The effect of rice protein-polyphenols covalent and non-covalent interactions on the structure, functionality and in vitro digestion properties of rice protein.
Food Chem
; 450: 139241, 2024 Aug 30.
Article
de En
| MEDLINE
| ID: mdl-38636382
ABSTRACT
The characteristics of the crosslinking between rice protein (RP) and ferulic acid (FA), gallic acid (GA), or tannin acid (TA) by covalent binding of Laccase and non-covalent binding were evaluated. The RP-polyphenol complexes greatly improved the functionality of RP. The covalent effect with higher polyphenol binding equivalence showed higher emulsion activity than the non-covalent effect. The solubility, and antioxidant activity of covalent binding were higher than that of non-covalent binding in the RP-FA group, but there was a contrasting behavior in the RP-GA group. The RP-FA was most soluble in conjugates, while the RP-GA had the highest solubility in mixtures. It was found that the covalent complexes were more stable in the intestinal tract. The content of polyphenols in the RP-TA group was rapidly increased at the later intestinal digestion, which indicated the high polyphenol-protective effect in this group. Meanwhile, the RP-TA group showed high reducing power but low digestibility.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Protéines végétales
/
Oryza
/
Digestion
/
Polyphénols
Limites:
Humans
Langue:
En
Journal:
Food Chem
Année:
2024
Type de document:
Article
Pays d'affiliation:
Chine