Amylopectin was digested with a purified alpha-amylase isolated from malted rye-flour. The products of enzyme action were D-glucose, maltose, maltotriose, and a series of branched alpha-limit dextrins having a degree of polymerisation =4; panose was not formed. The identity of the alpha-limit dextrins has been correlated with the ability of the enzyme to hydolyse some, but not all, of the a(1?4)-D-glucosidic linkages in the vicinity of the a-(1?6)-D-glucosidic inter-chain linkages. © 1971.
|Number of pages||7|
|Publication status||Published - Jun 1971|