Abstract
Lipase PS from Burkholderia cepacia in its free, commercial form (BCL-PS), immobilised in a sol–gel (BCLxero) and as a CLEA (BCL-CLEA) was tested in dry organic solvents, ionic liquids and their mixtures. Utilising the acylations of secondary alcohols 1–3 the influence of the enzyme preparation on its activity and enantioselectivity was studied. BCL-CLEA displays higher activity (initial rates) than BCLxero for all substrates in the ILs but loses its activity rapidly. Thus, BCLxero is suitable for kinetic resolution in ILs and in their mixtures with organic solvents. It is not possible to label one IL better than the other without taking the nature of the substrate into account. In neat solvents, the nature of the solvent affects enantioselectivity (E) only when furyl-substituted alcohol 2 serves as a substrate while variation in E is more evident for reactions in solvent mixtures.
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