ArticleFood chemistry: X2025
Investigation of how protein structure affects the adsorption of furan flavor compounds based on flash-evaporation treatment-induced soy protein isolate.
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.
- Interaction differences between selected sweet-fragrant aroma compounds and different salivary proteins: Effects of molecular structure.Food chemistry: X · 2026Article
- Recent Advances in the Study of Aroma Control and Release Through the Interaction of Matrix Components and Aroma Compounds in Soft Drinks.Journal of food science · 2026Review
- Characterization of key off-flavor compounds in soybean and their dynamic changes during progressive processing.Frontiers in nutrition · 2026Article
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Authors and funding
9 authors.
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Abstract
This study investigates the binding capacity and mechanism of flash-evaporation-treated SPI with 2-acetylfuran at 75-130 °C. SPME-GC/MS, spectroscopic methodologies, FRET, and ITC are used to estimate binding ability. The highest binding percentage (89.17 %) is observed at 100 °C. The conformational changes of flash-evaporation-treated SPI reveal that 100SPI exhibits the highest flexibility and solubility, as well as lower surface tension. Correlation analysis demonstrates that the structural changes of 100SPI enhance the effective binding between SPI and 2-acetylfuran, thereby improving the adsorption capacity of SPI. This work offers a theoretical foundation for flavor selection in SPI-based food production by shedding light on the mechanism through which conformational changes in flash-evaporation-treated SPI impact its capacity for flavor adsorption.
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