Potato amylopectin was hydrolyzed with the alpha-amylase of Bacillus a
myloliquefaciens to produce intermediate a-dextrins with a degree of p
olymerization < 1000. The products were then fractionated by methanol
precipitation into samples of different size distributions that were a
nalyzed by gel-permeation chromatography. All samples contained mixtur
es of high and low molecular weight dextrins, but in different proport
ions. Selected fractions were treated successively with phosphorylase
and beta-amylase to obtain phi,beta-limit dextrins. A further alpha-am
ylolysis of the limit dextrins was performed to investigate their comp
ositions and suggested that the amylopectin was build up of structural
ly different domains. The size of the units of clusters probably range
d from dp 30-70. Dextrins of this size were only slowly hydrolyzed fur
ther by the alpha-amylase and the long internal chains had been hydrol
yzed into chains of intermediate lengths. The ratio of A:B-chains and
of A:Ba-chains increased with decreasing size of the dextrins, whereas
Ba:Bb-chains decreased. The changes in the ratios can be used to inve
stigate the mode of interconnection of structural units in the amylope
ctin. (C) 1996 Elsevier Science Ltd.