Different protein-anthocyanin complexes engineered by ultrasound and alkali treatment: Structural characterization and color stability

Through alkali treatment (AT) and ultrasound (UT)-assisted processing producing covalent protein-anthocyanin complexes, we investigated the impact of treatment methods and protein types on conjugation efficiency, protein structure, and color stability. Our findings revealed the effective grafting of anthocyanins (ACNs) onto proteins, with myofibrillar protein (MP) exhibiting the highest conjugation efficiency of 88.33% after UT (p <.05). UT accelerated the structure unfolding of distinct protein samples, leading to the exposure of sulfhydryl, and hydrophobic groups in proteins, and enhanced the oxidation stability of ACNs. Notably, the modified ACNs maintained a favorable pH-color relationship, while U-MP showed a significantly higher absorbance (0.4998) than the other groups (p <.05) at pH 9.0, demonstrating an outstanding color improvement. UT-assisted processing also accelerated the NH3 reaction. Thus, the combination of UT and MP holds the potential for pH-color-responsive intelligent packaging and increases the efficiency of UT processing.