The RPs and SPIs were fabricated into nanoscale composites through synergistic structural interactions.

Recently, interests in binary protein systems have been developed considerably ascribed to the sustainability, environment‐friendly, rich in nutrition, low cost, and tunable mechanical properties of these systems. However, the molecular coalition is challenged by the complex mechanisms of interaction, aggregation, gelation, and emulsifying of the mixed system in which another protein is introduced. To overcome these fundamental difficulties and better modulate the structural and functional properties of binary systems, efforts have been steered to gain basic information regarding the underlying dynamics, theories, and physicochemical characteristics of mixed systems. Therefore, the present review provides an overview of the current studies on the behaviors of proteins in such systems and highlights shortcomings and future challenges when applied in scientific fields.

A self-sorted gel network was formed by heating a binary system of cod and soy proteins.

Protein structures combining designable nutritional and functional properties are attracting great attention in the food industry. In this study, novel protein composites with shared internal structures were fabricated by co-dissolving rice proteins (RPs) and pea proteins (PPs) at pH 12 prior to a one-step neutralization. Structural and morphological characterization revealed that both unfolded protein molecules reacted at pH 12 via their secondary structures, driven by hydrophobic forces. The co-assembled structures therefore obtained considerable resistance against acid-induced refolding, affording the formation of nanoscale (∼100 nm), water-dispersible composites at pH 7. Eventually, the drawbacks of either proteins, such as the insolubility of RPs or slow digestion of PPs, were overcome due to structural alterations. Moreover, the strategy raised the level of Lys which was limiting in RPs in the same way as the level of those that were limiting in PPs such as Met and Cys-s. Based on the above results, the study would enrich the techniques of processing protein ingredients toward tailored structures and on-demand nutritional properties.