Cloning,expression and characterization of a novel thermostable maltogenic dextrinase from Bacillus sp.ht0620


Hong-Bin Zhang;Ming Wu;Xue-Qin Hu;


A maltogenic dextrinase gene mdeHT was cloned from Bacillus sp.ht0620.The nucleotide sequence of the mdeHT was 1761 bp in length and encodes a protein of 587 aa with a molecular mass of90 kDa.Herein,we reported on the biochemical properties of a new thermo-stable maltogenic dextrinase.The recombinant protein was purified efficiently by using one-step nickel affinity chromatography.The purified enzyme exhibited optimal activity for 0-CD hydrolysis at 65-70℃and pH 6.5.When the enzyme was separately incubated at 4℃,50℃and 70℃in the buffer up to 7 days,it retained above 60%of its original activity at all investigated temperatures for 5 days incubation.The recombinant enzyme activity was strongly inhibited by 1 mmol 1~(-1)of Cu~(2+),Co~(2+),Zn~(2+)and Fe~(2+),and activated by 1 mmol 1~(-1)Mn~(2+),Ca~(2+)and K~+.The enzyme activity was significantly inhibited by SDS and Tris at the final concentration of 10mmol 1~(_1).These results suggested that this was a new thermostable maltogenic dextrinase and provided a potential application to the industrial processes.


Maltogenic;;Dextrinase;;Expression;;Characterization;;Thermostable;;Bacillus sp.ht0620


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