pH-Induced structural transitions in whey protein isolate and ultrasonically solubilized Persian gum mixture.

The present work evidently reports that ultrasonic depolymerization strongly enhanced complex coacervation between Persian gum (PG) and whey protein isolate (WPI). PG was sonicated at 60 °C, operating frequency of 20 kHz and nominal power output of 800 W for various times followed by mixing with WPI. Acid-induced interaction between the two biopolymers was studied by turbidity, light scattering, zeta potential and viscosity measurements over a wide pH range. Sonication of intact PG (IPG) for 10 min considerably reduced the molecular weight from 4.12 × 10 to 0.76 × 10 g/mol. Besides, ultrasonic fragmentation of water insoluble fraction of PG drove protein containing chains into the soluble phase. Sonicated PG (SPG) was shown to be more flexible with higher number of carboxyl groups available for electrostatic interaction with WPI, such that the complete neutralization did not occur even at protein to polysaccharide ratio of 50: 1. Additionally, scattered light intensity and viscosity measurements revealed two maxima in the pH ranges of 4.4-4.85 and 3.27-4.0, being highly intense for the gum sonicated for 10 min and longer. Considering the pH-behavior of WPI components, the former peak was related to interpolymer complex formation between β-lactoglobulin and long chain fraction of SPG, while the latter was attributed to intrapolymer association of α-lactalbumin with the short chain oligosaccharides arising from ultrasonic degradation of PG.