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Fig. 2 | BMC Biotechnology

Fig. 2

From: Expression of a fungal manganese peroxidase in Escherichia coli: a comparison between the soluble and refolded enzymes

Fig. 2

Effect of pH and temperature on the activity and stability of refolded and soluble MnP. And MnP activity at the beginning was considered to be 100%. Deviation values are standard deviations based on triplicate determinations. a The pH optimum of refolded and soluble MnP. The MnP activity was determined in the citrate-phosphate buffer, pH 2.2-8.0 and Tris–HCl, pH 8.6-9.0, at 25 °C. b The pH stability of refolded and soluble MnP. Refolded and soluble MnP was incubated for 6 h at 25 °C in various pH vaules in citrate-phosphate (2.2-8.0) or Tris–HCl buffer (8.6-9.0). The residual MnP activity was measured according to the method of MnP activity assay. c The temperature optimum of refolded and soluble MnP. The enzyme reaction was performed in 0.11 M sodium lactate buffer, pH 4.5 at 10–75 °C. d The temperature stability of refolded and soluble MnP. Refolded and soluble MnP were incubated for 6 h at 15–65 °C. The residual MnP activity was measured according to the method of MnP activity assay

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