Effect of reverse micelle on conformation of soy globulins: A Raman study
Effect of reverse micelle on conformation of soy globulins: A Raman study
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DOI：
10.1016/j.foodchem.2009.02.028
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发表时间：
2009-09
期刊：
影响因子：
8.8
通讯作者：
Xiaoyan Zhao;Q. Ao;Fusheng Chen;W. Xue;Li-te Li-Li-te-Li-2107892923;Jie Liu
中科院分区：
文献类型：
--
作者：
Xiaoyan Zhao;Q. Ao;Fusheng Chen;W. Xue;Li-te Li-Li-te-Li-2107892923;Jie Liu
利用拉曼光谱研究了水相缓冲和反胶束萃取大豆蛋白中7S和11S球蛋白的主链和侧链构象的变化。用两种方法提取的7S和11S球蛋白由于其特有的氨基酸组成和分子构象，表现出典型的光谱特征(如酰胺I、III区和特定残基的侧链构象)。相比之下，使用反胶束萃取的两种球蛋白的分子无序程度都增加了，并出现了新的条带。通过准确测量谱带强度，可以估计不同结构的7S和11S球蛋白的相对含量。最后，反胶束萃取11S球蛋白中拉曼酪氨酸双峰的I850/830强度比的增加表明酪氨酸残基向更暴露的状态转变，这与反胶束上呈现的更无序的构象很好地一致。
Raman spectroscopy was applied to investigate the main and side chain conformational changes of 7S and 11S globulins from soybean proteins using aqueous buffer and reverse micelle extraction. The 7S and 11S globulins using two extraction methods displayed typical spectral features (such as amide I, III region and the side chain conformations of particular residues) due to characteristic amino acid composition and molecular conformation. In comparison, the degree of molecular disorder increased in both globulins using reverse micelle extraction and new bands appeared. The relative amount of different structures of 7S and 11S globulins could be estimated through accurate measurement of the band intensities. Finally, the increase of the I850/830intensity ratio of Raman tyrosine doublet in 11S globulin with reverse micelle extraction suggested a change towards a more exposed state of tyrosine residues, in good agreement with the more disordered conformation taken upon reverse micelle.