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Fig. 1 | BMC Biotechnology

Fig. 1

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

Fig. 1

Comparison of the wild-type E. coli strain RV308 (WT) and mutant strains RV308(dsbArbs), RV308(dsbBrbs), and RV308(dsbArbsdsbBrbs) with regulated translation rate of components of the disulfide bond formation mechanism. 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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