The conformational modification of myofibrillar protein by magnetic field improves its emulsification properties.

ABSTRACT

This study investigated the effect of different magnetic field treatments (0, 3, 6, 9, 12 mT) on the structure and emulsification properties of myofibrillar protein (MP). The results showed that the emulsion stabilized by MP with 3, 6, 9 mT magnetic field treatments possessed higher emulsifying ability, storage stability and apparent viscosity, since magnetic field induced the structural unfolding of MP and exposed the hydrophobic groups (the surface hydrophobic increased from 30.10 to 43.73 µg). Meanwhile, the magnetic field treatments decreased the MP particle size from 1752.00 to 1278.67 nm, which was favorable for the diffusion and adsorption of proteins at the oil-water interface, thus improving the MP emulsification ability and stability. Furthermore, the 9 mT magnetic field-treated MP had the best ability to emulsify oil droplets with a more uniform and smaller emulsion size from 28.593 to 23.443 µm. However, high-intensity magnetic field treatment (12 mT) caused MP particles to aggregate and the hydrophobic binding sites to be buried, which was not conducive to encapsulating oil droplets.