Abstract
Pea proteins are promising oil-in-water emulsifying agents at both neutral and acidic conditions. In an acidic environment, pea proteins associate to form submicrometer-sized particles. Previous studies suggested that the emulsions at acidic pH were stabilized due to a Pickering mechanism. However, protein particles can be in equilibrium with protein molecules, which could play a significant role in the stabilization of emulsion droplets. Therefore, we revisited the emulsion stabilization mechanism of pea proteins at pH 3 and investigated whether the protein particles or the protein molecules are the major emulsifying agent. The theoretical and experimental surface load of dispersed oil droplets were compared, and we found that protein particles can cover only 3.2% of the total oil droplet surface, which is not enough to stabilize the droplets, whereas protein molecules can cover 47% of the total oil droplet surface. Moreover, through removing protein particles from the mixture and emulsifying with only protein molecules, the contributions of pea protein molecules to the emulsifying properties of pea proteins at pH 3 were evaluated. The results proved that the protein molecules were the primary stabilizers of the oil droplets at pH 3.