Abstract

In this study, the improvement mechanism of low-frequency alternating magnetic field (LF-AMF, 5 mT, 3 h) combined with calcium chloride (CaCl2, 0–100 mM) on the gel characteristics of low-salt myofibrillar protein (MP) was investigated. LF-AMF combined with 80 mM CaCl2 treatment increased solubility (32.71%), surface hydrophobicity (40.86 μg), active sulfhydryl content (22.57%), water-holding capacity (7.15%). Besides, the combined treatment decreased turbidity, particle size and intrinsic fluorescence strength of MP. Fourier transform infrared spectroscopy (FT-IR) results indicated that the combined treatment altered the secondary structure of MP by increasing β-sheet and β-turn, and reducing α-helix and random coil. The combined treatment also induced a high G' value and shortened T2 relaxation time for forming a homogeneous and compact gel structure. These results revealed that LF-AMF combined CaCl2 treatment could as a potential approach for modifying the gel characteristics of low-salt MP.

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