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中文摘要：
11S大豆球蛋白的结构及其功能特性存在天然的局限性,经过前期蛋白酶酶解-复聚后,得到改性11S球蛋白。利用扫描电镜分析仪、X射线衍射仪、DSC和氨基酸分析仪,从不同角度探讨改性后的11S球蛋白内部结构的变化,更加清晰和全面地认识复合酶改性对大豆11S球蛋白解离和聚集行为的影响,并阐明其改性机理。
英文摘要：
The structure and functional properties of l lS soybean globulin has natural limitations. The modified 11S globulin was obtained for application through enzymatic hydrolysis-aggregation. In recent years, research mainly concentrated in the effect of enzymes on the properties of globulin, and the internal structure of 11S globulin was ignored. In this study, the changes of the internal structure of modified 11S globulin from different point of view was characterized using scanning electron microscope （SEM）, X-ray diffraction （XRD）, differential scanning calorimeter （DSC） and amino acid analyzer. The results indicated that enzymatic hydrolysis of protease-polymerization changed the denatured temperature of 11S soybean globulin. The results also showed that the content of essential amino acids was improved through modification, which increased the nutritional value of 11 S soybean globulin. During this process, the hydrophobic properties of surface was firstly reduced and then increased later. In this study, comprehensive understanding the influence of enzyme modification on dissociation and aggregation behavior of l lS soybean globulin were presented which might contributed to illuminate its modification mechanism.
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