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Fig. 6 | Microbial Cell Factories

Fig. 6

From: Extracellular production of the engineered thermostable protease pernisine from Aeropyrum pernix K1 in Streptomyces rimosus

Fig. 6

a Far-UV circular dichroism spectra of the codon-optimised recombinant propernisine (black line; plasmid construct pVFPER3) and pernisine (grey line; plasmid construct pVFPER5) from S. rimosus, and pernisine from A. pernix (dashed line). The spectra of the purified proteins (0.2 mg/mL) were measured at pH 8.0 (10 mM Tris/HCl) at 25 °C. b Simultaneous influence of temperature and pH on the activity of the codon-optimised recombinant pernisine (plasmid construct pVFPER5). Data are means for the relative proteolytic activities from experiments carried out in triplicate, as a function of temperature and corrected for pH. Colour bars: relative activities. c Time-courses for the temperature stabilities (as indicated) of the proteolytic activities for codon-optimised purified recombinant pernisine (from plasmid construct pVFPER5) produced by S. rimosus (black squares, grey circles, dark grey triangles) and wild-type pernisine (dashed line, inverted triangles)

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