%0 Journal Article
%T Structural insights and functional characterization of a novel β-glucosidase derived from Thermotoga profunda.
%A Guo Y
%A Chen A
%A Liu K
%A Ji C
%J Biochem Biophys Res Commun
%V 732
%N 0
%D 2024 Nov 5
%M 39033552
%F 3.322
%R 10.1016/j.bbrc.2024.150405
%X β-Glucosidase is a crucial cellulase, as its activity determines the efficiency of cellulose hydrolysis into glucose. This study addresses the functional and structural characteristics of Thermotoga profunda β-glucosidase (Tp-BGL). Tp-BGL exhibited a Km of 0.3798 mM for p-nitrophenyl-β-d-glucopyranoside (pNPGlc) and 4.44 mM for cellobiose, with kcat/Km of 1211.16 and 4.18 s-1 mM-1, respectively. In addition, Tp-BGL showed significant pH adaptability and thermal stability, with a Tm of 85.7 °C and retaining >90 % of its activity after incubation at 80 °C for 90 min. The crystal structure of Tp-BGL was resolved at 1.95 Å resolution, and reveals a typical TIM barrel structure. Comparative structural analysis highlighted that the major distinction between Tp-BGL and the other glucosidases lies in their loop regions.