Ferulic acid-ovalbumin protein nanoparticles: Structure and foaming behavior

Abstract

Egg white was known for its excellent foaming properties, and some reports had studied the effect of polyphenol such as green tea on the foaming properties. However, ovalbumin, as the most abundant component of egg white protein, few literatures have reported the effects of polyphenols on its structure and foam property. In this study, ferulic acid (FA) was selected to explore the influence of polyphenol on the structure and foaming properties of ovalbumin (OVA). Results showed that hydrophobic interaction and hydrogen chemical bonds were the main driving force. FA could induce a significant decrease of free-SH content (12.76–3.72 μmol/g), a slight decline of surface hydrophobicity (716.39–577.65). Meanwhile, combined with the results of fluorescence spectroscopy and circular dichroism spectroscopy, we conclude that FA changed the structures and molecular flexibility of OVA. The increase of particle size and absolute zeta-potential showed there was a little aggregation between OVA molecules, proved FA could act as a cross-linker between OVA proteins. This behavior makes the adjacent films more firm and stable, therefore improved the foaming properties. This study suggested that FA could be a potential foaming agent to modify the foaming properties of OVA in the foam-related food industry.