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| Influence of Oxidative Modification of Hemin Prosthetic Group of Myoglobin on the Structure and Properties of Myosin |
| ZHU Hongxing, WANG Daoying, XU Weimin, SUN Chong, GE Qingfeng, GAO Tianyi, HUANG Yang |
| 1.College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China; 2.Institute of Agri-products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China |
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Abstract In this paper, the influence of oxidative modification of the hemin prosthetic group of myoglobin on the carbonyl and sulfhydryl groups, surface hydrophobicity, solubility, ATPase activity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile, endogenous fluorescence, and secondary structure of myosin. Meanwhile, molecular dynamics simulation was performed on myoglobin with oxidative modification of its hemin prosthetic group. The results showed that the surface hydrophobicity of myosin significantly decreased (P < 0.05) when the hemin prosthetic group was oxidized at low concentrations, but significantly increased (P < 0.05) at high concentrations, together with a significant reduction in the solubility (P < 0.05). Hemin prosthetic group modification significantly decreased the contents of total and reactive sulfhydryl groups and Ca2+-ATPase activity of myosin (P < 0.05). In addition, this treatment reduced the fluorescence intensity of myosin accompanied by a spectral blue shift and the proportion of α-helix indicating conformational changes in myosin. Molecular dynamics simulation revealed that the hemin prosthetic group could bind to myosin. However, its oxidation at high concentrations was detrimental to maintaining the stability of myosin. In a word, oxidative modification of the hemin prosthetic group could cause structural changes in myosin and consequently affect meat quality.
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2020, Vol. 34 
