Formation, structural characteristics, foaming and emulsifying properties of rice glutelin fibrils

The rice glutelin fibrils (RGFs) were formed under heating at acidic condition, and the optimal condition was achieved at pH 2, 150 mM (ionic strength), 4% (protein concentration), 90 °C and 300 rpm (stirring speed) through the thioflavin T intensity. The atomic force microscopy images showed that the average contour length of RGFs increased from < 100 to 365 nm under the optimal fibrillation. The average particle size of rice glutelin (RG) decreased from 650 to 221 nm after initial heating time. Combining the degraded subunits, it suggested that RG was hydrolyzed to peptides, then these released peptides assembled into the ordered fibrils via intermolecular interactions, accompanying by the structural rearrangement. Additionally, the foaming and emulsifying properties were improved during fibrillation, which could be related to the interfacial properties and structure of RGFs. This work will deepen the understanding of the formation of RGFs and explore their potential application.