelis–Menten kinetics and thermal stability from those of the native lipase. The V max of the modified enzyme was improved by as much as 160 times over the native lipase, in spite of a similar K m value to that of the native lipase. Water content of the reaction system containing the DGG-lipase, as estimated to be around 0.1%, was sufficient to fully express the catalytic activity of the surfactant-modified enzyme since introduction of additional water led to a sharp decrease in enzyme activity. When the substrate (HMPC) concentration was as high as 1 M, the reaction reached 40% conversion in 20 h with merely 1.0 mg ml −1 of the DGG-lipase, producing ( R )-HMPC acetate in nearly 100% ee .