Actions of Aspergillus oryzae alpha-amylase, potato phosphorylase, and rabbit muscle phosphorylase a and b on phosphorylated (1----4)-alpha-D-glucan.

Aspergillus oryzae alpha-amylase [(1----4)-alpha-D-glucan glucanohydrolase, EC 3.2.1.1] produced O-(6-phosphoryl-alpha-D-glucopyranosyl)-(1----4)-O-alpha-D-glucopyran osy l-(1----4)-D-glucopyranose (6(3)-phosphorylmaltotriose) and O-alpha-D-glucopyranosyl-(1----4)-O-(3-phosphoryl-alpha-D-glucopyranosyl )- (1----4)-O-alpha-D-glucopyranosyl-(1----4)-D-glucopyranose (3(3)-phosphorylmaltotetraose) from potato starch upon exhaustive hydrolysis. These products indicate that the enzyme hydrolyses the same linkages in the vicinity of the 6-phosphorylated residue as porcine-pancreatic alpha-amylase, but hydrolyses different linkages in the vicinity of the 3-phosphorylated residue when compared with B. subtilis and pancreatic alpha-amylases. Potato phosphorylase [(1----4)-alpha-D-glucan:orthophosphate alpha-D-glucosyltransferase, EC 2.4.1.1] and rabbit muscle phosphorylase a and b were unable to by-pass the phosphorylated D-glucosyl residue of 6-phosphorylated (1----4)-alpha-D-glucan, leaving three D-glucosyl residues attached to the 6-phosphorylated residue on the non-reducing side.