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Fig. 7 | Microbial Cell Factories

Fig. 7

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

Fig. 7

Biophysical characterization of recombinant mature version serratiopeptidase. a Native PAGE loaded with 1 μg and 5 μg of recombinant mature version serratiopeptidase (SP1, SP2) and bovine serum albumin (BSA) as a marker (M1, M2) suggests the purified protein is monomeric. b Analytical HPLC of the recombinant mature form, when compared to the commercial version serratiopeptidase and other control proteins viz—lysozyme (14.4 KDa) and bovine serum albumin (66.4 KDa) shows the protein elutes at 7.5 min coinciding with the significant peak of commercial version serratiopeptidase. The elution profile of the recombinant version is identical to the commercial counterpart, except there are very less intensity minor peaks in comparison to the commercial version. It suggests the protein does not have or very fewer contaminants or degraded products, if any, in comparison to the commercial counterpart. Comparative c circular dichroism spectra (200–250 nm) and d intrinsic protein fluorescence spectra(300–450 nm) of recombinant version mature serratiopeptidase (solid line) and its commercial counterpart (dotted line) showing both versions have an almost identical conformational signature, and recombinant version may prove a better biosimilar for application purposes

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