Solubilization and Hydrolysis of Ovotransferrin. Solubilization of α-chymotrypsin: Enthalpy changes for three processes

Author： D'Andrea G.   Mucciante V.   Fantauzzi F.  

Publisher： Springer Publishing Company

ISSN： 1388-6150

Source： Journal of Thermal Analysis and Calorimetry, Vol.65, Iss.3, 2001-09, pp. : 737-743

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Abstract

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 α-chymotrypsin (from bovine pancreas) at non-buffered pH 3.0 (0.001 M HCl) both resulted in large exothermic reactions, being the apparent ∆Hs −2485 in the first case and −780.1 kJ mol−1 in the second case, respectively. By contrast, the complete hydrolysis of ovotransferrin (pH 7.8) achieved by using a-chymotrypsin (pH 3.0) gave an endothermic reaction with ∆H=+31.84 kJ mol−1.

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