Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 57, Issue 16, Pages 7576-7583Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf901585n
Keywords
Soy protein isolate; pH shifting; emulsifying properties; molten globule
Funding
- Ministry of Science and Technology, China [2006AA10Z325, 2007AA10Z323]
- Ministry of Education, China [NCET-07-0377, IRT0627]
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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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