Characterization and structural analysis of the endo-1,4-β-xylanase GH11 from the hemicellulose-degrading Thermoanaerobacterium saccharolyticum useful for lignocellulose saccharification.

ABSTRACT: Xylanases are important for the enzymatic breakdown of lignocellulose-based biomass to produce biofuels and other value-added products. We report functional and structural analyses of TsaGH11, an endo-1,4-β-xylanase from the hemicellulose-degrading bacterium, Thermoanaerobacterium saccharolyticum. TsaGH11 was shown to be a thermophilic enzyme that favors acidic conditions with maximum activity at pH 5.0 and 70 °C. It decomposes xylans from beechwood and oat spelts to xylose-containing oligosaccharides with specific activities of 5622.0 and 3959.3 U mg^-1, respectively. The kinetic parameters, K_m and k_cat towards beechwood xylan, are 12.9 mg mL^-1 and 34,015.3 s^-1, respectively, resulting in k_cat/K_m value of 2658.7 m

SUBMITTER: Kim IJ 

PROVIDER: S-EPMC10576002 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature