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抗豆象绿豆胰蛋白酶抑制剂活性及理化性质
引用本文:樊艳平,张耀文,赵雪英,张仙红.抗豆象绿豆胰蛋白酶抑制剂活性及理化性质[J].作物学报,2017,43(11):1696-1704.
作者姓名:樊艳平  张耀文  赵雪英  张仙红
作者单位:1山西农业大学农学院,山西太谷030801; 2山西省农业科学园作物科学研究所,山西太原030000
基金项目:本研究由国家现代农业产业技术体系建设专项(GARS-08-G11)资助。
摘    要: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。

关 键 词:抗豆象绿豆  胰蛋白酶抑制剂  活性  温度  pH  超声波
收稿时间:2016-12-18

Activity and Physico Chemical Properties of Trypsin Inhibitor in Bruchid-Resistant Mung Bean
FAN Yan-Ping,ZHANG Yao-Wen,ZHAO Xue-Ying,ZHANG Xian-Hong.Activity and Physico Chemical Properties of Trypsin Inhibitor in Bruchid-Resistant Mung Bean[J].Acta Agronomica Sinica,2017,43(11):1696-1704.
Authors:FAN Yan-Ping  ZHANG Yao-Wen  ZHAO Xue-Ying  ZHANG Xian-Hong
Institution:1.College of Agriculture, Shanxi Agricultural University, Taigu 030801, China;2.Institute of Crop Science, Shanxi Academy of Agricultural Sciences, Taiyuan 030000, China
Abstract:Taking bruchid-resistant mung bean lines including B18, B20, B24, and A22 as experimental materials, a susceptible variety mung bean Jinlyu 1 as control, the activity of trypsin inhibitor and the stability of mung bean trypsin inhibitor under high temperature, pH and ultrasonic were measured. The trypsin inhibitor activities of four bruchid-resistant mung bean lines were significantly higher than those of control (Jinlyu 1). There were significant differences of trypsin inhibitor activity between four bruchid-resistant mung bean lines and the control at the 1% probability level. Among them, B18 had the highest activity (70.2 TI U g–1), following by B20 and A22, and B24 had the lowest one (55.2 TI U g–1). When treated with temperature, pH and amplitude of ultrasonic, the residual activities of trypsin inhibitor from the four bruchid-resistant mung bean lines were higher than those of control. The residual activities decreased with the increase of temperature and time of warm bath, which enhanced initially and then weakened when pH value was elevating between 2–12, with the highest when pH ranged from six to eight. The residual activities also reduced with the increasing ultrasonic intensity and treatment time. Among the four tested lines, B18 had the highest tolerance to high temperature, high acid and alkali stress, and ultrasonic intensity; B20 had the moderate tolerance, B24 had the lowest tolerance to high temperature, acid and alkali stress, while A22 had the lowest tolerance to ultrasonic treatment. We concluded that among four lines, B18 and B20 have the highest residual activity of bruchid-resistant mung bean trypsin inhibitor under temperature, pH and ultrasonic treatments, being of higher value of its application.
Keywords:Bruchid-resistant mung bean  Trypsin inhibitor  Activity  Temperature  pH  Ultrasonic
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