Enzymatic transesterification of sucrose, alpha-methyl glucopyranoside
and octyl-D-glucopyranoside with tributyrin, vinyl octanoate and viny
l laurate was carried out in nearly anhydrous pyridine using the bacte
rial protease, alcalase. The enzyme monoacylated both the alpha and be
ta anomers of octyl-D-glucopyranoside. In addition to the preferential
acylation of the primary hydroxyl groups of the sugars, the enzyme al
so acylated the secondary hydroxyl groups in lower quantities. The gen
erated sugar mono-, di- and triesters were purified by flash column ch
romatography and the positions of acylation were assigned by C-13 NMR.