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《CHEMICAL RESEARCH IN CHINESE UNIVERSITIES》 2000-05
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Covalent Immobilization of Trypsin on Glycidyl Methacrylate-Modified Cellulose Membrane as Enzyme Reactor

JIANG Hong-Hai, ZOU Han-Fa, WANG Hai-Lin, NI Jian-Yi, ZHANG Qiang (National Chromatographic R & A Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116011, China)  
The membrane of the activated glycidyl methacrylate (GMA)-modified cellulose was prepared and packed into a column piece by piece to make a microreactor by immobilization of trypsin. The microreactor based on the membrane medium showed the advantages of being cheaper, mechanically strong and chemically stable. The activity of immobilized trypsin towards N-benzoyl-L-arginine ethyl ester(BAEE) was 17 800 U/g dry membrane, and was 52 % of that for free enzyme. Besides, the effects of pH value of buffer, temperature, ionic strength, organic modifier, and protein denaturants on the activity of immobilized trypsin were investigated in comparison to the free trypsin, and thermal stability also was found especially to be improved after immobilization. The activity of the immobilized trypsin showed no decay after continuously pumping BAEE through immobilized trypsin microreactor for 24 h at 40 ℃ and 0.5 mL/min. Finally, the cytochrome C was digested by microreactor and the products were analysed by MALDI-TOF-MS. The peptide mapping for a protein by combination of the immobilized enzyme membrane microreactor and MALDI-TOF-MS has been developed.
【Fund】: 国家自然科学重点基金!(批准号:29635010);; 国家杰出青年基金!(批准号:29725512)
【CateGory Index】: O629
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