Tailoring lipase specificity by solvent and substrate chemistries

摘要: An acyl binding structural model has been developed to explain the observed catalytic efficiencies and enantioselectivities of Candida rugosa lipase-catalyzed (trans)esterification reactions involving 2-hydroxy acids vinyl esters, respectively, acylation both cyclic acyclic alcohols. A clear minimum was for six-carbon moieties. Morever, stereoselectivity acid esterification in a number hydrophilic hydrophobic solvents dependent on chain length: S-isomers were acylated lengths six or fewer, whereas R-isomers preferentially esterified eight more