四个抗豆象绿豆品种的胰蛋白酶抑制剂稳定性

以4个抗豆象绿豆C6749、C5200、C5193和C5205为试材, 以感豆象绿豆晋绿1号为对照, 测定和研究其胰蛋白酶抑制剂活性在高温高压、变性剂和还原剂处理后的稳定性。结果表明, 4个抗豆象绿豆胰蛋白酶抑制剂活性均高于对照(P<0.01), 且C5200>C5193>C6749>C5205, 在不同高温高压、变性剂和还原剂处理后残余活性均比对照高, 残余活性随温度压力升高、处理时间延长, 变性剂和还原剂处理时间的延长明显下降, 变性剂、还原剂对抗豆象绿豆胰蛋白酶抑制剂残余活性的影响表现为: 盐酸胍>尿素, TCEP>DTT>β-ME。4个抗豆象绿豆中C5200的耐高温高压性、耐变性和耐还原性最强, C5193次之; C5205的耐高温高压性、耐变性最差, C6749耐还原性最差。说明4个抗豆象绿豆中C5200和C5193是抗豆象绿豆胰蛋白酶抑制剂残余活性保存较高的2个品种, 有较大的应用价值。

Stability of Trypsin Inhibitor in Foun Bruchid-Resistant Mung Bean Varieties

Taking bruchid-resistant mung beans C6749, C5200, C5193, and C5205 as experimental materials, with a susceptible mung bean Jinlyu 1 as control, the activity and the stability of mung bean trypsin inhibitor were measured under high temperature, high pressure, denaturant and reductant stresses. The trypsin inhibitor activities of four bruchid-resistant mung beans were significantly higher (P<0.01) than those of control (Jinlyu 1), showing C5200 > C5193 > C6749 > C5205. When treated with high temperature, high pressure, denaturant and reductant, the residual activities of trypsin inhibitor from the four bruchid-resistant mung beans were higher than those of control, and decreased with increasing temperature and pressure, and extending treatment time of denaturant and reductant. The effects of denaturant and reductant on the residual activity of trypsin inhibitor of bruchid-resistant mung beans showed a tendency of guanidine hydrochloride > ure, and TCEP > DTT > β-ME. Among the four bruchid-resistant mung beans, C5200 had the highest tolerance and C5193 had the moderate tolerance to high temperature, high pressure, denaturant and reductant stresses; C5205 had the lowest tolerance to high temperature, high pressure, denaturant stresses, while C6749 had the lowest tolerance to reductant treatment. We concluded that C5200 and C5193 have the highest residual activity of bruchid-resistant mung bean trypsin inhibitor under high temperature, high pressure, denaturant and reductant stresses, being of the higher value in its application.