Effect of 6-Gingerol on Oxidation and Structure of Beef Myofibrillar Protein During Heating

High-temperature cooking can induce oxidation and structural changes in myofibrillar protein (MP), harming meat product quality. 6-gingerol is a key part of ginger and a natural antioxidant. In this study, MP was mixed with 6-gingerol and cooked at different temperatures. Chemical methods, fluorescence spectroscopy, Fourier transform infrared spectroscopy (FT-IR), scanning electron microscopy (SEM), and molecular docking were used to study the effects on protein aggregation, oxidation, molecular structure, and the microstructure of muscle fibers. The results showed that 40 μg/mL of 6-gingerol significantly optimized the indexes of beef MP. For example, 6-gingerol inhibited the decrease in MP sulfhydryl content and solubility, delayed the rise in surface hydrophobicity and carbonyl content, decreased the particle size of MP, and elevated the absolute value of Zeta potential, which, in turn, hindered oxidative denaturation and the aggregation of proteins. 6-gingerol could maintain the stability of the spatial conformational structure and microstructure of the protein. The protein secondary structure changed, and the α-helical might have been transformed into the β-folded one. The binding of 6-gingerol to MP mainly relied on hydrogen bonds, van der Waals forces, and hydrophobic interactions. Thus, 6-gingerol had a positive effect on the antioxidant properties and structural stability of beef MP during heating.