LAUSR

BACKGROUND Soy protein, peanut protein, and wheat protein are commonly applied in plant-based products, but specific off-odor makes it difficult for consumers to accept, with 2-pentylfuran being one of the most representative flavors. In this study, 2-pentylfuran was employed as an example to explore the behavior and mechanism of the three proteins in absorbing off-odors. RESULTS Gas chromatography-mass spectrometry (GC-MS) analysis indicated that different plant proteins were both able to adsorb 2-pentylfuran. Circular dichroism proved 2-pentylfuran could drive the α-helix to β-sheet transition of SPI, which was not obvious in PnPI and WPI. Ultraviolet spectroscopy tentatively determined that 2-pentylfuran caused changes in the tyrosine and tryptophan microenvironments of different plant proteins, which were further evidenced by synchronous fluorescence at fixed wavelength intervals of 15 nm and 60 nm. Static quenching of protein intrinsic fluorescence indicated that they formed a stable complex with 2-pentylfuran, except for WPI (dynamic quenching). CONCLUSION The various conformations of the three proteins are the main reason for the difference in flavor retention of protein. Soy protein, peanut protein, and wheat protein adsorbing 2-pentylfuran rely on non-covalent forces, especially hydrophobic interactions, maintained between the protein and 2-pentylfuran. This article is protected by copyright. All rights reserved.