Fig. 1: Peroxidase activity of KlebCP on a small molecule substrate. | Nature Communications

Fig. 1: Peroxidase activity of KlebCP on a small molecule substrate.

From: Revisiting the activity of two poly(vinyl chloride)- and polyethylene-degrading enzymes

Fig. 1

The figure shows the formation of resorufin resulting from H2O2-dependent oxidation of 100 µM Amplex Red by 0.1 μM KlebCP. The reactions were conducted at 30 °C in 50 mM Tris-HCl buffer, pH 8.0, containing 300 mM NaCl. Note that H2O2 was introduced to the reaction mixtures 3 times at 0, 2 and 4 min of the experiment (each time to 100 µM final concentration). Also note that the 100 µM Amplex Red was not consumed after two additions of 100 µM H2O2, whereas the added H2O2 is fully depleted; this shows that a considerable fraction of the added H2O2 is removed by the catalase activity of KlebCP. Progress curves represent the average result of three independent experiments (n = 3), whereas error envelopes indicate standard deviation between replicates. Source data are provided as a Source Data file.

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