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. © 1971.
|Number of pages||11|
|Publication status||Published - Dec 1971|