This experiment aims to study the effect of HL-low sodium salt on the gel properties of goose muscle fibrillin in Fenton oxidation system. Goose meat myofibrillar protein (MP) was used as the raw material, and 0.1%, 1%, and 3.5% NaCl added groups were used as controls, and 0.1%, 1%, 1.5%, 2.5%, and 3.5% HL-low sodium salt treatment group on the gel strength, gel cooking loss rate, gel water retention, gel chemical force and gel rheology of MP after oxidized by Fenton oxidation system for 24 h, 48 h and 72 h. The study found that with the extension of the oxidation cycle, the content of ionic bonds, hydrogen bonds, and disulfide bonds in MP gels decreased significantly (P<0.05), while hydrophobic interactions increased significantly (P<0.05). At the same time, the elastic modulus, gel strength and gel water retention of the MP gel were significantly reduced (P<0.05), and the gel cooking loss rate was significantly increased (P<0.05). In the same oxidation cycle, with the increase of NaCl and HL-low sodium salt, the content of hydrogen bonds, hydrophobic interactions, and disulfide bonds in MP gels is increasing, while the content of ionic bonds is decreasing. At the same time, the elastic modulus, gel strength and water retention of the MP gel were significantly increased (P<0.05), and the cooking loss rate of the gel was significantly reduced (P<0.05). When the addition ratio of HL-low sodium salt reaches 2.5%, the gel properties of MP and the gel properties of 3.5% NaCl treatment group are not significantly different or some properties are significantly better than the gel properties of 3.5% NaCl treatment group. This test provides a reference for the future research of HL-low sodium salt for myofibrillar protein.
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