%0 Journal Article
%T Purification and Immobilization of the Proteinase from Mung Bean Burgeon Inactivating Soybean Trypsin Inhibitor<br>萌发绿豆中水解大豆胰蛋白酶抑制子蛋白酶的纯化及固定化
%A CHEN Zhong
%A YANG Xiao
%A |Quan
%A ZHAO Mou
%A |Ming
%A <br>陈中
%A 杨晓泉
%A 赵谋明
%J 生物工程学报
%D 2001
%I 
%X By 30%-60% s(NH4)2SO4 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(ProteinTm-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 degrees C and pH7.5-8.5, and the Km and Vmax of the proteinase for STI was 769.2 alpha-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 degrees C and pH7.0-9.0, and the apparent Km* and Vmax* 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 4 degrees C.
%K mung bean
%K proteinase
%K inactivate
%K soybean trypsin inhibitor
%K immobilize<br>绿豆，
%K 蛋白酶，
%K 钝化，
%K 大豆胰蛋白酶抑制剂，
%K 固定化
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=BA029F5BDB074F1A&yid=14E7EF987E4155E6&vid=BCA2697F357F2001&iid=0B39A22176CE99FB&sid=CC0ECB9C52F1B85F&eid=797D49279EA93BC4&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=11