Multispectral characterization, molecular docking, and dynamics simulation of trans-cinnamaldehyde–ovalbumin interactions: implications for gel texture, water retention, and microstructural properties

This study investigated the interaction between trans-cinnamaldehyde (TC) and ovalbumin (OVA) at the molecular level and its impact on the gel properties of OVA. Multispectral analysis, molecular docking, and molecular dynamics simulations were employed to elucidate the underlying mechanisms. At room temperature, TC bound to OVA mainly through non-covalent interactions, characterized by static quenching, which consequently altered the secondary structure of OVA. Moderate TC incorporation significantly enhanced the textural properties of thermally induced OVA gels, with hardness, chewiness, and gumminess increased by 39.4%, 28.0%, and 34.9%, respectively (P < 0.05 ). In addition, TC treatment improved the gel's water-holding capacity (by 4.38%), optimized water distribution, and promoted a more uniform microstructure. These improvements were primarily attributed to TC-induced Schiff base formation and non-covalent interactions, which collectively modulated intermolecular forces within OVA. Overall, this study provides novel insights into the use of spice-derived compounds to enhance the structure and functional quality of protein-based foods.