Enzymatic resolution of 2,2-disubstituted-1,3-dioxolane-4-methanol carboxylic esters
The enantioselectivity of enzymatic hydrolysis of carboxylic esters of various 1,2-ketals of glycerol has been investigated. The influence of the ketal group has been studied. A number of lipases and proteinases have been tested and the best enantioselectivity was obtained with proteinase from Aspergillus oryzae which gave an E-value of 9 with 2,2-dimethyl-1,3-dioxolane-4-methanol butanoate. Variations in the acyl part revealed that butanoyl was optimal. All hydrolysis products have been synthesised in homochiral forms from homochiral starting materials.
Partali,Melbye,Alvik,Anthonsen
p. 65 - 72
(2007/10/02)
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