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中国精品科技期刊2020
刘妍妍,陈文璐,李建立,等. 复合保护剂与牛IgG的相互作用机制研究[J]. 食品工业科技,2023,44(11):45−53. doi: 10.13386/j.issn1002-0306.2022050111.
引用本文: 刘妍妍,陈文璐,李建立,等. 复合保护剂与牛IgG的相互作用机制研究[J]. 食品工业科技,2023,44(11):45−53. doi: 10.13386/j.issn1002-0306.2022050111.
LIU Yanyan, CHEN Wenlu, LI Jianli, et al. Study on the Interaction Mechanism between Compound Protective Agent and Bovine IgG[J]. Science and Technology of Food Industry, 2023, 44(11): 45−53. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022050111.
Citation: LIU Yanyan, CHEN Wenlu, LI Jianli, et al. Study on the Interaction Mechanism between Compound Protective Agent and Bovine IgG[J]. Science and Technology of Food Industry, 2023, 44(11): 45−53. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022050111.

复合保护剂与牛IgG的相互作用机制研究

Study on the Interaction Mechanism between Compound Protective Agent and Bovine IgG

  • 摘要: 本研究综合利用紫外吸收光谱法、荧光光谱法、傅里叶变换红外光谱法、圆二色谱法、拉曼光谱法、扫描电镜法和差示扫描量热法研究复合保护剂与IgG的相互作用机制以及IgG结构的变化。结果表明复合保护剂对IgG的肽骨架影响较小,而对氨基酸残基的微环境影响较大,使IgG氨基酸残基所处的微环境极性增强;复合保护剂与IgG的相互作用主要涉及氢键、静电作用力和疏水作用力,并引起IgG的二级结构从α-螺旋结构向β-折叠、β-转角和无规卷曲结构转变,使IgG的二级结构趋于无序化,IgG二硫键构型由g-g-g构型逐渐转变为g-g-t构型和t-g-t构型。扫描电镜表明,复合保护剂在IgG分子表面形成不规则的棱形晶体复合物;差示扫描量热法表明,复合保护剂使IgG的变性温度从71.76 ℃升高到87.22 ℃,IgG的热焓变从6.51 J/g降低到4.68 J/g。说明复合保护剂使IgG分子的构象发生转变,从而增强了IgG的热稳定性。

     

    Abstract: In this study, ultraviolet absorption spectroscopy, fluorescence spectroscopy, Fourier transform infrared spectroscopy, circular dichroism, Raman spectroscopy, scanning electron microscopy and differential scanning calorimetry were used to study the interaction of composite protectants with IgG mechanisms and changes in IgG structure. The results showed that the compound protective agent had little effect on the peptide skeleton of IgG, but had a great effect on the microenvironment of amino acid residues, which enhanced the polarity of the microenvironment of amino acid residues in IgG. The interaction of compound protective agent and IgG mainly involved hydrogen bond, electrostatic force and hydrophobic force, and caused the secondary structure from to changed from α-helix structure to β-folding, β-turning and random curl structure of IgG tended to disorder the secondary structure. The IgG disulfide bond configurations gradually changed from g-g-g to g-g-t and t-g-t. The results of SEM showed that the compound protective agent formed irregular prismatic crystal complexes on the surface of IgG molecules, differential scanning calorimetry showed that the compound protective agent increased the denaturation temperature of IgG from 71.76 ℃ to 87.22 ℃, and decreased the enthalpy change of IgG from 6.51 J/g to 4.68 J/g. The results showed that the conformation of IgG molecule was changed by compound protective agent, which enhanced the thermal stability of IgG.

     

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