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Fig. 2 | AMB Express

Fig. 2

From: Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete

Fig. 2

Effects of pH and temperature on the activity and stability of Il-DyP4 and Il-MnP6. And Il-DyP4 and Il-MnP6 activities at the beginning were considered to be 100%. Deviation values are standard deviations based on triplicate determinations. a The pH optimum of Il-DyP4 and Il-MnP6. The Il-DyP4 and Il-MnP6 activities were determined in the citrate–phosphate buffer, pH (2.2–8.0) and Tris–HCl buffer (pH 8.5) at 25 °C, respectively. b The pH stability of Il-DyP4 and Il-MnP6. Il-DyP4 and Il-MnP6 was incubated for 12 h at 25 °C in various pH values in citrate–phosphate (2.2–8.0) or Tris–HCl buffer (9.0). The residual activity of Il-DyP4 and Il-MnP6 was measured according to their enzyme activity assay. c The temperature optimum of Il-DyP4 and Il-MnP6. The enzyme reaction of Il-DyP4 was performed in 0.1 M sodium tartrate buffer, pH 3.5 at 0–60 °C. The enzyme reaction of Il-MnP6 was performed in 0.11 M sodium lactate buffer, pH 4.5 at 0–85 °C. d The temperature stability of Il-DyP4 and Il-MnP6. Il-DyP4 and Il-MnP6 were incubated for 12 h at 4–65 °C. The residual activity of Il-DyP4 and Il-MnP6 was measured according to their enzyme activity assay

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