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The enzymatic kinetic resolution of (RS)-trans-4-phenyl-3-butene-2-ol was investigated by screening a range of lipases both for enantioselective transesterification and for enantioselective hydrolysis of its acetate. The lipase from Pseudomonas cepacia immobilized on diatomaceous earth (PSL-D)-catalyzed asymmetric transesterification was performed on gram scale using isopropenyl acetate as an innocuous acyl donor in organic media affording the (S)-alcohol in high enantiomeric excess (>99% ee) and enantiomeric ratio E >150. The lipase (Candida antarctica B, CAL-B)-catalyzed asymmetric hydrolysis of the racemic acetate was performed on gram scale in phosphate buffer affording the (R)-alcohol in high enantiomeric excess (>99% ee) and enantiomeric ratio E >150. The investigation demonstrates that the transesterification of the racemic alcohol in organic solvent was faster than the hydrolysis of the corresponding acetate in phosphate buffer. A GC method was developed to achieve an effective analytical separation of the enantiomers of both substrate and product in one analysis using the chiral stationary phase heptakis(2,3-di-O-methyl-6-O-tert-butyldimethylsilyl)-â-cyclodextrin.

Item Type:	Refereed Article
Research Division:	Chemical Sciences
Research Group:	Organic chemistry
Research Field:	Organic green chemistry
Objective Division:	Expanding Knowledge
Objective Group:	Expanding knowledge
Objective Field:	Expanding knowledge in the chemical sciences
UTAS Author:	Ghanem, A (Dr Ashraf Ghanem)
ID Code:	57748
Year Published:	2003
Web of Science® Times Cited:	53
Deposited By:	Austn Centre for Research in Separation Science
Deposited On:	2009-08-12
Last Modified:	2009-08-13
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