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• W2052924389 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." @default.
• W2052924389 created "2016-06-24" @default.
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• W2052924389 date "2009-07-14" @default.
• W2052924389 modified "2023-10-14" @default.
• W2052924389 title "Structural and Emulsifying Properties of Soy Protein Isolate Subjected to Acid and Alkaline pH-Shifting Processes" @default.
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• W2052924389 doi "https://doi.org/10.1021/jf901585n" @default.
• W2052924389 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19601630" @default.
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