ArticleFood chemistry: X2025
Insight into the stabilization mechanism of rice protein amyloid fibrils modification on soy protein isolate gels: Gel properties, microstructure, and molecular conformation.
Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Protein Nanofibrils as Emerging Biomaterials for Sustainable Food Packaging: Advances, Challenges, and Future Opportunities.Comprehensive reviews in food science and food safety · 2026Review
- Molecular Mechanism of Rice Protein Amyloid Fibrils in Modulating Gel Properties of Northern Pike (Foods (Basel, Switzerland) · 2026Article
- Plant-Based Yogurt Using Rice Bran and Grain of Green Rice: Increasing the Protein Content of Raw Materials by Enzymatic Protein Extraction.Foods (Basel, Switzerland) · 2026Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The objective of this work was to investigate the effects of rice protein amyloid fibrils (RF) on gel and structural properties of soy protein isolate (SPI) gel. The addition of RF (3 % ∼ 10 %) increased the gel hardness (33.17 g to 74.43 g), thermal stability, viscoelastic properties and microstructure of SPI gel to some extent, whereas the 15 %RF was harmful to these gel properties of SPI gel. Fourier-transform infrared and X-ray diffraction results suggested that RF mainly interacted with SPI through non-covalent interaction, which decreased the proportion of α-helix and increased the β-sheet content of SPI. Molecular interactions indicated that hydrogen bonds and hydrophobic interaction was the main driving force for binding of RF and SPI, and the strength of the non-covalent interaction was determined by the RF content. These findings contributed to the development and manufacturing of SPI gel, as well as enhanced the added value of rice protein.
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