High intensity ultrasound modified ovalbumin: Structure, interface and gelation properties.

Influence of high intensity ultrasound (HIUS) on the structure and properties of ovalbumin (OVA) were investigated. It was found that the subunits and secondary structure of OVA did not change significantly with HIUS treatment from the electrophoretic patterns and circular dichroism (CD) spectrum. The amount of free sulfhydryl groups increased and intrinsic fluorescence spectra analysis indicated changes in the tertiary structure and partial unfold of OVA after sonication increased. Compared with the untreated OVA, HIUS treatment increased the emulsifying activity and foaming ability, and decreased interface tension (oil-water and air-water interface), which due to the increased surface hydrophobicity and decreased the surface net charge in OVA, while the emulsifying and foaming stability had no remarkable differences. The increased particle size may be attributed to formation of protein aggregates. Moreover, the gelation temperatures of HIUS-treated samples were higher than the untreated OVA according to the temperature sweep model rheology, and this effect was consistent with the increased in surface hydrophobicity for ultrasound treated OVA. These changes in functional properties of OVA would promote its application in food industry.