Abstract
Enzymatic degradation of vegetal biomass offers versatile procedures to improve the production of alternative fuels and other biomass-based products. Here we present the three-dimensional structure of a xylanase from Nectria haematococca (NhGH11) at 1.0 Å resolution and its functional properties. The atomic resolution structure provides details and insights about the complex hydrogen bonding network of the active site region and allowed a detailed comparison with homologous structures. Complementary biochemical studies showed that the xylanase can catalyze the hydrolysis of complex xylan into simple xylose aldopentose subunits of different lengths. NhGH11 can catalyze the efficient breakdown of beechwood xylan, xylan polysaccharide, and wheat arabinoxylan with turnover numbers of 1730.6 ± 318.1 min−1, 1648.2 ± 249.3 min−1 and 2410.8 ± 517.5 min−1 respectively. NhGH11 showed maximum catalytic activity at pH 6.0 and 45 °C. The mesophilic character of NhGH11 can be explained by distinct structural features in comparison to thermophilic GH11 enzymes, including the number of hydrogen bonds, side chain interactions and number of buried water molecules. The enzymatic activity of NhGH11 is not very sensitive to metal ions and chemical reagents that are typically present in associated industrial production processes. The data we present highlights the potential of NhGH11 to be applied in industrial biomass degradation processes.
Highlights
Enzymatic degradation of vegetal biomass offers versatile procedures to improve the production of alternative fuels and other biomass-based products
To overcome this and to obtain NhGH11 in amounts required for crystallization experiments and biochemical investigations, recombinant gene expression was performed by using a maltose-binding-protein (MBP) as fusion construct and to improve solubility[20]
The three-dimensional structure of NhGH11 has the typical fold of family 11 xylanases with a single catalytic domain and conserved active site residues
Summary
Enzymatic degradation of vegetal biomass offers versatile procedures to improve the production of alternative fuels and other biomass-based products. Agricultural wastes, especially sugar cane bagasse, can be treated with carbohydrate degrading enzymes to make them applicable for biofuel production[1,2]. In this context, research activities in the field of biofuel production are aiming at the potential of lignocellulosic material and carbohydrate degrading enzymes for bioethanol production. In combination with other carbohydrate degrading enzymes, xylanases are utilized in bio-refineries, chemical and pharmaceutical industries, processing of fruit juices and production of p rebiotics[3,4,5,6,7,8]. The acid/base residue E180 act as a base and deprotonates the neighboring nucleophilic water, which attacks the anomeric carbon of the α-glycosyl enzyme intermediate and allows the product formation with β-configuration[14]
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