胃蛋白酶和胰蛋白酶对大豆凝集素的稳定性研究  

Stability of soybean agglutinin to pepsin and trypsin

作　　者：张亮亮[1] 侯小强[2] 王利民[1] 孙泽威[1] 刘林娜[1] 赵元[1] 秦贵信[1] 

机构地区：[1]吉林农业大学发展学院,吉林长春130062 [2]军事医学科学院军事兽医研究所,吉林长春130062

出　　处：《畜牧与兽医》2009年第12期1-6,共6页Animal Husbandry & Veterinary Medicine

基　　金：国家自然科学基金(C020302)

摘　　要：本研究以纯化的大豆凝集素(SBA)为研究对象,体外研究了动物体内两大主要蛋白消化酶即胃蛋白酶和胰蛋白酶对其酶解作用。试验通过SDS-PAGE方法分析了SBA经蛋白酶酶解后的降解程度;利用间接竞争ELISA方法测定其在酶解过程中的活性变化。结果表明:SBA可缓慢地被胃蛋白酶降解,SBA浓度越高,完全降解需要的时间越长;随着SBA的降解,SBA的活性也逐渐减小,随着酶解时间的延长活性消失速度也逐渐变慢,并且在本研究选取的酶浓度作用下,SBA浓度越高,活性减小的速度越快,但活性完全消失的时间延长。然而,SBA不能被胰蛋白酶降解,并且酶解过程中SBA的活性也保持完好,说明SBA对胰蛋白酶具有很好的稳定性。因本研究结果将为进一步揭示大豆凝集素在动物体内的消化动力学及其对机体的抗营养作用机理研究奠定理论基础。To investigate the stability of soybean agglutinin （SBA） against pepsin and trypsin degradation in vitro, proteolytic degree of SBA were analyzed by SDS-PAGE. The activity of SBA was detected by indirect competitive ELISA in process of proteolysis. The results of SBA degraded by pepsin showed that SBA can be hydrolyzed by pepsin slowly. The time of complete degradation was prolonged when concentration of SBA was higher. In addition, during the process of proteolysis, activity of SBA diminished and vanished at last. The activity of SBA diminished as the concentration of SBA increased, while, the time of complete disappearance of activity was prolonged. Compared with pepsin degradation, SBA can not be hydrolyzed by trypsin, and activity of SBA was unaffected in the process of enzymolysis. These demonstrated that SBA had high stability to enzymolysis of trypsin. In conclusion, the data provide a foundation for further study on the mechanism of SBA.

关 键 词：大豆凝集素 胃蛋白酶 胰蛋白酶 降解 生物活性 

分 类 号：S816.1[农业科学—饲料科学]