![]() ![]() In addition, some other characteristics of the purified PCPEL2 differed from the two systems, such as crystallographic features. The purity, specific activity and pathogenicity of the purified PCPEL2 expressed by the pMAL system were higher than the purified PCPEL2 expressed by the pET system. The expressed products were purified using affinity chromatography and gel filtration chromatography. Pcpel2 was constructed by pET system and pMAL system, and both constructs were used to express the PCPEL2 in Escherichia coli BL21 (DE3 pLysS. Results We cloned a new pectate lyase gene (Pcpel2 from Phytophthora capsici. The production of a large-scale soluble recombinant PEL would allow not only a more detailed structural and functional characterization of this enzyme but also may have important applications in the food industry. Most of the PELs were expressed as soluble recombinant proteins, while a few recombinant proteins were insoluble. Comparison of expression, purification and characterization of a new pectate lyase from Phytophthora capsici using two different methodsĭirectory of Open Access Journals (Sweden)įull Text Available Abstract Background Pectate lyases (PELs play an important role in the infection process of plant pathogens and also have a commercial significance in industrial applications. ![]()
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