Modifying functional properties of food amyloid-based nanostructures from rice glutelin.

Amyloid-based nanostructures from food sources have been received intensive interests recently in material science, biomedicine and especially delivery system. This is due to the ability of protein-based amyloid architecture that proved to be an attractive system to carry drug and nutrition. However, few research focused on the modification of functional properties of different fractions isolated from amyloid fibrils. Hereby, we separated the retentate (RGFs) and filtrate (FGFs) fractions from rice glutelin fibrils (GFs) using centrifugal filtration and then investigated the structural characteristics and functional properties of these fractions. We proved that protein fibrillization would highly improve both emulsifying and antioxidant abilities of protein dispersion. In addition, further processed RGFs with rich β-sheet structures exhibited a similar functional performance to GFs dispersion. By contrast, FGFs dispersion with less β- sheet content, lower molecular weight, interestingly re-assembled into spherical aggregates with weaker interaction, exhibiting better antioxidant and emulsifying properties.