AbstractProtein aggregation into gel networks is of immense importance in diverse areas from food science to medical research; however, it remains a grand challenge as the underlying molecular interactions are complex, difficult to access experimentally, and to model computationally. Early stages of gelation often involve protein aggregation into protein clusters that later on aggregate into a gel network. Recently synthesized protein microparticles allow direct control of these early stages of aggregation, decoupling them from the subsequent gelation stages. Here, by following the gelation of protein microparticles directly at the particle scale, we elucidate in detail the emergence of a percolating structure and the onset of rigidity as measured by microrheology. We find that the largest particle cluster, correlation length, and degree of polymerization all diverge with power laws, while the particles bind irreversibly indicating a nonequilibrium percolation process, in agreement with recent results on weakly attractive colloids. Concomitantly, the elastic modulus increases in a power-law fashion as determined by microrheology. These results give a consistent microscopic picture of the emergence of rigidity in a nonequilibrium percolation process that likely underlies the gelation in many more systems such as proteins, and other strongly interacting structures originating from (bio)molecules.
Influence of Pea and Potato Protein Microparticles on Texture and Sensory Properties in a Fat-Reduced Model Milk Dessert
