Purified AfAA9_B activity was analyzed as reported by Breslmayr et al. (2018) [80 (link)]. The assay consisted of a reaction mixture containing 1 mM 2,6-dimethoxyphenol (2,6-DMP) (Sigma–Aldrich, St. Louis, MO, USA), 100 μM H2O2, and recombinant purified AfAA9_B in 50 mM sodium phosphate buffer (pH 8.0). For the blank, the enzyme was denatured by incubation at 99 °C for 30 min before the reaction mixture was added. After 5 min at 30 °C, absorbance was read at 469 nm to calculate the LPMO peroxidase activity.
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