Nanofibril system constructed by protein self-assembly is widely used in the food industry because of purposive functional properties. Soy protein isolate nanofibrils (SPINs) were reported to form via heating at pH 2.0. In this research, the soy protein isolate (SPI) hydrolysate prepared by trypsin was used as a raw material for the formation of nanofibrils called soy protein isolate hydrolysate nanofibrils (SPIHNs). Microscopic images demonstrated the formation of two nanofibrils. Based on circular dichroism spectroscopy and Thioflavin T (ThT) fluorescence spectral, we concluded that β-sheet played an important role in SPIN and SPIHN’s structural composition. At the same time, the α-helix in SPI had not been destroyed, thereby favoring the formation of SPIHN. The surface hydrophobicity of SPIHN continued to increase during the heating process and reached the highest value when heating 8 h. SDS-PAGE analysis showed that peptides produced by enzyme-modified SPI affected the formation of SPIHN. These results proposed that enzymatic hydrolysis prior to acidic during fibrillation process affected the fibrillation of SPI, and the peptides formed by enzymatic hydrolysis were more efficient for the self-assembly process. This study will provide a theoretical basis for the future research of SPI nanofibril functionality.

Due to the high aspect ratio, appealing mechanical characteristics, and various adjustable functional groups on the surface proteins, food-grade protein nanofibrils have attracted great research interest in the field of food science. Fibrillation, known as a process of peptide self-assembly, is recognized as a common attribute for food-grade proteins. Converting food-grade proteins into nanofibrils is a promising strategy to broaden their functionality and applications, such as improvement of the properties of gelling and emulsifying, especially for constructing various delivery systems for bioactive compounds. Protein source and processing conditions have a great impact on the size, structure, and morphology of nanofibrils, resulting in extreme differences in functionality. With this feature, it is possible to engineer nanofibrils into four different delivery systems, including gels, microcapsules, emulsions, and complexes. Construction of nanofibril-based gels via multiple cross-linking methods can endow gels with special network structures to efficiently capture bioactive compounds and extra mechanical behavior. The adsorption behavior of nanofibrils at the interface is highly complex due to the influence of several intrinsic factors, which makes it challenging to form stabilized nanofibril-based emulsion systems. Based on electrostatic interactions, microcapsules and complexes prepared using nanofibrils and polysaccharides have combined functional properties, resulting in adjustable release behavior and higher encapsulation efficiency.The bioactive compounds delivery system based on nanofibrils is a potential solution to enhance their absorption in the gastrointestinal tract, improve their bioavailability, and deliver them to target organs. Although food-grade protein nanofibrils show unknown toxicity to humans, further research can contribute to broadening the application of nanofibrils in delivery systems.