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

Jiang, Jiang, Chen, Jie, Xiong, Youling L.·2009·Journal of Agricultural and Food Chemistry

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.

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Metadata

Authors
Jiang, J., Chen, J., & Xiong, Y. L.
Venue
Journal of Agricultural and Food Chemistry
Published
2009-07-14
Volume
57
Issue
16
Pages
7576-7583
ISSN
  • 0021-8561 (ISSN-L)
  • 1520-5118
OpenAlex
W2052924389
Cited by
587
References
0
FWCI
9.64
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structural and Emulsifying Properties of Soy Protein Isolate Subjected to Acid and Alkaline pH-Shifting Processes. https://app.cochat.ai/papers/10.1021/jf901585n
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Jiang, J., Chen, J., & Xiong, Y. L. (2009). Structural and Emulsifying Properties of Soy Protein Isolate Subjected to Acid and Alkaline pH-Shifting Processes. Journal of Agricultural and Food Chemistry. https://doi.org/10.1021/jf901585n

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