Background: Ovalbumin (OVA), a protein with excellent nutritional and processing properties, is the major allergen of hen egg white. High-intensity ultrasound treatment increases the immunoglobulin (Ig)G and IgE binding abilities by unfolding the conformational structure of OVA. This may allow a modification of the IgG and IgE binding of OVA by combining high-intensity ultrasound with other methods, such as glycation, thus representing a promising method for the improvement of protein properties.
Results: Glycation with mannose (M) after ultrasound pretreatment at 0-600 W significantly reduced the IgG and IgE binding abilities and dramatically enhanced the antioxidant activity of OVA-M conjugates, with the lowest values of IgG and IgE binding and highest values of antioxidant capacity observed at 600 W. Polyacrylamide gel electrophoresis showed that the molecular weight of OVA-M conjugates with ultrasound pretreatment increased more than non-pretreatment sample, implying that ultrasound pretreatment promoted glycation. The α-helix content and ultraviolet absorption of OVA were observably increased, whereas β-sheet content, intrinsic fluorescence and surface hydrophobicity were notably decreased, indicating that the tertiary and secondary structures of OVA were markedly changed.
Conclusion: High-intensity ultrasound pretreatment can be conducive to reducing the binding abilities of IgG and IgE and enhancing the antioxidant activity of OVA-M conjugates. Therefore, glycation combined with high-intensity ultrasound pretreatment might be a promising method for producing hypo-allergenic and high-antioxidant OVA products. © 2018 Society of Chemical Industry.
Keywords: IgE binding; IgG binding; antioxidant activity; glycation; ovalbumin; ultrasound.
© 2018 Society of Chemical Industry.