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| Effects of Temperature on the Structure and Surface Hydrophobicity of Mixed Myofibrillar Proteins |
| LI Qingzheng1, ZHANG Shunliang2, LUO Yongkang1, FENG Ligeng1,* |
1.College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China;
2. China Meat Research Center, Beijing 100068, China |
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Abstract Temperature is a main factor that affects the change of protein structure and function. This study researched the changes with temperature in secondary structures, conformation, turbidity and surface hydrophobicity of pork and silver carp myofibrillar proteins (MP) as well as their mixture (1:1, m/m) and correlated protein secondary structures with surface hydrophobicity. The results indicated that for all three MP samples, turbidity increased; the contents of α-helix and random coil decreased to a constant level, and β-corner added to constant; protein conformation changed and tended to be stable to adapt to the new environment; surface hydrophobicity increased and then decreased slightly to a stable level with temperature. As a result, the proteins tended to be completely denaturated. The thermal denaturation profile of the pure myofibrillar proteins was not completely the same as that of the mixed ones. The mixture could combine the advantages of pork MP and silver carp MP, and improved their properties with temperature.
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