大豆蛋白-酪蛋白复合物结构的红外光谱分析

FTIR Analysis on the Structure of Soybean-Casein Protein Complex

使用傅里叶变换红外光谱技术对大豆蛋白-酪蛋白组装物的二级结构进行研究。组装物在酰胺Ⅰ带和Ⅲ带位置中各特征峰相互叠加,采用Gausses峰型对圆头峰进行拟合、解析,判断其α-螺旋,β-折叠,β-转角和无规则卷曲的相对含量。研究发现:酰胺Ⅰ带和酰胺Ⅲ带在数值上对CNPSPC的二级结构定量表现出差异性,而在pH对CNPSPC的β-折叠结构及α-螺旋结构的影响上表现一致,即随着p H值的增大,α-螺旋结构含量呈先降低后增加趋势,β-折叠含量呈现先增加后降低的趋势,且在pH 6.0时含量最大。

The secondary structure of soybean-casein assembly was studied using Fourier transform infrared spectroscopy(FTIR) techniques. Due to the type of assembly product in amide Ⅰ belt and Ⅲ belt position, each characteristic peaks overlap, so the type of round head Gausses peak fitting, parsing, judge the α-helix, β-sheet, β-turn and Random coil relative content. It was found that amide Ⅰ was difference from amide Ⅲ to secondary structure quantitative of CNPSPC in the numerical. But the effect of p H on the β-folding and the α-helix structure of CNPSPC is consistent;With the increase of pH, The content of α-helix structure decreases and then increases. The content of the β-folding increases and then decreases, and when pH6.0 beta folding content is the largest.