ArticleFood chemistry: X2026
Interaction mechanism between tetramethylpyrazine and pumpkin seed protein: binding characteristics and functional property changes.
Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Tetramethylpyrazine (TTMP) is a bioactive aroma compound from fermented foods, but its high volatility and short half-life limit application. This study investigated pumpkin seed protein (PSP) as a carrier for TTMP due to its nutritional and functional properties. Multiple characterization techniques and functional assessments were combined to examine the PSP-TTMP system. Results showed that TTMP bound to PSP in a concentration-dependent manner, causing conformational changes. Fluorescence analysis indicated a static quenching process, with spontaneous and exothermic binding mainly driven by hydrogen bonds and van der Waals forces. Structural analyses confirmed that TTMP affected PSP secondary structure, aggregation, surface hydrophobicity, and microstructure, promoting a more ordered and dispersed state at suitable concentrations. Simulations confirmed stable binding between PSP and TTMP through key residues such as ASP, ARG, HIS, and GLN. TTMP also improved PSP antioxidant activity, α-glucosidase inhibition, and emulsion stability, highlighting PSP as a promising volatile flavor carrier.
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