Abstract In this paper, the structural, thermodynamic, and rheological properties of soybean 7S globulins extracted by bis(2-ethylhexyl) sulfosuccinate sodium salt (AOT)/isooctane reverse micelle method and alkali extraction-acid precipitation method were studied. Amino acid composition results showed that the 7S globulin produced by reverse micelle had more hydrophobic and sulfur-containing amino acids. Fourier transform infrared spectroscopy results demonstrated that the 7S globulin extracted by reverse micelle had more β-sheets but less turn structure, and formed a more compact conformation. However, lower surface hydrophobicity was observed in the 7S globulin extracted by reverse micelle, indicating that the reverse micelle environment could protect the native folded structure of protein. Thermal stability tests showed that the 7S globulin extracted by reverse micelle had poorer thermostability with lower denaturation temperature, which was in accordance with the results of initial gelling temperature. Final storage modulus (G’) and frequency sweep results revealed that the 7S globulin obtained by reverse micelle produced a harder textured gel.

中文翻译：

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反胶束对大豆7S球蛋白理化性质的影响

摘要 本文研究了双(2-乙基己基)磺基琥珀酸钠(AOT)/异辛烷反胶束法和碱提取-酸沉法提取大豆7S球蛋白的结构、热力学和流变学性质。氨基酸组成结果表明，反胶束产生的7S球蛋白含有较多的疏水性和含硫氨基酸。傅里叶变换红外光谱结果表明，反胶束提取的7S球蛋白β-折叠较多，转角结构较少，构象更为紧密。然而，在反胶束提取的 7S 球蛋白中观察到较低的表面疏水性，表明反胶束环境可以保护蛋白质的天然折叠结构。热稳定性试验表明，反胶束提取的7S球蛋白热稳定性较差，变性温度较低，与初始胶凝温度结果一致。最终储能模量 (G') 和频率扫描结果表明，通过反胶束获得的 7S 球蛋白产生了质地较硬的凝胶。