Starch Phosphorylase Inhibitor Is β-Amylase

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Abstract
The proteinaceous noncompetitive inhibitor of starch phosphorylase isolated from the root of sweet potato (Ipomoea batatas [L.] Lam.) (TC Chang, JC Su 1986 Plant Physiol 80:534-538) has been identified as a .beta.-amylase. The starch phosphorylase inhibitor and .beta.-amylase activities copurified to give a protein indistinguishable from commercial .beta.-amylase by electrophoretic and immunological methods, and the two activities showed parallel responses in pH, temperature, and inhibitor sensitivity tests. The amylolytic pattern of the inhibitor corresponded to that of .beta.-amylase and its inhibitory effect toward starch phosphorylase was due to neither deprivation of starch, the primer for the phosphorylase assay, nor the inhibitory effect of amylolytic products.

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