The application of plant proteins in food systems is largely hindered by their poor foaming or emulsifying properties and low digestibility compared with animal proteins, especially due to the aggregate state with tightly folded structure, slowly adsorbing at the interfaces, generating films with lower mechanical properties, and exposing less cutting sites. Physical fields and pH shifting have certain synergistic effects to efficiently tune the structure and redesign the interfacial layer of plant proteins, further enhancing their foaming or emulsifying properties. The improvement mechanisms mainly include: i) Aggregated plant proteins are depolymerized to form small protein particles and flexible structure is more easily exposed by combination treatment; ii) Particles with appropriate surface properties are quickly adsorbed to the interfacial layer, and then unfolded and rearranged to generate a tightly packed stiff interfacial layer to enhance bubble and emulsion stability; and iii) The unfolding and rearrangement of protein structure at the interface may result in the exposure of more cutting sites of digestive enzymes. This review summarizes the latest research progress on the structural changes, interfacial behaviors, and digestion properties of plant proteins under combined treatment, and elucidates the future development of these modification technologies for plant proteins in the food industry.
Keywords: Digestibility; emulsion/foam; oil/air-water interface; pH shifting; physical field modification; plant protein.