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Fig. 8 | Biotechnology for Biofuels

Fig. 8

From: Improvement in catalytic activity and thermostability of a GH10 xylanase and its synergistic degradation of biomass with cellulase

Fig. 8

Conformational changes and interactions between wild-type XylE and its hybrid mutants after binding with xylopentaose. The figure shows the confirmations and interactions between xylopentaose and the amino acid residues in the substrate binding pocket of a, XylE-M3 (b), XylE-M6 (c), XylE-M9 (d), XylE-M3/M6 (e), XylE-M3/M9 (f), XylE-M6/M9 (g), and XylE-M3/M6/M9 (h). Catalytic residues are indicated in red; residues forming hydrogen bond interaction with the substrate are indicated in blue; xylopentaose is indicated in chromatic; and hydrogen bonds are represented by blue dashed lines

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