Effect of pH on the gel properties and secondary structure of fish myosin
2010
Liu, Ru | Zhao, Si-ming | Liu, You-ming | Yang, Hong | Xiong, Shan-bai | Xie, Bi-jun | Qin, Li-hong
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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