Abstract

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 α(1→4)- D-glucosidic linkages in the vicinity of the α-(1→6)- D-glucosidic inter-chain linkages.

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