Advances in dietary proteins binding with co-existed anthocyanins in foods: Driving forces, structure-affinity relationship, and functional and nutritional properties

Abstract

Anthocyanins, which are the labile flavonoid pigments widely distributed in many fruits, vegetables, cereal grains, and flowers, are receiving intensive interest for their potential health benefits. Proteins are important food components from abundant sources and present high binding affinity for small dietary compounds, e.g., anthocyanins. Protein-anthocyanin interactions might occur during food processing, ingestion, digestion, and bioutilization, leading to significant changes in the structure and properties of proteins and anthocyanins. Current knowledge of protein-anthocyanin interactions and their contributions to functions and bioactivities of anthocyanin-containing foods were reviewed. Binding characterization of dietary protein-anthocyanins complexes is outlined. Advances in understanding the structure-affinity relationship of dietary protein-anthocyanin interaction are critically discussed. The associated properties of protein-anthocyanin complexes are considered in an evaluation of functional and nutritional values.

Keywords:

• Anthocyanin
• dietary protein
• non-covalent interaction
• structure-affinity relationship

Author contributions

Zhen Ma and Anqi Guo: Formal analysis; Writing-original draft. Pu Jing: Funding acquisition; Investigation; Supervision; Writing-review & editing.

Competing interests

The authors declare that they have no competing interests.

Additional information

Funding

This work was supported by the National Natural Science Foundation of China (Grant No. 21978169) and Key-Area Research and Development Program of Guangdong Province (Grant No. 2018B020239001).