Scientists have analysed a new pectate lyase with chromatography in order to establish an alternative way to purify insoluble recombinant proteins.
Playing a crucial role in the "infection process of plant pathogens", pectate lyases (PEL) can also be used in commercially significant industrial applications.
The researchers, whose paper was published in BMC Biotechnology, highlight that producing a large-scale recombinant PEL could be a useful tool for the food industry.
Huizheng WangLi and FuXiuguo Zhang, who conducted the study, cloned a new PEL gene from Phytophthora capsici.
"The two different methods and comparison presented here would be highly valuable in obtaining an ideal enzyme for the downstream experiments and supply a useful alternative to purify some insoluble recombinant proteins," they conclude.
BMC Biotechnology is an open-access journal that publishes research articles.
These cover various biological disciplines, from manipulation of macromolecules to tissue engineering and pharmaceutical papers and are reviewed by peers and released as soon as possible afterwards.
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