Structural and Emulsifying Properties of Soy Protein Isolate Subjected to Acid and Alkaline pH-Shifting Processes

TLDR

The soy protein isolate was exposed to sequential acidic (pH 1.5–3.5) and alkaline (pH 10.0–12.0) pH shifts for up to 4 h, then refolded at pH 7.0, and its structural changes and emulsifying properties were evaluated. The pH‑shifting treatments increased surface hydrophobicity, tryptophan fluorescence, disulfide‑mediated aggregation, and tyrosine exposure, producing a molten‑globule‑like conformation that preserved secondary structure but altered tertiary structure, thereby markedly enhancing the emulsifying activity and stability of the soy protein isolate.

Abstract

Structural unfolding of soy protein isolate (SPI) as induced by holding (0, 0.5, 1, 2, and 4 h) in acidic (pH 1.5−3.5) and alkaline (pH 10.0−12.0) pH solutions, followed by refolding (1 h) at pH 7.0, was analyzed. Changes in emulsifying properties of treated SPI were then examined. The pH-shifting treatments resulted in a substantial increase in protein surface hydrophobicity, intrinsic tryptophan fluorescence intensity, and disulfide-mediated aggregation, along with the exposure of tyrosine. After the pH-shifting processes, soy protein adopted a molten globule-like conformation that largely maintained the original secondary structure and overall compactness but lost some tertiary structure. These structural modifications, consequently, led to markedly improved emulsifying activity of SPI as well as the emulsion stability.