High-temperature glycosylation modifies the molecular structure of ovalbumin to improve the freeze-thaw stability of its high internal phase emulsion

In this study, ovalbumins (OVAs) were glycosylated with fructo-oligosaccharide (FO) at different temperatures (80 °C, 100 °C, 120 °C, and 140 °C) and durations (1 h and 2 h) via wet-heating. The glycosylated OVAs (GOVAs) were characterized by the degree of glycosylation (DG), particle size, zeta potentials, and structural changes. GOVAs-stabilized high-internal-phase emulsions (HIPEs) were then prepared to compare their macro- and microstructure and freeze–thaw stability. The results showed that the DG of GOVAs increased with the increase in glycosylation temperature and the protein structure unfolded with it. Glycosylation decreased the particle size, zeta potential, and α-helical structures and increased the β-sheets and surface hydrophobicity (H 0 ) of GOVAs compared with unmodified OVAs. Moreover, GOVAs-stabilized HIPEs exhibited smaller particle sizes, zeta potentials, agglomeration indexes, oil loss rates, and freezing points and higher viscoelasticity, centrifugal stabilities, flocculation indexes, and freeze–thaw stabilities. Notably, HIPEs prepared by GOVAs (glycosylated higher than 120 °C) showed the least changes in macro- and microscopic appearances after freeze-thawing. These findings will provide a novel method for improving and broadening the functionalities of OVAs and potentially develop HIPEs with enhanced freeze–thaw stabilities.