Pea protein has attracted widespread attention due to its high nutritional value, low allergenicity, non-GMO status, and broad availability. However, compared to animal proteins, pea protein has inferior functional properties, which limits its application in the food industry. This study used pea protein isolate (PPI) as the main raw material and investigated the effects of high-pressure homogenization (HPH), ultrasonic treatment (US), and the combination of the two in different orders on the structure and function of PPI. The results showed that HPH or US promoted the transformation of PPI insoluble suspension into a uniform protein dispersion, significantly reducing particle size, unfolding the spatial structure, exposing more amino acid residues. These structural changes resulted in a substantial increase in the solubility, foaming capacity and emulsifying activity of PPI. Moreover, the combined treatments further impacted the properties of PPI, largely depending on the order of the processing steps; the combination of HPH-US exhibited the best functional characteristics.

There is increasing interest in using plant-derived proteins in foods and beverages for environmental, health, and ethical reasons. However, the inherent physicochemical properties and functional performance of many plant proteins limit their widespread application. Here, we prepared pea protein isolate (PPI) dispersions using a combined pH-shift/heat treatment method, and then, prepared PPI-epigallocatechin-3-gallate (EGCG) complexes under neutral conditions. Spectroscopy, calorimetry, molecular docking, and light scattering analysis demonstrated that the molecular complexes formed spontaneously. This was primarily ascribed to hydrogen bonds and van der Waals forces. The complexation of EGCG caused changes in the secondary structure of PPI, including the reduction in the α-helix and increase in the β-sheet and disordered regions. These changes slightly decreased the thermal stability of the protein. With the accretion of EGCG, the hydrophilicity of the complexes increased significantly, which improved the functional attributes of the protein. Optimization of the PPI-to-EGCG ratio led to the complexes having better foaming and emulsifying properties than the protein alone. This study could broaden the utilization of pea proteins as functional ingredients in foods. Moreover, protein–polyphenol complexes can be used as multifunctional ingredients, such as antioxidants or nutraceutical emulsifiers.