Enzyme-catalyzed partial deacetylation of 1,6-anhydro-2,3,4-tri-O-acetyl-β-D-glucopyranose

Abstract

Various esterases, lipases, and proteases with esterolytic activity were investigated for their power to catalyse deacetylation of 1,6-anhydro-2,3,4-tri-O-acetyl-β-D-glucopyranose. Out of these, chymotrypsin, esterase ex liver, lipase ex pancreas, and lipase ex wheat-germ have been found to be selective catalysts of deacetylation; chymotrypsin and wheat-germ lipase preferably removed the acetyl at C(3), whereas liver esterase and pancreas lipase the acetyl at C(4). Compared to chemical catalysis, whether by methanolic hydrogen chloride or hydrazine hydrate, the locoselectivity of the enzyme-catalysed deacetylation appear to be much better.