In order to expand the applications of plant protein in food formulations, enhancement of its functionalities is meaningful. Herein, the effects of ultrasonic (20 KHz, 400 W, 20 min)-assisted pH shift (pH 10 and 12) treatment on the structure, interfacial behaviors, as well as the emulsifying and foaming properties of perilla protein isolate (PPI) were investigated. Results showed that the solubility of PPI treated by ultrasonic-assisted pH shift (named UPPI-10/12) exceeded 90 %, which was at least 2 and 1.4 times that of untreated PPI and ultrasound-based PPI. Meanwhile, UPPI-10/12 possessed higher foamability (increasing by at least 1.2 times) and good emulsifying stability. Ultrasonic-assisted pH shift treatment decomposed large PPI aggregates into tiny particles, evident from the dynamic light scattering (DLS) and atomic force microscopy results. Besides, this approach induced a decrease in α-helix of PPI and an increase in β-sheet, which might result in the exposure of the hydrophobic group on the structural surface of PPI, thus leading to the increase of surface hydrophobicity. The smaller size and higher hydrophobicity endowed UPPI-10/12 faster adsorption rate, tighter interfacial structure, and higher elastic modulus at the air- and oil-water interfaces, evident from the cryo-SEM and interfacial dilatational rheological results. Thus, the emulsifying and foaming properties could evidently enhance. This study demonstrated that ultrasonic-assisted pH shift technique was a simple approach to effectively improve the functional performance of PPI.
Keywords: Functionality; Interfacial properties; Plant protein; Structure; Ultrasound; pH shift.
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