Flexibility and Charge of Solutes as Factors That Determine Their Diffusion in Casein Suspensions and Gels

This work explores the influence of both the physicochemical characteristics of solutes and the solute–matrix interactions on diffusion in casein systems. Diffusion coefficients of three solute groups (dextrans, proteins, and peptides) presenting different physicochemical characteristics, such as molecular flexibility and charge, were measured using the technique of fluorescence recovery after photobleaching (FRAP). The casein systems had the same casein concentration, but different microstructures (suspension or gel), and/or a different pH (5.2 or 6.6). Flexible solutes diffused more rapidly through the casein systems than the rigid ones. Electrostatic interactions between charged solute molecules and the casein matrix were partly screened due to the high ionic strength of the systems. As a consequence, it was the flexibility of the solute molecule (rather than its charge) that most influenced its diffusion through casein systems.