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OALib Journal期刊
ISSN: 2333-9721
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Purification and Immobilization of the Proteinase from Mung Bean Burgeon Inactivating Soybean Trypsin Inhibitor
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

Keywords: mung bean,proteinase,inactivate,soybean trypsin inhibitor,immobilize
绿豆,
,蛋白酶,,钝化,,大豆胰蛋白酶抑制剂,,固定化

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Abstract:

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.

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