Interaction between pea protein isolate and quercetin: Effects on protein conformation and quercetin activity

Comprehensive comprehension of the interaction between proteins and polyphenols is crucial for advancing their utilization in food processing. This study investigated no‐covalent interaction between pea protein isolate (PPI) and quercetin (Que) through spectroscopic analysis and molecular simulation. Fourier transform infrared spectroscopy and circular dichroism spectrum showed that the interaction between PPI and Que changed the secondary structure of the protein due to a decrease in α‐helix content and an increase in the random coil. Thermodynamic parameters indicated that the Quebound PPI via hydrogen bonds and hydrophobic interactions (ΔH > 0, ΔS > 0, and ΔG