在低盐溶液中使用脯氨酸提高罗非鱼肌球蛋白的溶解度。
Enhancing tilapia fish myosin solubility using proline in low ionic strength solution.
机构信息
Department of Food Science & Technology, National University of Singapore, Singapore 117542, Singapore; National University of Singapore (Suzhou) Research Institute, 377 Lin Quan Street, Suzhou Industrial Park, Suzhou, Jiangsu 215123, PR China.
Department of Food Science & Technology, National University of Singapore, Singapore 117542, Singapore; National University of Singapore (Suzhou) Research Institute, 377 Lin Quan Street, Suzhou Industrial Park, Suzhou, Jiangsu 215123, PR China.
出版信息
Food Chem. 2020 Aug 1;320:126665. doi: 10.1016/j.foodchem.2020.126665. Epub 2020 Mar 21.
The effects of using proline to solubilise fish myosin under low ionic strength conditions were studied. After solubilising myosin in 0.1 M NaCl containing 5, 10, 15, and 20 mM proline, respectively, it was observed that more than 80% of the myosin was effectively solubilised using 10 mM proline. The addition of 10 mM proline lowered the surface hydrophobicity of myosin from 18.25 to 8.22 mg/g, increased the amount of β-sheet structure from 33.87% to 46.88%, both of which facilitated solubilisation. As revealed by transfer free energy measurements, the interactions between proline and tyrosine and tryptophan residues were more favourable. Furthermore, the ability of proline to shield hydrophobic sites of myosin and to partially break disulphide bonds helped to form myosin oligomer aggregates. Transmission electron microscopy images verified the effects of proline on myosin proteins. A solubilisation mechanism based mainly on chemical interactions between myosin and proline was proposed.
研究了在低离子强度条件下使用脯氨酸溶解鱼肌球蛋白的效果。分别在含有 5、10、15 和 20 mM 脯氨酸的 0.1 M NaCl 中溶解肌球蛋白后，发现使用 10 mM 脯氨酸可有效溶解超过 80%的肌球蛋白。添加 10 mM 脯氨酸将肌球蛋白的表面疏水性从 18.25 降低到 8.22 mg/g，并将 β-折叠结构的含量从 33.87%增加到 46.88%，这都有助于溶解。通过转移自由能测量发现，脯氨酸与酪氨酸和色氨酸残基之间的相互作用更有利。此外，脯氨酸屏蔽肌球蛋白疏水区和部分打断二硫键的能力有助于形成肌球蛋白寡聚体聚集物。透射电子显微镜图像证实了脯氨酸对肌球蛋白蛋白的影响。提出了一种主要基于肌球蛋白和脯氨酸之间化学相互作用的溶解机制。
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