Biochemical and Structural Characterization of a Highly Glucose-Tolerant β-Glucosidase from the Termite <i>Reticulitermes perilucifugus</i>.

ABSTRACT: The enzymatic hydrolysis of lignocellulose is often hindered by the glucose-mediated inhibition of β-glucosidases, a major bottleneck in industrial cellulose degradation. Identifying novel glucose-tolerant β-glucosidases is essential for enhancing saccharification efficiency. In this study, we cloned and heterologously expressed a novel β-glucosidase, RpBgl8, from the termite Reticulitermes perilucifugus in Escherichia coli. Sequence and structural analyses classified RpBgl8 as a glycoside hydrolase family 1 enzyme. The purified enzyme exhibited optimal activity at 45 °C and pH 7.0, with broad stability across pH 4.0-8.0. Notably, RpBgl8 demonstrated high tolerance to lignocellulose-derived inhibitors and organic solvents, maintaining 100% activity in 15% ethanol. Furthermore

SUBMITTER: Mao G 

PROVIDER: S-EPMC11989107 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature