A comprehensive study on structures and characterizations of 7S protein treated by high intensity ultrasound at different pH and ionic strengths

High intensity ultrasound (HIU) effects on soy 7S proteins in various pH (pH = 3.0 and 7.0) and ionic strengths (I = 0.1, 0.3 and 0.5) were investigated. When dissolved in pH = 7.0, the 7S proteins formed aggregates at the low ionic strength (I = 0.1), while large aggregates were dissociated as the ionic strengths increased (I = 0.3 or 0.5) after HIU treatments. Moreover, the 7S proteins were unfolded at I = 0.3 and I = 0.5 through HIU. When...