| Abstract
| - This report describes a high-throughput method for measuring the enantiomeric excess of allylicacetates. Such methods are useful tools for screening libraries of potential catalysts for enantioselective reactions. This technique, which is called EMDee for an enzymatic method for determiningenantiomeric excess, uses the lipase from Pseudomonas cepacia to hydrolyze the (R) enantiomer ofan allylic acetate, while the (S) enantiomer does not react. The rate of the reaction is monitored bymeasuring the acetic acid that is produced during the hydrolysis reaction with a pH indicator.Using the Michaelis−Menten equation, the rate of the reaction can be correlated with theconcentration of the (R) enantiomer. This method can process 88 samples in less that 30 min.
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