Additional file 1 of Exploring the synergy between fungal CE15 glucuronoyl esterases and xylanases for lignocellulose saccharification

Additional file 1. Exploring the synergy between fungal CE15 glucuronoyl esterases and xylanases for lignocellulose saccharification” includes Supplementary Figs. 1–3 and Supplementary Tables 1 and 2. Supplementary Fig. 1. IEF of AeGE15 and TlGE15. Lanes; Purified AeGE15 (1) and TlGE15 (3), and AeGE15 (2) and TlGE15 (4) after treatment with Endo H, standard protein markers with pI range 3.0–10.0 (M). Supplementary Fig. 2. Effect of temperature and pH on the activity of AeGE15 (A, C) and TlGE15 (B, D) on cinnamyl alcohol ester of D-glucuronic acid. All assays were carried out in duplicates. Supplementary Fig. 3. Structure-based sequence alignment of AeGE15, TlGE15, AfGE15 and CuGE15. Secondary structure elements are drawn as black arrows (β-sheets) and black spirals (α-helixes). The 310-helixes are labeled as “η”. Strict β-turns are rendered with TT letters. Blue frames indicate similarity across groups. Identical and similar residues are printed in white on a red background and in red on a white background, respectively. The conserved motifs that include catalytic amino acids are indicated by green lines and green triangles, respectively. The Lysine residue suggested to interact with the MeGlcA moiety and the “SGXGG” motif that forms the cavity for its accommodation are denoted by a yellow star and a yellow line, respectively. The conserved Tryptophan of TtGE15A is rendered with a red star. Green digits resemble disulfide bridges and grey stars indicate residues with alternate conformations. Supplementary Table 1. Identity values among the amino acid sequences of AeGE15 and TlGE15, compared to other mature GEs from different microorganisms. Supplementary Table 2. Different pretreatment methods of beechwood biomass and the compositional analysis of the derived samples. Data have been obtained from [25].