| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1350699 | Tetrahedron: Asymmetry | 2006 | 8 Pages |
The enzymatic resolution of racemic mixtures of hydroxy tellurides with a range of lipases has been investigated. Lipase-B from Candida antarctica (CALB) gave the best conversions, providing both enantiomers with high enantiomeric purity. A comparative study of the effect of solvent and substrate on the enzymatic kinetic resolution was performed.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
(S)-1-(Phenyltellanyl)-2-propanolC9H12OTeEe > 99%[α]D28=+5 (c 1.0, CH2Cl2)Absolute configuration: S
(S)-1-(n-Butyltellanyl)-2-propanolC7H16OTeEe > 99%[α]D23=+33 (c 1.0, CH2Cl2)Absolute configuration: S
(S)-1-(n-Butyltellanyl)-3-butanolC8H18OTeEe = 99%[α]D22=+7 (c 1.0, CH2Cl2)Absolute configuration: S
(R)-O-Acetyl-1-(phenyltellanyl)-2-propanolC11H14O2TeEe > 99%[α]D22=-6 (c 1.0, CH2Cl2)Absolute configuration: R
(R)-O-Acetyl-1-(n-butyltellanyl)-2-propanolC9H18O2TeEe = 98%[α]D22=+4 (c 1.0, CH2Cl2)Absolute configuration: R
(R)-O-Acetyl-1-(n-butyltellanyl)-3-butanolC10H20O2TeEe = 98%[α]D22=+18 (c 1.0, CH2Cl2)Absolute configuration: R
