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The actions of amylases in the vicinity of the phosphate groups at C-3 and C-6 of the glucosyl residues of potato starch and the locations of the phosphate groups in the starch, which were determined by analyses of the phosphorylated products, were summarized.Sweet potato β-amylase and Aspergillus niger glucoamylase cleaved the (1→4)-α-D-linkage of the 6-phosphorylated residue at the non-reducing side but not that of the 3-phosphorylated one, leaving at least one glucosyl residue attached to the 3-phosphorylated one. α-Amylases from various origins cleaved different sites in the vicinity of the 3- and 6-phosphorylated residues, that is, the enzymes from Bacillus subtilis, porcine pancreas and Aspergillus oryzae produced 32-phosphoryl maltotetraose (32-PG4) and 62-phosphoryl maltotriose (62-PG3), 32-PG4 and 63-phosphoryl maltotriose (63-PG3), and 32-PG4 and 63-PG3, respectively, upon exhaustive hydrolysis. The phosphate group at C-6 was as obstructive as the branch linkage of amylopectin, but less obstructive than the phosphate group at C-3. Their inhibitory behavior seemed to reflect a bulk rather than an electronegative effect.Most phosphate groups were found in the amylopectin fraction. The results of analyses of phosphorylatedbranched- and unbranched-chains produced from potato amylopectin on exhaustive β-amylolysis followed by isoamylolysis indicated that the phosphate groups were located mostly in B-chains (chains with side chains) and largely on the outer section of chains of amylopectin, except in the vicinity of the branch linkages.

Actions of various amylases in the vicinity of phosphate groups of potato starch and location of the phosphate groups in the starch.