Exploration of molecular interaction between different plant proteins and 2‐pentylfuran: based on multiple spectroscopy and molecular docking

Abstract

AbstractBACKGROUNDSoy 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.RESULTSGas chromatographic–mass spectrometric analysis indicated that different plant proteins were able to adsorb 2‐pentylfuran. Circular dichroism proved 2‐pentylfuran could drive the α‐helix to β‐sheet transition of soy protein, which was not obvious in peanut protein or wheat protein. 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 wheat protein (dynamic quenching).CONCLUSIONThe 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 relies on non‐covalent forces, especially hydrophobic interactions, maintained between the protein and 2‐pentylfuran. © 2023 Society of Chemical Industry.