The enzymic deacylation of esterified mono- and di-saccharides. IV. The products of esterase-catalyzed deacetylations

Abstract

Wheat germ lipase, or a purified esterase from it, catalyzed the deacylation of peracylated glucose and glucose-containing disaccharides in the pH range 5.6–8.1 at 25–37 °C with the substrate in either a homogeneous or heterogeneous state. Acetyl groups were hydrolyzed 12 times more rapidly than propionyl and 25 times more rapidly than benzoyl groups. Partially acylated compounds were separated by preparative chromatography. Analysis of these intermediates indicated a preferential order of removal of acetyl groups, namely [Formula: see text]. Measurement of initial rates of deacetylation were in accord with the results from the product analysis of the intermediates. The Km values for the peracetylated disaccharides were quite similar and exhibited an order of magnitude less than that observed for the monosaccharide.