Fluid laminarization process and rheological properties of protein-stabilized high internal phase emulsions

Protein-based high internal phase emulsions (HIPEs) have gained tremendous attention in diverse fields, but their mechanism in the emulsification process remains elusive. In this article, HIPEs were stabilized directly by food-grade proteins, depending on a self-organized process featuring a fluid laminarization. We elucidated that the emulsification with the rotor-stator mixer is a typical non-equilibrium process. The crucial factor for the process is related to the irreversible energy dissipation, while the internal phase volume fraction is the threshold determining the laminarization. The feasible explanation speculated that the transition corresponds to the dissipative structure, i.e., compressive droplets, arising from the spatiotemporal self-organization, to dissipate the turbulent kinetic energy. We found a new paradigm of dissipative structure, comprehending such structure in the HIPEs emulsification process, which is expected to pave the way for its industrial-scale production with the virtue of low-cost proteins.