Fig. 2. Catalytic properties of XacGH43_1.

a Capillary electrophoresis analysis showing the cleavage pattern of xylobiose, xylotriose, xylotetraose, xylopentaose, and xylohexaose. The reactions were interrupted at 0 min (dark yellow) or 30 min (blue). The standard patterns of xylose (X1), xylobiose (X2), xylotriose (X3), xylotetraose (X4), xylopentaose (X5), and xylohexaose (X6) are shown as gray curves. All data were normalized (starting from 4.5 min to omit APTS signal). b Influence of cations and chelating agents in XacGH43_1 activity and the enzyme response with increasing concentrations of CaCl₂ (inset). Results are expressed as mean  ± SD from three independent experiments. Data points are shown as empty symbols. In the bars plot, one-way ANOVA (P < 0.05) and tukey post hoc tests were performed for multiple comparisons (P < 0.001). Bars showing the same letters do not present significant statistical difference, according to tukey post hoc test. c Kinetics curves of XacGH43_1 activity on X2 (light pink) or X6 (dark pink) without the addition of CaCl₂ in the reaction. d Kinetics curves of XacGH43_1 activity on X2 (light blue) or X6 (dark blue) with the addition of 6 mM CaCl₂ in the reaction. The (c, d) curves were built based on mass spectrometric analysis of xylose release by the enzyme and data are expressed as mean ± SD from three independent experiments (V₀ = initial velocity; [E_T] = enzyme concentration). Data points are shown as empty symbols. Source data are provided as a source data file.