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Characterization of the Intact Form of Thermotoga maritima Pectinase TmPecN Expressed in Escherichia coli
- Source :
- Journal of Applied Biological Chemistry. 58:97-100
- Publication Year :
- 2015
- Publisher :
- Korean Society for Applied Biological Chemistry, 2015.
-
Abstract
- 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.
Details
- ISSN :
- 22347941 and 19760442
- Volume :
- 58
- Database :
- OpenAIRE
- Journal :
- Journal of Applied Biological Chemistry
- Accession number :
- edsair.doi...........5f2a45d47e28ad1f8c73422947caae82