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- W2378699985 abstract "The recombinant plasmid pBlueScript SK-ndh carrying nicotine dehydrogenase (NDH) gene was digested with restriction enzyme EcoRI and SpeI, and the desired DNA fragment was subcloned to prokaryotic express vector pET-17B to obtain PET-17B-ndh which was transformed into E. coli BL21(DE3)pLYS to produce highly-expressed engineering strain. Even without induction of IPTG, the engineering strain still produced soluble and active recombinant NDH whose yield was 25 times greater than that of wild strain A. nicotinovorans. NDH was purified 39.82 fold by ammonium sulfate precipitation, ion exchange chromatography, and gel filtration, and SDS-PAGE electrophoresis of the purified fraction mitigated a simple band. Results showed that the enzyme had the highest activity at pH7.0 and 40 ℃ with Km of 7.694×10-4 mol/L. Mn2+ and Co2+ activated the enzyme while Cu2+ inhibited it. The nicotine degradation conditions showed that prosthetic group or electron accepter were necessary for the transfer of H+ in reaction system and the enzyme catalyze reaction is an oxide reductive reaction system." @default.
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- W2378699985 date "2007-08-31" @default.
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- W2378699985 title "Research on prokaryotic expression and enzymatic properties of nicotine dehydrogenase genes" @default.
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