绿豆中胰蛋白酶抑制子的纯化及部分性质的研究

Study on the Purification and Properties of Trypsin Inhibitor (TI) in Mungbean

摘要:

本文研究将绿豆经过粉碎、过筛和正己烷脱脂后，采用(NH4)2SO4分级沉淀、DEAE-Sepharose CL-6B离子交换、Sephacryl S-200凝胶过滤等方法，对其中的胰蛋白酶抑制因子进行了分离纯化。然后研究了所纯化出的胰蛋白酶抑制子的pH和温度稳定性，实验结果表明：在20~100 ℃的范围和pH 2.2~10.2范围内，胰蛋白酶抑制因子性质较稳定。

Abstract:

By (NH4)2SO4 fractional precipitation, DEAE-Sepharose CL-6B anion-exchange chromatographs and Sephacryl S-200 gel filtration, trypsin inhibitor(TI) was purified from degrease Mungbean powder. Then the stability of TI was studied. It was showed that the activity of TI was not obviously changed at temperature of 20~100 ℃ and with pH value of 2.2~10.2.