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

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 Vmax of the modified enzyme was improved by as much as 160 times over the native lipase, in spite of a similar Km 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.