Abstract
Dialdehyde derivatives of cyclodextrin (dial-CD) were prepared by the periodate oxidation method. The dial-CD inhibited not only exo-type amylases (β-amylase and glucoamylase) but also endo-type α-amylase, and the degree of inhibition was much stronger than that with the corresponding native cyclodextrin (CD). α-Glucan phosphorylases from muscle, yeast, and potato were also inhibited by the dial-CD and the resulting Ki values for the muscle enzyme were 7 - 8-fold lower than those of the native CD. A progressive inactivation of the muscle phosphorylase by the dial-α-CD suggested that this compound would be useful as an affinity-labeling reagent for phosphorylase. Although the dial-CD was less effective for the irreversible inactivation of amylases than the phosphorylase, the potent inhibition of several amylases by the dial-CD would provide an useful inhibitory compound for kinetic analysis.
