Solubilization and hydrolysis of ovotransferrin. Solubilization of alpha-chymotrypsin. Enthalpy changes for three processes

At 298.15 K, the solubilization of hen ovotransferrin at buffered pH 7.8 (0 .08 M Tris . HCl buffer, containing 0.1 M CaCl2) and the solubilization of alpha -chymotrypsin (from bovine pancreas) at non-buffered pH 3.0 (0.001 M HCl) both resulted in large exothermic reactions, being the apparent Delta Hs -2485 in the first case and -780.1 kJ mol(-1) in the second case, respec tively. By contrast, the complete hydrolysis of ovotransferrin (pH 7.8) ach ieved by using alpha -chymotrypsin (pH 3.0) gave an endothermic reaction wi th DeltaH=+31.84 kJ mol(-1).