摘要
圆二色性分析结果表明，醇变性使大豆蛋白α－螺旋构象的含量增加，结构更加有序；同时，荧光偏振测定显示大豆蛋白分子的链运动自由度发生变化。另一方面，大豆蛋白紫外差示光谱未出现负峰，荧光发射波长不变，说明蛋白质的疏水核未被破坏，因而是一种局部变性。运用″溶剂吸附″模型对大豆蛋白的醇变性过程作了理论阐述。
Circular dichroism(CD) demonstrated that the content of α-helix conformation of alcohol denatured soy protein increased, fluoresence polarization analysis showed that,after alcohol denaturation, the peptide chain became more flexible. On the other hand,UV difference spectroscope did not give negative peaks and the fluorescence emit wavelenght did not shift toward red end. The results led to the conclusion that soy protein undergoes a kind of ″partial denaturation, in which the hydrophobic core of soy protein remains intact while the conformation of the hydrophilic shell has been changed. Theoratical elucidation of soy protein alcohol denaturation by solvent preferential binding was attempted.
