Structure and functionality of whey protein, pea protein, and mixed whey and pea proteins treated by pH shift or high-intensity ultrasound

Three modifications (pH-shift, ultrasound, combined pH-shift/ultrasound) induced alterations in pure whey protein (WPI), pea protein (PPI), and mixed whey/pea protein (WPI/PPI) were investigated. The processing effect was related to the protein type and technique utilized. Solubility of WPI remained unchanged by various treatments. Particle size was enlarged by pH-shift while reduced by ultrasound and combined approach. All methods exposed more surface hydrophobic groups on WPI, while pH-shift and joint processing was detrimental to its emulsifying activity. PPI and mixture exhibited similar responses toward the modifications. Solubility of PPI and the blend enhanced in the sequence of pH-shift/ultrasound > ultrasound > pH-shift. Individual approach expanded while co-handling diminished the particle diameter. Treatments also caused more disclosure of hydrophobic regions in PPI and WPI/PPI and emulsifying activity was ameliorated in the order of pH-shift/ultrasound > ultrasound > pH-shift.