ArticleMolecular biology reports2026
A thermostable GH10 xylanase from Anoxybacteroides tepidamans: structural insights and biochemical characterization.
Article in Molecular biology reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundRenewable energy sources have gained importance due to environmental concerns and rising energy costs. Plant biomass is an abundant and eco-friendly resource, with xylan as a major hemicellulose component requiring xylanases for its degradation. Thermostable xylanases are valuable for their stability under harsh conditions. This study aimed to identify and characterize novel thermophilic xylanases for sustainable biotechnological applications. METHODS AND
resultsA novel glycoside hydrolase family 10 (GH10) endo-1,4-β-xylanase from the thermophilic bacterium Anoxybacteroides tepidamans was identified, cloned, overexpressed, and biochemically characterized. The 39.06 kDa protein showed the classical (α/β)
conclusionsThe thermophilic character of AtepXyn, together with its activity across a broad temperature and pH range and its high catalytic efficiency toward beechwood xylan, makes it a promising candidate for industrial applications in biomass conversion, biofuel production, and other biotechnological processes requiring robust xylan-degrading enzymes.
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