Effect of high intensity ultrasonic treatment on structural, rheological, and gelling properties of potato protein isolate and its co‐gelation properties with egg white protein

Abstract The study aimed to investigate the effect of high intensity ultrasonic (HIU) treatment at different times (0, 10, 20, and 30 min) on the structure and gel properties of water‐soluble potato protein isolate (WPPI) and to further investigate the improvement of gel properties of ultrasonicated WPPI (UWPPI) by the addition of egg white protein (EWP). HIU reduced the particle size of WPPI, whose structure became loose and disordered, which improved gelling properties of UWPPI. Fourier transform infrared results indicated that α‐helix content decreased, whereas the proportion of irregular curl increased with the increase in ultrasonication time (0–20 min), indicating that the initially ordered structure of UWPPI became disordered. After HIU treatment, the free sulfhydryl groups of UWPPI and surface hydrophobicity decreased and fluorescence intensity increased. These results demonstrated that the HIU loosened the structure of UWPPI, exposing more chromogenic groups while embedding more hydrophilic groups. After thermal induction, UWPPI gel hardness increased and exhibited excellent water holding capacity. After the addition of EWP, rheological properties stabilized, and the hardness of UWPPI‐EWP gels increased significantly, forming internally structured protein gels with a tightly ordered structure and increased brightness. Thus, HIU changed the structure and gelling properties of WPPI, and the addition of EWP further enhanced the performance of hybrid protein gels. Practical Application High intensity ultrasonic changed the structure of water‐soluble potato protein isolate (WPPI) and improved the properties of WPPI gels. The addition of egg white protein significantly improved the quality of mixed protein gels which showed great potential industrial value.