Evaluation of crossing-linking sites of egg white protein–polyphenol conjugates: Fabricated using a conventional and ultrasound-assisted free radical technique

Abstract

There has been strong interest in developing effective strategies to inhibit lipid oxidation in emulsified food products such as ω-3 fatty acids, carotenoids, or carotenoids. Dual-functional protein emulsifiers with antioxidant and emulsifying properties are in the spotlight. Our aim was to investigate the influence of caffeic acid (CF), chlorogenic acid (CA) with a C3-C6 structure, epigallocatechin gallate (EGCG), catechin (CT), and quercetin (QE) with a C6-C3-C6 structure on the cross-linking sites and structure of egg white protein (EWP)–polyphenol conjugates fabricated by the free radical method under conventional water bath (WB) and ultrasound assisted (US) conditions. Results of structural analysis and liquid chromatography–tandem mass spectrometry indicated that the structure of EWP–polyphenol conjugates and the cross-linking sites of the two are influenced by the polyphenol structure and the free radical system. Our study provides important information about the mechanism of research into proteins and polyphenols using the free radical method.