Abstract
The enantioselectivity of lipase from Candida rugosa in the hydrolysis of methyl 2-chloropropionate was measured at several substrate concentrations. Initial reaction rates for the pure enantiomers differ by a factor of 2.1 (low substrate concentration) and 1.6 (high substrate concentration), respectively. Determination of the enantiomeric ratio, E-value, in (1) kinetic resolution experiments, and (2) by the method of initial reaction rates on mixed enantiomers, however, showed E=1 (no enantioselectivity) for the full range of substrate concentrations.
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