Investigation of how protein structure affects the adsorption of furan flavor compounds based on flash-evaporation treatment-induced soy protein isolate

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.