The Formation and Disaggregation of Soy Protein Isolate Fibril: Effects of pH
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To identify the effects of charged states on the formation and disaggregation of soy protein isolate (SPI) fibril, we studied the thermal aggregation behaviors of the constituent peptides of SPI fibril (CPSF) at various pH values (2–10) and investigated the structural changes of SPI fibril with increasing pH (2–11). Results showed that CPSF would assemble into diverse shapes at different pH values, among which the aggregates contained multiple β-sheet structures at pH less than 6, but these β-sheets were stacked to form fibrils only at pH 2. The damages from the increased pH to SPI fibril structure could be roughly divided into two stages, as follows: when pH was less than or equal to 6, the morphology of fibrils changed markedly due to electrostatic neutralization; at pH larger than 6, the fibrils suffered great losses in β-sheet, causing its structure to disintegrate rapidly. This study could provide theoretical reference to improve the pH stability of SPI fibril from the aspects of preparation and structural protection of the fibril.
KeywordsSoy protein isolate fibril pH β-Sheet Morphology Disaggregation Fibrillation
The authors acknowledge the financial support provided by the Natural Science Foundation of China (NSFC, No. 31471582).
Compliance with Ethical Standards
Conflict of Interest
The authors declare that they have no conflict of interest.
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