Lipase-catalyzed access to enantiomerically pure (R)- and (S)-trans-4-phenyl-3-butene-2-ol

• Published in: Tetrahedron: Asymmetry
• Main Authors: Ghanem, A, Schurig, V
• Format: Article in Journal/Newspaper
• Language: English
• Published: Elsevier 2003
• Subjects: Chemical Sciences; Organic Chemistry; Organic Green Chemistry; Antarc*; Antarctica
• Online Access: http://www.sciencedirect.com; https://doi.org/10.1016/S0957-4166(02)00745-0; http://ecite.utas.edu.au/57748

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)--cyclodextrin.