Using a lipase as a high-throughput screening method for measuring the enantiomeric excess of allylic acetates.
This report describes a high-throughput method for measuring the enantiomeric excess of allylic acetates. 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 determining enantiomeric excess, uses the lipase from Pseudomonas cepacia to hydrolyze the (R) enantiomer of an allylic acetate, while the (S) enantiomer does not react. The rate of the reaction is monitored by measuring 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 the concentration of the (R) enantiomer. This method can process 88 samples in less that 30 min.
Onaran
M Burak
MB
Department of Chemistry, Brown University, Providence, Rhode Island 02912, USA.
Seto
Christopher T
CT
D000085:Acetates / Q000737:chemistry*; D000498:Allyl Compounds / Q000737:chemistry*; D016956:Burkholderia cepacia / Q000201:enzymology; D002384:Catalysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D015394:Molecular Structure; D013237:Stereoisomerism; D013379:Substrate Specificity
D000085:Acetates; D000498:Allyl Compounds; D008049:Lipase