Octa-O-Acetyl-Sucrose: Regioselective Deacetylations by Lipolytic Enzymes

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Abstract
Treatment of octa-O-acetyl sucrose (1) with a lipolytic enzyme preparation from the yeast Candida cylindracea in aqueous buffer resulted in the predominant formation of 1′, 2, 3, 3′, 4, 6, 6′-hepta-O-acetyl-sucrose (2). Treatment of 1 with lipase from wheat germ afforded a minor amount of 1′, 2, 3, 3′, 4, 6-hexa-O-acetyl-sucrose (3) together with 2, 3, 3′, 4, 6-penta-O-acetyl-sucrose (4) as the major product. Effects of calcium ions, cosolvents, temperature and enzyme treatment on enzyme activity and selectivity were investigated. Results indicate that so called wheat-germ lipase is actually an esterase. Wheat germ lipase, immobilised on agarose, did not show appreciable activity on octa-O-acetyl-sucrose (1).