ENZYMATIC TRANSESTERIFICATION OF SUGARS IN ANHYDROUS PYRIDINE

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.