以4个抗豆象绿豆品系B18、B20、B24和A22为试材,以感虫绿豆品种晋绿1号为对照,研究了不同绿豆中胰蛋白酶抑制剂活性及其在高温、酸碱及超声波下绿豆的胰蛋白酶抑制剂稳定性。结果表明,4个抗豆象绿豆品种胰蛋白酶抑制剂活性均显著高于对...以4个抗豆象绿豆品系B18、B20、B24和A22为试材,以感虫绿豆品种晋绿1号为对照,研究了不同绿豆中胰蛋白酶抑制剂活性及其在高温、酸碱及超声波下绿豆的胰蛋白酶抑制剂稳定性。结果表明,4个抗豆象绿豆品种胰蛋白酶抑制剂活性均显著高于对照感虫品种,且均与对照在0.01水平差异极显著,其中B18活性最高,高达70.2TI U g–1,B20和A22活性次之,B24活性最差,但仍高达55.2 TI U g–1。4个抗豆象绿豆品种在不同温度、不同p H和不同振幅超声波下,残余活性均比对照高,且残余活性均随温度升高、温浴时间延长而降低,p H在2~12之间,随p H值的升高,残余活性均呈现先升高后降低的趋势,且p H值为6~8之间残余活性最高,残余活性也随超声波辐射强度升高、时间延长而降低,且4个抗虫品种中B18的耐高温性、耐酸碱性和耐辐射性最强,B20次之,B24的耐高温性、耐酸碱性最差,A22耐辐射性最差,说明在不同温度、p H和超声波处理后,B18、B20是抗豆象绿豆胰蛋白酶抑制剂残余活性保存最高的2个品种,应用价值较大。展开更多
By 30%～60%s(NH\-4)\-2SO\-4 fractional precipitation,anion\|exchange chromatographs on DEAE\|Sepharose CL\|6B,gel filtration on Sephacryl S\|200 and anion\|exchange chromatographs on Waters AP\|1 column(Protein Tm \|P...By 30%～60%s(NH\-4)\-2SO\-4 fractional precipitation,anion\|exchange chromatographs on DEAE\|Sepharose CL\|6B,gel filtration on Sephacryl S\|200 and anion\|exchange chromatographs on Waters AP\|1 column(Protein Tm \|Pak DEAE 15HR),a proteinase which can inactivated STI was purified from mung bean( Phaseolus aureus )burgeon.It was stable at temperatures lower than 50℃ and pH7.5～8.5,and the K m and V max of the proteinase for STI was 769.2 α\|N\|benzoyl\|L\|arginine ethyl ester(BAEE)/mL and 115.3BAEE/min/mL respectively.The molecular weight of the proteinase was estimated to be 29.8kD by SDS\|PAGE.The proteinase immobilized by polyacrylamide was stable at temperatures lower than 60℃ and pH7.0～9.0,and the apparent K * m and V max * of the immobilized proteinase for STI was 1303.8(BAEE)/mL and 94.34(BAEE)/min/mL respectively.The half\|life of the immobilized proteinase was about 12 days at展开更多
文摘以4个抗豆象绿豆品系B18、B20、B24和A22为试材,以感虫绿豆品种晋绿1号为对照,研究了不同绿豆中胰蛋白酶抑制剂活性及其在高温、酸碱及超声波下绿豆的胰蛋白酶抑制剂稳定性。结果表明,4个抗豆象绿豆品种胰蛋白酶抑制剂活性均显著高于对照感虫品种,且均与对照在0.01水平差异极显著,其中B18活性最高,高达70.2TI U g–1,B20和A22活性次之,B24活性最差,但仍高达55.2 TI U g–1。4个抗豆象绿豆品种在不同温度、不同p H和不同振幅超声波下,残余活性均比对照高,且残余活性均随温度升高、温浴时间延长而降低,p H在2~12之间,随p H值的升高,残余活性均呈现先升高后降低的趋势,且p H值为6~8之间残余活性最高,残余活性也随超声波辐射强度升高、时间延长而降低,且4个抗虫品种中B18的耐高温性、耐酸碱性和耐辐射性最强,B20次之,B24的耐高温性、耐酸碱性最差,A22耐辐射性最差,说明在不同温度、p H和超声波处理后,B18、B20是抗豆象绿豆胰蛋白酶抑制剂残余活性保存最高的2个品种,应用价值较大。
文摘By 30%～60%s(NH\-4)\-2SO\-4 fractional precipitation,anion\|exchange chromatographs on DEAE\|Sepharose CL\|6B,gel filtration on Sephacryl S\|200 and anion\|exchange chromatographs on Waters AP\|1 column(Protein Tm \|Pak DEAE 15HR),a proteinase which can inactivated STI was purified from mung bean( Phaseolus aureus )burgeon.It was stable at temperatures lower than 50℃ and pH7.5～8.5,and the K m and V max of the proteinase for STI was 769.2 α\|N\|benzoyl\|L\|arginine ethyl ester(BAEE)/mL and 115.3BAEE/min/mL respectively.The molecular weight of the proteinase was estimated to be 29.8kD by SDS\|PAGE.The proteinase immobilized by polyacrylamide was stable at temperatures lower than 60℃ and pH7.0～9.0,and the apparent K * m and V max * of the immobilized proteinase for STI was 1303.8(BAEE)/mL and 94.34(BAEE)/min/mL respectively.The half\|life of the immobilized proteinase was about 12 days at
