Effect of Binding of Retinol and Palmitic Acid to Bovine β-Lactoglobulin on Its Resistance to Thermal Denaturation

Abstract

Differential scanning calorimetry was used to study the thermal stability of bovine p-LG as influenced by binding of palmitic acid or retinol. Maximum peak temperature and apparent enthalpy of denaturation of @-LG (70.5 f S'C and 267.5 f 26.5 kJ/mol, respectively) increased significantly when palmitic acid was bound to @-LG. However, for @-LG with bound retinol, maximum peak temperature and apparent enthalpy of denaturation are lower than those for 6-