Sousa I M, Mitchell J R, Ledward D A, Hill S E, da Costa M L
SACTA, Instituto Superior de Agronomia, Universidade Técnica de Lisboa, Portugal.
Z Lebensm Unters Forsch. 1995 Dec;201(6):566-9. doi: 10.1007/BF01201587.
Differential scanning calorimetry (DSC) was used to study the 7S and 11S globulin fractions extracted from lupin seed (Lupinus luteus) flour. In agreement with previous work on other lupin species, the isolate showed three denaturation peaks compared to the two observed with soy. By comparison with the isolated globulin fractions, the denaturation peaks at the two higher temperatures in the lupin isolate were assigned to the 11S and 7S globulins. The denaturation temperature of the lupin 7S globulin was about 10 K higher than that for the corresponding soy globulin, whereas the values for the 11S globulin were similar. All globulins displayed increasing thermal stability with decreasing moisture contents. Possible reasons for the differences in behaviour of soy and lupin protein isolates are discussed.
采用差示扫描量热法（DSC）研究了从羽扇豆种子（白羽扇豆）粉中提取的7S和11S球蛋白组分。与之前对其他羽扇豆品种的研究一致，该分离物显示出三个变性峰，而大豆分离物观察到两个变性峰。与分离的球蛋白组分相比，羽扇豆分离物中两个较高温度下的变性峰归属于11S和7S球蛋白。羽扇豆7S球蛋白的变性温度比相应大豆球蛋白的变性温度高约10K，而11S球蛋白的值相似。所有球蛋白都表现出随着水分含量降低热稳定性增加的趋势。讨论了大豆和羽扇豆蛋白分离物行为差异的可能原因。
