THERMODYNAMIC STUDIES ON THE INTERACTION OF COBALT WITH ALPHA-AMYLASE

The interaction of cx-amylase from Bacillus amyloliquefaciens with div alent cobalt ion was studied by equilibrium dialysis and isothermal ti tration microcalorimetry methods at 27 degrees C in neutral solution a t pH = 7.0. A new equation with a useful graphical method, very simila r to the Scatchard plot was introduced to obtain a dissociation equili brium constant using microcalorimetric data. The constant is remarkabl y like that obtained from a normal Scatchard plot, which uses equilibr ium dialysis data. The enzyme activity increased significantly with an increasing concentration of cobalt; however, the temperature of denat uration of the enzyme decreased.