title: [Purification and immobilization of the proteinase from mung bean burgeon inactivating soybean trypsin inhibitor].
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.
authors: College of Food Science and Bioengineering, South China University of Technology, Guangzhou 510641, China. chzhminaa@163.com
authors: Z
authors: Z
authors: Chen
authors: X Q
authors: XQ
authors: Yang
authors: M M
authors: MM
authors: Zhao
mesh_terms: D010450:Endopeptidases / Q000302:isolation & purification* / Q000494:pharmacology; D004800:Enzymes, Immobilized; D007887:Fabaceae / Q000201:enzymology*; D008970:Molecular Weight; D010940:Plant Proteins / Q000037:antagonists & inhibitors*; D010946:Plants, Medicinal; D013025:Glycine max; D014361:Trypsin Inhibitors; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
chemical_list: D004800:Enzymes, Immobilized; D010940:Plant Proteins; D014361:Trypsin Inhibitors; D000516:alpha-Amylases; D010450:Endopeptidases