Effects of three polyphenols with different numbers of phenolic hydroxyls on the structural and interfacial properties and lipid-protein co-oxidation of oil body emulsions.

Oil bodies (OBs) are organelles for storing lipids, and they are composed of lipid cores and monolayer phospholipid protein membranes. During storage, membrane proteins anchored in the lipid core are often damaged by lipid oxidation products, leading to oxidative damage and a decreased quality of emulsified foods. Here, three natural antioxidants (gallic acid (GA), epigallocatechin gallate (EGCG), and tannic acid (TA)) were added to OB emulsions to study the effects of polyphenols on protein interfacial properties during oxidation and the lipid-protein co-oxidation behavior. Compared to GA, EGCG and TA with higher molecular weights and hydroxyl substitution showed better antioxidant activity, metal chelating activity, iron reduction ability, and affinity for OB. The polyphenols significantly reduced the contents of free amino and sulfhydryl groups in OB. Infrared spectroscopy analysis indicate that hydrogen bonding and hydrophobic interactions may exist between the polyphenols and OB. During storage, polyphenols inhibited >23% of the primary and secondary lipid oxidation products in the emulsions, whereas the formation of carbonyl groups and disappearance of sulfhydryl groups were only inhibited by 10.7% and 7.4%, respectively, indicating that polyphenols preferentially inhibited lipid oxidation over protein oxidation. Electrophoresis results showed that moderate oxidation (3 days of storage) disrupted the disulfide bonds of proteins. Note that moderate oxidation enhanced the interfacial properties of OB proteins, whereas excessive oxidation led to protein aggregation. This study offers new perspectives on using polyphenols to regulate the lipid-protein co-oxidation in OB, as well as the different properties of OB proteins after oxidation. [Display omitted] • Three polyphenols increase the stability of oil body (OB) emulsions. • Tannic acid with a high hydroxyl content has the best affinity for OB. • Hydrogen bonding and hydrophobic interactions occur between the polyphenols and OB. • Polyphenols are more likely to inhibit lipid oxidation than protein oxidation. • Moderate oxidation enhances the interfacial properties of proteins. [ABSTRACT FROM AUTHOR]