This study examined the interaction between myofibrillar proteins (MPs) and the numbing substance hydroxy-α-sanshool (α-SOH) in a thermal environment, and provided an explanation of the numbness perception mechanism through muti-spectroscopic and molecular dynamics simulation methodology. Results showed that addition of α-SOH could reduce the particle size and molecular weight of MPs, accompanied by changes in the tertiary and secondary structure, causing the α-helix of MPs transitioned to β-sheet and β-turn due to the reorganization of hydrogen bonds. After a moderate heating (60 or 70 °C), MPs could form the stable complexes with α-SOH that were associated with attachment sites and protein wrapping. The thermal process might convert a portion of α-SOH' into hydroxy-β-sanshool' (β-SOH'). When docking with the sensory receptor TRPV1, the RMSD, RMSF and binding free energy all showed that β-SOH' demonstrated a low affinity, thereby reducing the numbing perception. These findings can provide a theoretical foundation for the advanced processing of numbing meat products.
Keywords: Hydroxy-α-sanshool; Meat protein; Molecular simulation; Sensory properties; TRPV1.
Copyright © 2024 Elsevier Ltd. All rights reserved.