Non-covalent interaction of rice protein and polyphenols: The effects on their emulsions
Nanchang University · Nanchang Normal University · +2 more institutions
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…
Citation impact
- FWCI
- 47.43
- Percentile
- 100%
- References
- 87
Authors
8- WSWeitong Shu
Nanchang University, Nanchang Normal University, State Key Laboratory of Food Science and Technology
- WSWenyi Shi
Nanchang University, Nanchang Normal University, State Key Laboratory of Food Science and Technology
- HXHexiang Xie
University of Massachusetts Amherst
- SWSongyu Wang
Nanchang University, Nanchang Normal University, State Key Laboratory of Food Science and Technology
- QZQin Zhang
Nanchang University, Nanchang Normal University, State Key Laboratory of Food Science and Technology
Topics & keywords
- Polyphenol
- Rice protein
- Chemistry
- Covalent bond
- Emulsion
- Food science
- Biochemistry
- Organic chemistry
- Zero hunger