Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes

Jiang Jiang, Jie Chen, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

425 Scopus citations

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.

Original languageEnglish
Pages (from-to)7576-7583
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume57
Issue number16
DOIs
StatePublished - 2009

Keywords

  • Emulsifying properties
  • Molten globule
  • PH shifting
  • Soy protein isolate

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences

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