| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1349118 | Tetrahedron: Asymmetry | 2007 | 7 Pages |
Different lipases were screened as biocatalysts in the kinetic resolution process of (±)-hept-1-en-3-ol 1, (±)-5-methylhex-1-en-3-ol 2, (±)-6-methylhept-2-en-4-ol 3, (±)-6,6-dimethylhept-2-en-4-ol 4, and 1-phenylbut-3-en-2-ol 5 by enantioselective transesterification. The acylation of (±)-1 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% ee. Low enantioselectivities were observed in the cases of lipase-catalyzed acylation of (±)-3 and (±)-4.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
(R)-5-Methylhex-1-en-3-olC7H14OEe = 91%[α]58923=+12.0 (c 1.9, CHCl3)Source of chirality: enzyme-mediated kinetic resolutionConfiguration predicted: (R)
(S)-3-Methyl-1-vinyl-butyl propionateC10H18O2Ee = 100%[α]58923=-6.9 (c 2.5, CHCl3)Source of chirality: enzyme-mediated kinetic resolutionConfiguration predicted: (S)
(R)-Hept-1-en-3-olC7H14OEe = 96%[α]58923=-8.1 (c 1.1, CHCl3)Source of chirality: enzyme-mediated kinetic resolutionAbsolute configuration: (R)
(S)-1-Vinyl-pentyl propionateC10H18O2Ee = 100%[α]58923=6.5 (c 1.9, CHCl3)Source of chirality: enzyme-mediated kinetic resolutionAbsolute configuration: (S)
(R)-1-Phenylbut-3-en-2-olC10H12OEe = 95%[α]58923=-12.5 (c 1.0, CHCl3)Source of chirality: enzyme-mediated kinetic resolutionAbsolute configuration: (R)
(S)-1-Benzyl-allyl butanoateC10H16O2Ee = 100%[α]58923=-5.9 (c 1.0, CHCl3)Source of chirality: enzyme-mediated kinetic resolutionAbsolute configuration: (S)
