ArticleFood science & nutrition2025
Amyloid Fibrils of Pea Protein Isolated Induced by Cold Plasma Treatment and Its Stabilization on High Internal Phase Emulsions.
Article in Food science & nutrition, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Amyloid Fibrils of Pea Protein Isolated Induced by Cold Plasma Treatment and Its Stabilization on High Internal Phase Emulsions.Food science & nutrition · 2025Article
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7 authors.
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Abstract
The potential of forming pea protein isolate (PPI) amyloid fibrils promoted by cold plasma (CP) treatment (40 kV; 0, 3, 5, and 7 min), heat treatment (85°C for 12 h), and its ability to stabilize high internal phase emulsions (HIPEs) was investigated. Results indicated that rod-like amyloid fibrils of PPI were successfully formed and promoted by CP treatment, with a 12 nm diameter and 132-261 nm average length, as confirmed by Thioflavin T (ThT) fluorescence spectroscopy, SEM, and TEM. The globular structure unfolding, cleavage of the backbone of PPI by CP treatment, release of the building block "β-strands" structure, and assembly of the building blocks into fibrils during the fibrillation process were confirmed by SDS-PAGE, FTIR, fluorescence spectroscopy, and hydrophobic analysis. Compared with native PPI, fibrous PPI exhibited a strong capacity for stabilizing HIPEs, and the ability to stabilize HIPEs was PPI fibrils length dependent. Compared with HIPEs stabilized by long fibrils (CP5PF-8 and CP5PF-12), the HIPEs prepared by short fibrils (CP5PF-2 and CP5PF-4) displayed better thermal stability. Moreover, CP5PF-stabilized HIPEs exhibited excellent ionic and storage stability, while PPI amyloid fibrils with shorter lengths (CP5PF-2 and CP5PF-4) showed superior performance compared with longer fibrils lengths (CP5PF-8 and CP5PF-12).
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