本论文对豌豆球蛋白(7S、11S)和豌豆分离蛋白（PPI）的物化和功能特性进行了分析和比较。结果表明，豌豆球蛋白具有良好的功能特性，其溶解度(PS)、乳化能力、乳化稳定性均显著高于PPI。荧光光谱和表面疏水性(H0)分析表明，PPI是部分变性的蛋白，其制备过程中的酸碱处理导致蛋白分子伸展、H0增加。DSC表明，11S热稳定性比7S要高，豌豆分离蛋白和豌豆7S出现不同程度的蛋白变性。

Physicochemical and functional properties of pea globulin (7S, 11S) and pea protein isolate (PPI) were analyzed and compared. The results showed that pea globulin showed excellent functional properties. Its protein solubility (PS), emulsifying ability and stability were much higher than those of PPI. Intrinsic fluorescence spectrum analyses confirmed much loss of tertiary conformation of PPI, which may be attributed to acid and alkaline treatment during PPI preparation resulted in protein denaturation, exposure of hydrophobic groups. DSC showed that thermal stability of 11S was higher than 7 S, and the lower degree of degeneration of the 11S protein. DSC data showed that thermal stability of 11S was higher than 7 S, pea protein isolate and 7S had undergone denaturation.

国家自然科学基金资助项目（B5091230）