Abstract
This study aimed to investigate the effect of a low-frequency magnetic field (LF-MF; 0, 0.25, 0.5, and 1.4 mT) on the gel properties of pork myofibrillar protein (MP) and to explore potential mechanisms. The water-holding capacity (WHC) and rheological properties of MP gels treated at 0.5 mT were better than those from other treatments. The water mobility did not change significantly as intensity increased, while the ratios of immobilized water (PT21) and free water (PT22) significantly decreased and increased, respectively. This suggested that the effect of LF-MF on MP hydration might be related to the formation of water clusters. Raman spectra suggested that α-helices unfolded and β-sheets, β-turns, and random coils were formed in MP gels (from 0.25 to 1.4 mT). Furthermore, the intensities of characteristic peaks in the tryptophan and aliphatic residues band were highest at 0.5 mT, indicating that 0.5 mT was the optimum intensity for hydrophobic interactions.
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