**2.1 Enzyme and protein measurements**

The chitinase activity was assayed by determining the reducing sugars released from soluble chitin. The activity was assayed according to a previously paper [11].

The β-GlcNAcase activity was measured by determining the release of *p*-nitrophenol from *p*NP-GlcNAc. The enzyme activity required to form 1 μmol *p*-nitrophenol was regarded as one unit. The enzyme activity was measured according to a standard assay method. The reaction mixtures comprised 40 μL of 1 mM *p*NP-GlcNAc solution in 0.1 M acetate buffer (pH 6.0) and 20 μL of enzyme solution. After the reaction mixtures were incubated for 15 min at 37°C, the enzyme reaction was stopped by adding 200 μL of 0.5 M Na2CO3 solution.

The LPMO activity was measured by detecting the oxidized products released from chitin. Solutions of α or β-chitin (5 mg/mL), Pb-LPMO (1.0 mM), ascorbic acid (1.0 mM), and 20 mM acetate buffer (pH 5.0) were mixed to 1.0 mL volume. The reaction mixture was incubated at 37°C for 24 h. The oxidized products were then applied onto a TSK-gel Amide-80 column (4.6 × 250 mm, Tosoh Co., Tokyo, Japan) and eluted with 70% acetonitrile at a flow rate of 0.7 mL/min; the products were monitored by absorbance measurement at 210 nm.

Protein contents were assayed using Micro BCA protein assay kits (ThermoFisher Scientific) with bovine serum albumin as the standard. Protein concentrations of Pb-LPMO, Pb-ChiA, and Pb-GlcNAcase were calculated from absorbance measurement at 280 nm and the protein extinction coefficient according to the method of Gill and von Hippel [12].
