화학공학소재연구정보센터
Enzyme and Microbial Technology, Vol.34, No.5, 523-528, 2004
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 V-max of the modified enzyme was improved by as much as 160 times over the native lipase, in spite of a similar K,,, 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 I 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. (C) 2004 Elsevier Inc. All rights reserved.