Effect of CaCl 2 on 2 heat-induced whey protein concentrate fibrillation pathways: Spontaneous and nuclear induction
Amyloid fibrils have many excellent functional properties that facilitate their applications in the food industry. There are 2 pathways for whey protein concentrate (WPC) to form amyloid fibril aggregates: spontaneous pathway and nuclear induction pathway. Low ionic strength is a necessary condition...
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Veröffentlicht in: | Journal of dairy science 2022-05 |
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Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Amyloid fibrils have many excellent functional properties that facilitate their applications in the food industry. There are 2 pathways for whey protein concentrate (WPC) to form amyloid fibril aggregates: spontaneous pathway and nuclear induction pathway. Low ionic strength is a necessary condition for the spontaneous pathway to proceed successfully. In this paper, the effect of salt ions on 2 WPC fibrillation pathways was investigated by adding CaCl
. The results demonstrated WPC fibrils were unable to form normally through spontaneous pathway as adding CaCl
; but still could form through nuclear induction pathway with 20 to 30 mM CaCl
, the nuclei accelerated the fibrillation process led to the resistance to the disordered aggregation brought by CaCl
. Moreover, divalent cations (Ca
, Mg
) had much stronger effects than monovalent cations (Na
) on fibril formation, and the results of X-ray photoelectron spectrum together with Fourier-transform infrared spectroscopy suggested that Ca
had a greater effect on the fibril formation than Cl
. |
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ISSN: | 1525-3198 |