Mechanism for formation of ovalbumin–fatty acid salt mixed gels

In this study, changes in the secondary structure of ovalbumin (OVA) during sodium caprate-induced gel formation were analyzed by FT-IR to help clarify mechanisms of protein gelation. Due to aggregation, there was an increase in intermolecular β-sheet bands and a decrease in α-helix and intramolecular β-sheet content during sodium caprate-induced gel formation. Furthermore, heat treatment of the gel caused a further enhancement in the content of intermolecular β-sheet bands. These results suggest that, similar to β-lactoglobulin gels, sodium caprate-induced OVA gels and heat-induced OVA gels form by similar mechanisms, although the sodium caprate-induced gel formation is accompanied by less marked changes in protein conformation.