Effect of static magnetic field-assisted freezing at different temperatures on the structural and functional properties of pacific white shrimp (Litopenaeus vannamei) myofibrillar protein.

The effects of static magnetic field-assisted freezing (MF) on the structural and functional characteristics of Litopenaeus vannamei myofibrillar protein (MP) at various temperatures (-35 ∼ -20 °C) were examined to assess its influence on MP and its energy-saving potential. The results indicated that -35 °C MF (MF-35) exhibited greater solubility and lower turbidity than -35 °C immersion freezing (IF-35), suggesting that MF-35 inhibited MP aggregation. MF-35 prevented the reduction in fluorescence intensity and α-helix content, protecting the MP tertiary and secondary structures. The emulsifying stability and gel strength of MF-35 surpassed those of the other frozen samples, indicating that MF-35 was the most efficient at mitigating the degradation of MP emulsifying and gel properties generated by freezing. No significant differences in solubility, surface hydrophobicity, emulsifying activity, and gel strength were detected between IF-35 and MF-25 (P > 0.05). In conclusion, MF impeded the denaturation of MP and exhibited energy-saving potential.