Xylanases are the main enzymes to hydrolyze xylan, the major hemicellulose found in lignocellulose. Xylanases also have a wide range of industrial applications. Therefore, the discovery of new xylanases has the potential to enhance efficiency and sustainability in many industries. Here, we report a xylanase with thermophilic character and superior biochemical properties for industrial use. The new xylanase is discovered in Anoxybacillus ayderensis as an intracellular xylanase (AAyXYN329) and recombinantly produced. While AAyXYN329 shows significant activity over a wide pH and temperature range, optimum activity conditions were determined as pH 6.5 and 65 °C. The half-life of the enzyme was calculated as 72 h at 65 °C. The enzyme did not lose activity between pH 6.0-9.0 at +4 °C for 75 days. Km, kcat and kcat/Km values of AAyXYN329 were calculated as 4.09824 ± 0.2245 µg/µL, 96.75 1/sec, and 23.61/L/g.s -1, respectively. In conclusion, the xylanase of A. ayderensis has an excellent potential to be utilized in many industrial processes.
Anoxybacillus , Bacterial Proteins , Endo-1,4-beta Xylanases , Enzyme Stability , Recombinant Proteins , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Recombinant Proteins/isolation & purification , Anoxybacillus/enzymology , Anoxybacillus/genetics , Endo-1,4-beta Xylanases/genetics , Endo-1,4-beta Xylanases/chemistry , Endo-1,4-beta Xylanases/metabolism , Bacterial Proteins/chemistry , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Hydrogen-Ion Concentration , Cloning, Molecular , Temperature , Escherichia coli/genetics , Xylans/metabolism , Xylans/chemistry , Substrate Specificity , Kinetics
