Utilization of sonication-glycation to improve the functional properties of ovalbumin: A high-resolution mass spectrometry study

Abstract

Ovalbumin (OVA) is a globular protein found in hen's eggs that has excellent nutritional and functional properties but is a major allergen. Previous studies have shown that ultrasound pretreatment combined with glycation (sonication-glycation) of OVA markedly reduced its IgG and IgE binding capacities and enhanced its antioxidant activity. In this study, the effects of sonication-glycation on a number of important functional attributes of OVA were studied: foaming, emulsifying, and digestibility. These processes significantly enhanced the foaming and emulsifying properties of OVA by increasing the exposure of hydrophobic residues at the protein surfaces. Moreover, reversed-phase chromatography indicated that sonication-glycation only caused a small decrease in OVA digestibility under simulated gastric and small intestine conditions, and that the level of IgG and IgE binding of OVA was exceedingly low after digestion. Furthermore, sonication promoted the glycation of OVA by increasing the number of exposed glycation sites, as determined by high-resolution mass spectrometry. These results imply that sonication-glycation is a promising method for improving the functional performance of food proteins, while also reducing their immunogenicity.