An efficient preparative scale resolution of 3-phenylbutyric acid by lipase from Burkholderia cepacia (Chirazyme L1) |
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| Institution: | 1. School of Mechanical Engineering and Automation, P.O. Box 319, Northeastern University, No. 11 Lane 3, Wenhua Rd, Heping District, Shenyang 110819, Liaoning Province, PR China;2. Department of Mechanical and Biofunctional Systems, Institute of Industrial Science, The University of Tokyo, Komaba 4-6-1, Meguro, Tokyo 153-8505, Japan |
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| Abstract: | Lipase from Burkholderia cepacia (Chirazyme L1) catalysed the highly enantioselective hydrolysis of racemic methyl 3-phenylbutyrate to afford (R)-(−)-methyl 3-phenylbutyrate of >98% ee (E>50). The resolution was performed at 150 g scale yielding 68.7 g of (R)-(−)-methyl 3-phenylbutyrate (>98% ee, 92% yield on enantiomer) and (S)-(+)-3-phenylbutyric acid of 89% ee. |
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