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The thermostable pectinase gene TmPec isolated from Thermotoga maritima was introduced into the NdeI site of pRSET-B vector and expressed in its intact form in Escherichia coli BL21. The overexpressed intact form of pectinase (TmPecN protein) was partially purified by heat-denaturation procedure. TmPecN showed the highest activity between 85 and 95 o C, and at approximately pH 6.5. Enzyme activity was stably maintained at temperatures below 85 o C. In the presence of Ca 2+ , pectinase activity of TmPecN increased to 128.4% of normal level. In contrast, Ba 2+ , Zn 2+ , and Mn 2+ strongly inhibited TmPecN activity. We conclude that the biochemical properties of the intact form of TmPecN are comparable to those of the recombinant protein TmPec reported previously.

Characterization of the Intact Form of Thermotoga maritima Pectinase TmPecN Expressed in Escherichia coli