A flow-calorimetric study of the binding of iodine to amylodextrin fractions.

Acid hydrolyzates of waxy-maize starch were separated to give Fractions I, II, and III [T. Watanabe, and D. French, Carbohydr. Res., 84 (1980) 115-123]. Watanabe and French suggested that Fraction II, which contains approximately 25 D-glucose residues including an alpha-D-(1----6)-linked branch, has a double helical structure. In the present study, the thermodynamics of binding of iodine to Fractions II and III, and debranched Fraction II (Fraction II') was measured by isothermal-flow calorimetry. If four binding sites for Fraction II and two for Fractions II' and III are assumed, the standard free-energy changes, delta Gb0, for the binding of I2 are -18.5, -18.8, and -18.4 kJ X (mol I2)-1, and the enthalpy changes, delta Hb, are -28.4, -24.7, and -26.9 kJ X (mol I2)-1, respectively. The similarity of these values for the three fractions indicates that the conformation of Fraction II is essentially the same as those of Fractions II' and III, and that Fraction II, therefore, does not have a double helical structure in solution. The values for delta Gb0 are approximately 15 kJ X mol-1 less negative, and those for delta Hb approximately 40 kJ X mol-1 less negative than published values for the starch-I2 complex. These differences are due to the relatively very short D-glucose chains in the amylodextrin fractions employed in the present work.