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.
