Effect of CaCl2 on 2 heat-induced whey protein concentrate fibrillation pathways: Spontaneous and nuclear induction

• Published in: Journal of dairy science Vol. 105; no. 7; pp. 5573 - 5586
• Main Authors: Yang, Xiaotong, Xie, Mingming, Guan, Chen, Yingchen, Guo, Ruichi, Ma, Caihong, Xu, Honghua, Shao, Meili
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 01-07-2022; Elsevier
• Subjects: CaCl2; fibril; nuclear induction pathway; spontaneous pathway; whey protein concentrate; fibril; spontaneous pathway; nuclear induction pathway; CaCl2; whey protein concentrate
• ISSN: 0022-0302; 1525-3198
• DOI: 10.3168/jds.2021-20895

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 CaCl2. The results demonstrated WPC fibrils were unable to form normally through spontaneous pathway as adding CaCl2; but still could form through nuclear induction pathway with 20 to 30 mM CaCl2, the nuclei accelerated the fibrillation process led to the resistance to the disordered aggregation brought by CaCl2. Moreover, divalent cations (Ca2+, Mg2+) 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 Ca2+ had a greater effect on the fibril formation than Cl−.