The effect of a pH-shifting and ultrasound combined process on the functional properties and structure of pea protein isolate (PPI) was investigated. PPI dispersions were adjusted to pH 2, 4, 10, or 12, treated by power ultrasound for 5min, and incubated for 1h before the sample pH was brought back to neutral. After treatment, water solubility, protein aggregate size, solution turbidity, surface hydrophobicity (Ho), free sulfhydryl content (SH), and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the soluble PPI were determined. pH-shifting at pH 12 and ultrasound combined treatment (pH12-US) significantly improved protein properties, while property modification of the samples treated under acidic conditions was less pronounced. The pH12-US treated PPI had a solubility seven times higher than the control, reaching an average particle size of 45.2nm. In addition, the pH12-US treated PPI significantly improved Ho due to disulfide bonds disruption, and produced more protein sub-units than other treatments. The soluble PPI obtained through this process may be a promising emulsifier for the enrichment of fat-soluble nutrients in foods.
Keywords: Particle size; Pea protein; Solubility; Ultrasound; pH-shifting.
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