Non-covalent interaction of rice protein and polyphenols: The effects on their emulsions
Year: 2025
Type: article
Abstract: In this study, we investigated the non-covalent interaction mechanism between rice protein (RP) and three polyphenols with different concentrations (ferulic acid FA, gallic acid GA, and tannic acid TA) and their effects on the structure and emulsion stability of the proteins. Hydrophobic forces dominated the binding of RP to the polyphenols, and the reaction was heat-absorbing. The three polyphenols are bound to RP in the form of static quenching to form a non-covalent complex, and during the binding process, the RP provides one binding site. RP-polyphenol complexes, particularly RP-GA, enhanced ABTS scavenging and FRAP reduction. Polyphenols improved RP emulsion oxidative stability, inhibiting lipid oxidation and enhancing emulsion rheology and interfacial structure. RP-GA was most effective, maintaining low POV. These findings support the potential applications of RP-polyphenol noncovalent complexes in food processing.
Source: Food Chemistry
Authors: Weitong Shu, Wenyi Shi, Hexiang Xie, Songyu Wang, Qin Zhang, Kefan Ouyang, Fangjie Xiao, Qiang Zhao
Institutions: Nanchang University, University of Massachusetts Amherst
Language: English
Topic: Proteins in Food Systems
Subfield: Food Science
Domain: Life Sciences
SDG: Zero hunger
Open Access status: hybrid
Estimated APC paid: $4,930
Awards: G6356961568, G6547032909
OpenAlex ID: W4408160265