Kinetic resolution of racemic secondary aliphatic allylic alcohols in lipase-catalyzed transesterification

Different lipases were screened as biocatalysts in the kinetic resolution process of (+/-)-hept-1-en-3-ol 1, (+/-)-5-methylhex-1-en3-ol 2, (+/-)-6-methythept-2-en-4-ol 3, (+/-)-6,6-dimethylhept-2-en-4-ol 4, and 1-phenylbut-3-en-2-ol 5 by enantio selective transesterification. The acylation of (+/-)-l and (+/-)-2 catalyzed by Novozym 435 (Candida antarctica) was very effective and proceeded with good enantioselectivity. After 4-8 h of reactions the esters formed and the alcohols, which remained were obtained with high enantiomeric excess with 97-100% ee and 91-100% ee, respectively. The lipase Amano PS (Burkholderia cepacia) was the best catalyst in the asymmetric transesterification of (+/-)-5 affording the (R)-alcohol with 90-95% ee and the (S)-ester with 98-100% ce. Low enantio selectivities were observed in the cases of lipase-catalyzed acylation of (+/-)-3 and (+/-)-4. (c) 2007 Elsevier Ltd. All rights reserved.