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

¹ Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Miguel Servet 177, 50013-Zaragoza, Spain

Differential scanning calorimetry was used to study the thermal stability of bovine ß-LG as influenced by binding of palmitic acid or retinol. Maximum peak temperature and apparent enthalpy of denaturation of ß-LG (70.5 ± 5°C and 267.5 ± 26.5 kJ/mol, respectively) increased significantly when palmitic acid was bound to ß-LG. However, for ß-LG with bound retinol, maximum peak temperature and apparent enthalpy of denaturation are lower than those for ß-LG with bound palmitic acid. The apparent activation energy for ß-LG with bound palmitic acid was higher than that of delipidated ß-LG or ß-LG with bound retinol. These results indicate that the binding of fatty acids to ß-LG may be an important factor in the stabilization of ß-LG structure.

Key Words: ßbeta;-lactoglobulin • palmitic acid • retinol • thermal denaturation

Submitted on September 22, 1993
Accepted on December 21, 1993

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