Collect. Czech. Chem. Commun.
1987, 52, 2347-2352
https://doi.org/10.1135/cccc19872347
Enzyme-catalyzed partial deacetylation of 1,6-anhydro-2,3,4-tri-O-acetyl-β-D-glucopyranose
Jiří Zemeka, Štefan Kučárb and Dušan Anderleb
a Institute of Biotechnology, Slovak Institute of Technology, 812 37 Bratislava
b Institute of Chemistry, Centre of Chemical Research, Slovak Academy of Sciences, 842 38 Bratislava
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.
