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. © 1971.
Original language | English |
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Pages (from-to) | 339-349 |
Number of pages | 11 |
Journal | Carbohydrate Research |
Volume | 20 |
Issue number | 2 |
Publication status | Published - Dec 1971 |