Effect of Alkaline pH on the Thermal Aggregation Behavior of Mackerel Myosin
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Abstract:
In order to explore the effect of alkaline pH on the thermal aggregation behavior of mackerel myosin, mackerel myosin was used to explore the effect of pH (7.0, 8.0, 9.0) on the structure and structure of myosin under heating conditions. For the influence of physical and chemical properties (solubility, turbidity, secondary structure, total sulfhydryl content, surface hydrophobicity), the unheated group was used as a blank control group. The results showed that the solubility of myosin in the control group increased from 68.00% to 82.00% at pH (7.0, 8.0, 9.0), and the turbidity did not change significantly; there was a big difference in the heating group, and the solubility increased from 30.00% to 94.00% , The turbidity absorbance value decreased from 0.49 to 0.23; the content of myosin α-helix at pH 9.0 in the heating group decreased, and the content was the lowest among all groups, at 45.60%, and the β-sheet content increased at 10.60%; the sulfhydryl group content of the heating group showed a downward trend, from 70.45 nmol/mg to 50.11 nmol/mg. The protein at alkaline pH facilitates the conversion of sulfhydryl groups into intermolecular and intramolecular disulfide bonds; as the pH value increases, for the myospheroids of the control group, the surface hydrophobicity coefficient of the protein increased successively, while the heating group decreased, but the surface hydrophobicity coefficient of myosin in the heating group was still much higher than that of the control group. In summary, by exploring the properties of myosin thermal aggregates under alkaline conditions, it will conducive to regulate their thermal aggregation and obtain a myosin solution with better thermal stability. The addition of emulsifiers to food is of great significance.
