Effect of pH on the gel properties and secondary structure of fish myosin |
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Authors: | Ru Liu Si-ming Zhao You-ming Liu Hong Yang Shan-bai Xiong Bi-jun Xie Li-hong Qin |
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Affiliation: | 1. College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei Province 430070, PR China;2. Aquatic Product Engineering and Technology Research Center of Hubei Province, Wuhan, Hubei Province 430070, PR China;3. The Public Laboratory of Electron Microscope, Huazhong Agricultural University, Wuhan, Hubei Province 430070, PR China |
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Abstract: | The relationships between gel properties and the secondary structures of silver carp myosin were investigated at pH 5.5–9.0 using dynamic rheological measurement, circular dichroism and scanning electron microscopy. The gel properties of fish myosin were strongly pH and temperature dependent. During heating at 1 °C/min, myosin formed gels in the pH range 5.5–7.5, but not at pH 8.0–9.0. α-Helix was the predominant structure at pH 7.0. The α-helix fraction declined with increasing temperature and the pH away from 7.0, whilst the other secondary structure fractions increased. The α-helix structure of myosin was more susceptive to acid-treatment than alkali-treatment. As pH increased, the gelation rate and gel strength decreased, and the water-holding capacity (WHC) showed an increasing trend followed by a plateau. High β-sheet and β-turn fractions prior to heating could improve G′ at 90 °C, but they depressed the WHC. A compact and uniform gel of fish myosin was obtained at pH 7.0. |
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Keywords: | Gel property pH Myosin Secondary structure Microstructure |
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