Structural and functional insights into β-glucosidase derived from Thermoproteus sp. AZ2

β-glucosidase (BGL) is a pivotal enzyme with broad implications across diverse industrial sectors, demonstrating robust proficiency in catalyzing glycosidic bond hydrolysis, particularly critical in lignocellulosic biomass conversion. This study explored the structural features and enzymatic activity of Thermoproteus sp. AZ2-derived BGL (TsBGL2). The optimum temperature and pH for TsBGL2 were 95 °C and 5.0, respectively. TsBGL2 exhibited strong thermal stability, retaining >95 % of its activity after incubation at 99 °C for 10 h. Three high-resolution crystal structures of TsBGL2 revealed a canonical (α/β)8-barrel catalytic domain and thermostabilization mechanism. Based on the structure of TsBGL2, Δ(473-495) TsBGL2 was constructed, revealing a significant decrease in thermal stability. Collectively, this study provides enzymatic properties and structural analyses of TsBGL2, laying the groundwork for further studies of β-glucosidase.