Studies on carbohydrate-metabolising enzymes : Part XXVII. A comparison of the action of yeast isoamylase and bacterial pullulanase on amylopectin

Abstract

The action of purified yeast isoamylase on amylopectin, like that of bacterial pullulanase, results in the hydrolysis of the outermost inter-chain linkages with the liberation of linear maltosaccharides having an average degree of polymerisation of approximately 15 D-glucose residues. This hydrolytic action distinguishes yeast isoamylase from yeast amylo-(1→6)-glucosidase, which acts by a combination of transferase and glucosidase activities. The products of enzyme action on amylopectin are discussed in relation to the probable molecular structure of the polysaccharide.