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中国精品科技期刊2020
胡婷,耿勤,付敏,等. 多光谱学与分子模拟技术表征甜菜苷与乳清蛋白的相互作用[J]. 华体会体育,2022,43(23):86−94. doi: 10.13386/j.issn1002-0306.2022020243.
引用本文: 胡婷,耿勤,付敏,等. 多光谱学与分子模拟技术表征甜菜苷与乳清蛋白的相互作用[J]. 华体会体育,2022,43(23):86−94. doi: 10.13386/j.issn1002-0306.2022020243.
HU Ting, GENG Qin, FU Min, et al. The Interaction between Betanin and Whey Protein: Based on Multi-spectroscopy and Molecular Simulation[J]. Science and Technology of Food Industry, 2022, 43(23): 86−94. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022020243.
Citation: HU Ting, GENG Qin, FU Min, et al. The Interaction between Betanin and Whey Protein: Based on Multi-spectroscopy and Molecular Simulation[J]. Science and Technology of Food Industry, 2022, 43(23): 86−94. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022020243.

多光谱学与分子模拟技术表征甜菜苷与乳清蛋白的相互作用

The Interaction between Betanin and Whey Protein: Based on Multi-spectroscopy and Molecular Simulation

  • 摘要: 为研究甜菜苷(Betanin)与乳清分离蛋白(Whey protein isolate, WPI)的相互作用及乳清分离蛋白对甜菜苷热稳定的影响,本文通过自组装法构建了WPI-Betanin复合物,利用紫外可见光谱验证了复合物的形成,并通过荧光光谱和圆二色谱探究了复合物形成的作用机制及蛋白质结构的变化,最后采用分子模拟技术将复合物相互作用可视化。结果表明,甜菜苷与乳清分离蛋白主要通过氢键与范德华力形成复合物,结合位点数约为1。复合物的形成导致蛋白的浊度增加,表面疏水性降低,内源荧光猝灭,且猝灭机制为静态猝灭,常温下的猝灭常数为1.78×103 L/mol。相互作用改变了乳清分离蛋白中色氨酸、酪氨酸的微环境和二级结构含量,使甜菜苷在80 ℃下加热1 h的保留率从6.17%提高到27.26%。本研究为功能性蛋白色素复合物的应用开发和甜菜苷的护色提供了理论基础。

     

    Abstract: In order to study the interaction between betanin and whey protein isolate (WPI) and the effect of whey protein isolate on the thermal stability of betanin, WPI-Betanin complex was constructed by self-assembly method. UV-vis spectroscopy was used to verify the formation of complex. The mechanism of complex formation and the changes of protein structure were investigated by fluorescence spectroscopy and circular dichroism, and the complex was visualized by molecular simulation technology. The results showed that betanin and whey protein isolate formed a complex mainly through van der Waals force and hydrogen bond, and the number of binding sites was about 1. The formation of the complex resulted in increased turbidity and decreased surface hydrophobicity of the protein, and the quenching mechanism was static, with a quenching constant of 1.78×103 L/mol at room temperature. The interaction changed secondary structure contents and the microenvironment of tryptophan and tyrosine in whey protein isolate. Moreover, the thermal stability of betanin was improved by WPI. The retention rate of betanin increased from 6.17% to 27.26% after heating at 80 ℃ for 1 h. This study provides a theoretical basis for the application and development of functional protein pigment complex and the color protection of betanin.

     

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