The complexation of rice glutelin fibrils (RGFs) with cyanidin-3-O-glucoside (C3G) at acidic condition was investigated. The RGFs at pH 3.5 had a greatest protective effect on the thermal stability of C3G. The binding of C3G for RGFs was exothermic and driven by hydrophobic and electrostatic interactions. The RGFs exhibited a stronger binding interaction with C3G than rice glutelin (RG), resulting from the exposure of hydrophobic groups and positive charges on the fibrils surface, and thus RGFs exhibited better protective effect on C3G. The interaction with C3G resulted in the rearrangement of polypeptide chain, thereby reducing the β-sheet content. The larger aggregates were observed in RG/RGFs-C3G complexes due to protein-polyphenols aggregation. It was noteworthy that the pre-formed RGFs were restructured into entangled aggregates due to the interaction. This study proposed a novel protein fibril to protect anthocyanins, expanding the application of anthocyanins as stable and functional ingredients in acidic food systems.
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