Off-odor removal in chicken meat: Role of phenolic Compound–Myofibrillar protein interactions

Epigallocatechin gallate (EGCG) and epigallocatechin (EGC) are promising in removing off-odor in meat products. Their removal mechanisms on chicken meat off-odor were investigated in this study by using bond-breaking, multispectral, and molecular docking methods. The results showed that the addition of EGCG and EGC changed the conformation of myofibrillar protein (MP), enhanced protein-protein interactions, and promoted protein aggregation. Compared to the control, the surface hydrophobicity of MP respectively reduced by 63.49% and 64.39% at 80 μmol/L of EGC and EGCG, while the α-helix content increased by 77.35% and 110.09%, respectively. Binding force analysis and molecular docking of off-odor compounds and MP both revealed that aldehydes predominantly bound to MP through hydrophobic interactions, whereas 1-octen-3-ol interacted with MP through hydrogen bonds. Notably, off-odor compounds and two phenolic compounds competitively bound to MP at the amino acid sites of VAL 659, LYS 274, and ARG 440, thereby enhancing the release of off-odor compounds. Among the two phenolic compounds, EGCG exhibited better removal effects than EGC. When adding EGC at 80 μmol/L, 1.89-fold of decanal and 2.29-fold of nonanal than those in the control were released from chicken meat. These findings provided deep insight into the polyphenol-induced off-odor removal in chicken meat. • Epigallocatechin gallate exhibits a stronger interaction with MP in chicken meat. • Five aldehydes predominantly bind to MP mainly through hydrophobic interactions. • 1-Octen-3-ol binds to MP mainly through hydrogen bonds and ionic bonds. • Phenolics and off-odors competitively bind to MP, thus achieving off-odor removal. • VAL 659, LYS 274, and ARG 440 were the key competition binding sites of MP.