Xiuling Zhang

Fibrillization is extensively recognized as a promising strategy for endowing food‐derived proteins with desirable functional properties. However, there remains a critical knowledge gap regarding the systematic investigation of how the functional and biological properties of food‐derived protein fibrils can be further enhanced via the synergistic or complementary effects of different modification technologies. This review summarizes recent research on the modulation of the fibrillization process of food‐derived proteins via various strategies (physical, chemical, biological techniques, and fibrillization parameter optimization). In addition, their functional properties, potential food applications, current challenges, and future directions are discussed. The key finding is that the integration of other modification technologies (e.g., ultrasonication, glycosylation, enzymatic hydrolysis) promotes the enhancement of functional properties (e.g., emulsifying, foaming, and gelling properties) and biological properties (antioxidant, antibacterial, and low allergenicity) of food‐derived protein fibrils. These enhanced properties are closely associated with the structural changes of protein fibrils induced by the combined technologies. Notably, the impacts of different regulatory strategies on the morphology of protein fibrils are mainly reflected in length, flexibility, and branching structure. As research advances, food‐derived protein fibrils have emerged as a promising ingredient for food applications, such as delivery systems, starch digestion inhibitors, food packaging, and biomimetic foods. Future research should focus on a deeper understanding of the structure–function relationships and the safety of food‐derived protein fibrils.

Thus far, the focus of research has been on employing perilla seed protein isolate (PSPI) to stabilize emulsions encapsulating hydrophobic substances, but there is a dearth of studies focusing on PSPI-stabilized double emulsions for encapsulating hydrophilic materials. This experiment investigated the environmental stability (thermal, ionic strength, and freeze–thaw stability) of PSPI-stabilized double emulsions encapsulating anthocyanins. During thermal stability experiments, the emulsion color lightened as the treatment temperature increased, whereas the microstructures of the emulsions exhibited no notable differences among the groups. The anthocyanin retention and antioxidant capacity decreased with increasing thermal treatment temperature. After thermal treatment, no creaming or separation was observed, and anthocyanin retention remained above 65% in all groups. Ionic strength exerted a certain influence on the stability of the emulsions, with droplet size increasing and anthocyanin retention dwindling as ionic strength intensified. At an ionic strength of 100 mmol/L, anthocyanin retention surpassed 70%. No delamination was observed at any of the ionic strengths. With the augmentation of freeze–thaw cycles, the emulsions darkened and yet remained unseparated, droplet size progressively increased, and anthocyanin retention progressively decreased. The findings indicate that the emulsions were environmentally stable and could serve as a reference for the development of related emulsions.