Effect of Ultrasound Time on Structural and Gelling Properties of Pea, Lupin, and Rice Proteins

Plant proteins are garnering interest due to the growing demand for plant-based products, but their functionality in gel-based foods remains limited. Ultrasound (US) technology may improve the technological properties of proteins. Thus, the effect of US treatment time (0-15 min) on the structure and gelling properties of pea, lupin, and rice proteins was evaluated. The results showed that the whiteness (~60%) of all freeze-dried proteins remained unchanged (<i>p ></i> 0.05), regardless of the US time. However, FT-IR analysis revealed progressive reductions in α-helix and β-sheet for pea and lupin proteins (~50%) with US time, indicating partial unfolding. In addition, microstructure analysis showed an ~80% reduction in aggregate size for these proteins, while rice protein exhibited minimal changes. Conversely, weak gels were formed with pea and lupin proteins treated after 5 and 10 min of US, respectively, whereas rice protein did not form gels. Furthermore, US treatment time significantly increased (<i>p <</i> 0.05) the mechanical moduli, resulting in more structured gels after longer treatment times (tan δ ~0.3 at 15 min of US). These findings suggest that US treatment enhances the gelling properties of pea and lupin proteins, making them more suitable for plant-based food applications such as yogurt or desserts.