54315-41-2Relevant articles and documents
ENENTIOSELECTIVE HYDROLYSES BY BAKER'S YEAST - III. MICROBIAL RESOLUTION OF ALKYNYL ESTERS USING LYOPHILIZED YEAST
Glaenzer, B. I.,Faber, K.,Griengl, H.
, p. 5791 - 5796 (1987)
Both enantiomers of optically active 1-alkyn-3-ols were obtained in high optical purity by microbial resolution of their racemic acetate using a stable ready-to-use lyophilized yeast preparation.
Novel chemoenzymatic strategy for the synthesis of enantiomerically pure secondary alcohols with sterically similar substituents
Abad, Jose-Luis,Soldevila, Carles,Camps, Francisco,Clapes, Pere
, p. 5351 - 5356 (2007/10/03)
A novel chemoenzymatic strategy for the synthesis of enantiomerically pure secondary alcohols with sterically similar substituents is described. The key step is the kinetic lipase-catalyzed resolution of racemic mixtures of substituted propargylic alcohols. The efficiency of this new approach was tested in the preparation of the corresponding enantiomers of 1,11-hexadecandiol derivatives ((R)-5 and (S)-5). Two strategies were tested. In the first one, the racemic intermediate 1-octyn-3-ol (1) was resolved enzymatically and then elongated with 1-bromo-9,11-dioxadodecane. Alternatively, the racemic 1 can be elongated to the corresponding racemic 17,19-dioxa-7-eicosyn-6-ol (3) first and then resolved biocatalytically. Twelve commercially available lipases were screened for the kinetic resolution of these intermediates. Among them, Candida antarctica lipase (CAL-B) and Humicola lanuginosa lipase (HLL) were the best biocatalysts for the resolution of 1 (S enantiomer 90% ee, E = 35), and 3 (R enantiomer 90% ee, E = 34), respectively.
