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Fig. 6 | Microbial Cell Factories

Fig. 6

From: Enhanced production of recombinant serratiopeptidase in Escherichia coli and its characterization as a potential biosimilar to native biotherapeutic counterpart

Fig. 6

Purification of recombinant mature serratiopeptidase and proteolytic activity assay. Representative SDS-PAGE gels showing a isolated inclusion body (IB) of recombinant version mature serratiopeptidase from 6 h grown induced culture of E. coli C43(DE3) cells harbouring the expression plasmid pMSrp, b refolded serratiopeptidase by rapid dilution in ice-cold refolding buffer (refolded srp lane) and protein profile after concentration (concentrated srp). The lane Flow through was loaded with filtrate collected during concentration using 30 kDa molecular weight cut-off during concentration. c Representative SDS-PAGE gel showing collected elution fractions (E1–E4) of purified refolded mature version recombinant serratiopeptidase by size exclusion chromatography. d Protease activity of purified mature recombinant serratiopeptidase (rMSrp) its commercially available wild counterpart (standard) was measured using azocasein as substrate. The obtained specific activity of each one is plotted in the form of bar graph with error bars representing the standard error calculated from three independent experiments

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