Interaction between casein and the oppositely charged surfactant.

The interactions between the classical cationic surfactant dodecyltrimethylammonium bromide (DTAB) and 2.0 mg/mL casein were investigated using isothermal titration calorimetry (ITC), turbidity, dynamic light scattering (DLS), and fluorescence spectra measurements. The results suggest that the cationic headgroup of the surfactant individually binds to the negatively charged amino acid sites on the casein chains because of the electrostatic attraction upon the addition of DTAB. When the surfactant concentration reaches a critical value c1, DTAB forms micelle-like aggregates on the casein chain, resulting in the formation of insoluble casein/DTAB complexes. Further addition of DTAB leads to the redissolution of casein/DTAB complexes because of the net positive charge on casein/DTAB complexes and the formation of DTAB free micelles. The addition of salt screens the repulsion between the surfactant headgroups and the attraction between casein and surfactant molecules, which weakens the binding of surfactant onto the casein chain, favoring the formation of free surfactant micelles.