Difference in Transglycosylation between Human Pancreatic and Salivary α-Amylases

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Abstract
Transglycosylation reactions of α-amylases from human pancreatic juice and saliva were examined by using O-6-deoxy-6-[(2-pyridyl)amino]-α-D-glucopyranosyl-(1→4)-O-α-D-glucopyranosyl-(1→4)-O-α-D-glucopyranosyl-(1→4)-O-α-D-glucopyranosyl(1→4)-O-α-D-glucopyranose as a substrate and O-α-D-glucopyranosyl-(1→4)-O-α-D-glucopyranosyl-(1→4)-1-deoxy-1-[(2-pyridyl)amino]-D-glucitol as an acceptor. The transfer reaction was estimated by quantitation of O-α-D-glucopyranosyl-(1→4)-1-deoxy-1-[(2-pyridyl)amino]-D-glucitol produced by the enzymes from the transfer products, because the acceptor was not hydrolyzed. The amount of O-α-D-glucopyranosyl-(1→4)-1-deoxy-1-[(2-pyridyl)amino]-D-glucitol in the digest with pancreatic α-amylase was six times that in the digest with salivary α-amylase at the stage when the substrate was completely consumed, and the difference increased gradually on further incubation. The phenomenon can be applied to differentiate the two α-amylases in human serum.

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