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Fig. 2 | BMC Biotechnology

Fig. 2

From: Translational regulation of periplasmic folding assistants and proteases as a valuable strategy to improve production of translocated recombinant proteins in Escherichia coli

Fig. 2

Comparison of the wild-type E. coli strain RV308 (WT) and mutant strains RV308(skprbs), RV308(sppArbs), and RV308(degPrbs) with regulated translation of Skp (folding chaperone), SppA (signal peptidase), and DegP (periplasmic protease). The panels show AP activity a and concentration of GM-CSF c under induced conditions and the corresponding growth curves: pSB-M1s b, pGM29ompA d. Following 2 h incubation, the XylS/Pm-mediated protein expression was induced (OD600 ~ 0.3–0.5) by adding m-toluic acid to a final concentration of 1 mM. The AP activity and GM-CSF concentration were measured in the periplasmic fraction of cells harvested 4 h (pGM29ompA) and 5 h (pSB-M1s) post induction. The data presented are the averages of three biological replica with the standard deviation indicated. The AP activity and GM-CSF concentration data were normalized against the total protein content measured in the periplasmic fraction

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