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Enzymatic deacetylation of the peracetylated xylosides in anhydrous methanol

V. Kéry, P. Gaduš, and Š. Kučár

Institute of Chemistry, Centre for Chemical Research, Slovak Academy of Sciences, CS-842 38 Bratislava


Abstract: Using serine hydrolases such as trypsin, chymotrypsin, pancreatic lipase and plasmic pseudocholinesterase as the catalysts, a study of the enzymic deacetylation of methyl and umbelliferyl 2,3,4-tri-0-acetyl-β-D-xylopyranosides in anhydrous methanol was carried out. Analysis of the products was performed by means of thin-layer chromatography on silica gel. It was found that the mentioned enzymes catalyzed deacetylation of the peracety­lated xylopyranosides in anhydrous medium. However, deacetylation was inselective, and no increase of the selectivity was reached even when arginine, tyrosine, glycerol, and choline were used as the acceptors of the leaving acetyl groups.

Full paper in Portable Document Format: 442a273.pdf


Chemical Papers 44 (2) 273–280 (1990)

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