Ultrasound-induced structural modification and thermal properties of oat protein

The objective of this study was to characterize the solubility, structural, thermal, and aggregation properties oat protein under high-intensity ultrasound (HIU) treatment. Suspensions isolate (OPI) at pH 2.0–8.0 were subjected HIU for 5 min 70% amplitude; particle size, surface attributes, UV–Vis absorption, intrinsic fluorescence, polypeptide profiles, calorimetric properties, thermal determined. treatment significantly reduced size (up 37%) increased charge OPI leading solubility increases 48%, P < 0.05) 2.0–3.0 5.5–8.0. However, did not alter profile nor disrupt disulfide linkages between α β subunits. Reduced enthalpy denaturation with no shift in transition temperature observed samples unless bonds pre-cleaved. While control displayed variable changes upon heating from 20 95 °C, sample maintained a relatively uniform smaller size. findings indicate that disruption weakening intermolecular forces by improved physicochemical OPI, which are value processing protein-based beverages other food products.