Regulatory mechanism and flavor perception of heat induced conformational changes in chicken myofibrillar proteins on the binding affinity with sanshool and capsaicin
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引用次数: 0
Abstract
The interaction mechanisms between sanshool and capsaicin with chicken myofibrillar proteins (MPs) under thermal-induced conditions (25–100 °C) have been systematically investigated. By analyzing the characteristics of MPs- sanshool/capsaicin -complex, heating process significantly altered MPs conformation, exposing internal hydrophobic groups and disulfide bonds, affecting binding properties. Flavor adsorption experiments demonstrated enhanced release of linalool and progressively strengthened adsorption of trans-2-decenal and trans-2,4-decadienal with rising temperatures. Molecular docking simulations indicated that sanshool and capsaicin spontaneously bind to TRPV1/TRPA1 sensory receptors through hydrogen bonds, hydrophobic forces, and van der Waals interactions. Sanshool binds to TRPV1 with energies of −6.42 and −6.06 kcal/mol, lower than capsaicin's −4.96 and −4.52 kcal/mol. This enhanced energy release potentiates neuronal tingling perception. Fluorescence analysis showed that the formation of the MPs-capsaicin complex is dominated by hydrogen bonds and van der Waals forces, while the formation of the MPs-sanshool complex primarily relies on hydrophobic interactions and electrostatic forces.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.