Magnetic field-mediated oxidative modification of myoglobin: One effective method for improving the gel properties of...

This study employed a magnetic field to investigate the impact of myoglobin (Mb) oxidation (0-20 mmol/L H₂O₂) on the gel properties of myofibrillar protein (MP). The results indicated that magnetic field could further facilitate the rearrangement of the Mb structure, resulting in the transfer of its internal reactive groups to the external environment. This contributed to hydration and cross-linking between MP. The Raman spectroscopy results demonstrated that the oxidised Mb altered the secondary structure of MP (increased α-helix content and reduced random coil), making its environment more hydrophobic. This significantly diminished gel water mobility (confirmed by low-field Nuclear Magnetic Resonance). While under the magnetic field treatment, the MP gel network was more relatively porous and uniformly flat, and the gel strength was significantly enhanced (P < 0.05). Ultimately, the water holding capacity increased from 62.47 % to 76.42 %. In conclusion, the magnetic field combined with moderately oxidised Mb had a ripple effect, resulting in an improvement in the gel quality of MP.