The Influence of Different Physicochemical Parameters of the Solvent On The Activity and Selectivity of Lipase.
The asymmetric esterification of octanoic acid with racemic 2-octanol catalyzed by a lipase from Pseudomonas sp. was investigated in several typical solvents. It was found that the catalytic activity and the enantioselectivity of the enzyme were governed by different physicochemical parameters of the solvent employed. While the former depended on the hydrophobicity (lgP) of the solvent, by contrast the latter was a function of the dielectric constant and the dipole moment. A mechanistic model for the binding site of the enzyme was postulated to rationalize this phenomenon based on the results of the kinetic studies of the reaction in some representative solvents.
Gao
Xiu-Gong
XG
School of Biotechnology, Wuxi University of Light Industry, Wuxi 214036, China.
Cao
Shu-Gui
SG
Zhang
Ke-Chang
KC