Abstract
Aspergillus oryzae alpha-amylase [(1→4-α- d-glucan glucanohydrolase, EC 3.2.1.1] produced O-6-phosphoryl-α- d-glucopyranosyl)-(1→4)- O-α- d-glucopyranosyl-(1→4)- d-glucopyranose (6 3-phosphorylmaltotriose) and O-α- d-glucopyranosyl-(1→4)- O-(3-phosphoryl-α- d-glucopyranosyl)-(1→4)- O-α- 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)-α- d-glucan:orthophosphate α- d-glucosyl-transferase, 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)-α- d-glucan, leaving three d-glucosyl residues attached to the 6-phosphorylated residue on the non-reducing side.
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