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- W2049875125 abstract "Thermophilic xylanases are of great interest for their wide industrial application prospects. Here we identified a thermophilic xylanase (XynC01) of glycoside hydrolase (GH) family 10 in a thermophilic fungal strain Achaetomium sp. Xz-8. The deduced amino acids of XynC01 showed the highest identity of ≤52% to experimentally verified xylanases. XynC01 was functionally expressed in Pichia pastoris, showed optimal activity at pH 5.5 and 75 °C with stability over a broad pH range (pH 4.0–10.0) and at temperatures of 55 °C and below. XynC01 had the highest catalytic efficiency (kcat/Km, 3710 mL/s/mg) ever reported for all GH 10 xylanases, and was resistant to all tested metal ions and chemical reagents. Its hydrolysis products of various xylans were simple, mainly consisting of xylobiose and xylose. Under simulated mashing conditions, XynC01 alone had a comparable effect on filtration improvement with Ultraflo from Novozymes (20.24% vs. 20.71%), and showed better performance when combined with a commercial β-glucanase (38.50%). Combining all excellent properties described above, XynC01 may find diverse applications in industrial fields, especially in the brewing industry." @default.
- W2049875125 created "2016-06-24" @default.
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- W2049875125 date "2013-12-01" @default.
- W2049875125 modified "2023-10-16" @default.
- W2049875125 title "A novel thermophilic xylanase from Achaetomium sp. Xz-8 with high catalytic efficiency and application potentials in the brewing and other industries" @default.
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- W2049875125 doi "https://doi.org/10.1016/j.procbio.2013.08.020" @default.
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