Interaction between casein and sodium dodecyl sulfate

The interaction of the anionic surfactant sodium dodecyl sulfate (SDS) with 2.0 mg/ml casein was first investigated using isothermal titration calorimetry (ITC), dynamic light scattering (DLS), and fluorescence spectra. ITC results show that individual SDS molecules first bind to casein micelles by the hydrophobic interaction. The micelle-like SDS aggregate is formed on the casein chains when SDS concentration reaches the critical aggregation concentration (c1c1), which is far below the critical micellar concentration (cmc) of SDS in the absence of casein. With the further increase of SDS concentration to the saturate binding concentration c2c2, SDS molecules no longer bind to the casein chains, and free SDS micelles coexist with casein micelles bound with SDS aggregates in the system. DLS results show that the addition of SDS leads to an increase in the hydrodynamic radius of casein micelles with bound surfactant at SDS concentration higher than 4 mM, and also an increase in the casein monomer molecule (or submicelles) at SDS concentration higher than 10 mM. Fluorometric results suggest the addition of SDS leads to some changes in the binding process of hydrophobic probes to casein micelles.

Graphical abstractThe isothermal titration curves for titrating 200 mM SDS into (■) 0; (●) 0.25; (▴) 0.5; (▾) 1.0; (♦) 2.0; (◂) 5.0 mg/mL casein solution.Figure optionsDownload full-size imageDownload as PowerPoint slide