ArticleUltrasonics sonochemistry2026
Ultrasonic-assisted production of okara protein isolate amyloid fibrils from plant-based by-products: Structural and morphological characteristics.
Article in Ultrasonics sonochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The amyloid fibrilliation technology of plant proteins points to the development of new functional foods using plant processing by-products. Okara protein isolate (OPI) is such a sustainable protein resource from soybean processing, with huge output and rich nutrition. This study employed ultrasonic pretreatment to enhance the fibrillation capacity of OPI. Following ultrasonic pretreatment, heating at 90 °C under pH 2 conditions for 9 h yielded amyloid fibrils with high conversion rates, validated through ThT fluorescence, SDS-PAGE, and AFM techniques. UV and FTIR analyses confirmed the formation of amyloid fibril structures rich in characteristic cross-β-sheets. Furthermore, this study revealed that ultrasonic pretreatment may partially unfold proteins and expose hydrophobic regions, subsequently promoting amyloid fibril aggregation during incubation. Conversely, excessive ultrasonic pretreatment may lead to over-unfolding of protein structures, resulting in structural instability that hinders amyloid fibril aggregation. This research not only elucidates the mechanism by which ultrasound regulates amyloid fibril formation but also provides a practical solution for the application of soybean residue protein in the field of food science.
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