Enhance quinoa protein foaming properties through amyloid-like fibrillation and 2S albumin blending

Native quinoa protein has weak processability. Fibrillation can vary the structure and foaming properties of proteins. Quinoa 2S albumin also has the potential to be an interface active substance. In this study, quinoa protein amyloid-like fibrils (QPF) and 2S albumin were blended to stabilize foams for the first time, and their interfacial behavior, foaming properties and the microstructure of foams were analyzed. The absolute value of zeta potential and surface tension of quinoa protein isolates (QPI) decreased after fibrillation, which improved the foam capacity and stability significantly. When QPF were further blended with 2S albumin at a ratio of 1:1, foam capacity and foam stability reached the highest values of 183.33% and 86.38%, respectively. The adsorption of QPF at the air-water interface along with 2S albumin’s filling in the interfacial voids may strengthen the protein interfacial network and their foaming properties. Meanwhile, our study revealed that both the viscosity of the liquid phase as well as the interfacial properties of the protein dispersion influenced the foam capacity and foam stability of QPF/2S albumin. Furthermore, foams generated from QPF/2S albumin were applied to prepare coffee latte art and chiffon cakes. The cakes using foams generated from QPF/2S albumin to fully replace egg white exhibited a fluffy, porous, and stable structure. To conclude, the fibrillated quinoa protein and 2S albumin complex showed the potential to be an innovative plant-based ingredient to generate foams and applied in food processing industry, which will contribute to the food sustainability.