Production, characterization and foamability of α-lactalbumin/glycomacropeptide supramolecular structures

- Production of supramolecular structures of the alpha-lactalbumin/glycomacropeptide.
- Processing conditions induced conformational changes in proteins.
- Temperature and pH affected the formation of protein supramolecular structures.
- Calorimetric analysis confirmed the interaction between proteins.
- Self-assembly of proteins can improve techno-functional properties of food.

The study of protein interactions has generated great interest in the food industry. Therefore, research on new supramolecular structures shows promise. Supramolecular structures of the whey proteins α-lactalbumin and glycomacropeptide were produced under varying heat treatments (25 to 75 °C) and acidic conditions (pH 3.5 to 6.5). Isothermal titration calorimetry experiments showed protein interactions and demonstrated that this is an enthalpically driven process. Supramolecular protein structures in aqueous solutions were characterized by circular dichroism and intrinsic fluorescence spectroscopy. Additional photon correlation spectroscopy experiments showed that the size distribution of the structures ranged from 4 to 3545 nm among the different conditions. At higher temperatures, lower pH increased particle size. The foamability of the supramolecular protein structures was evaluated. Analysis of variance and analysis of regression for foaming properties indicated that the two-factor interactions between pH and temperature exhibited a significant effect on the volume and stability of the foam.