Characterization, thermostable mechanism, and molecular docking of a novel glucose-tolerant <i>β</i>-glucosidase/<i>β</i>-galactosidase from the GH1 family isolated from Rehai hot spring.

ABSTRACT:

Introduction

As a renewable alternative to fossil fuels, second-generation bioethanol production relies heavily on efficient lignocellulose conversion, with β-glucosidase playing a critical role.

Methods

This study focused on the β-glucosidase gene y50bg4 discovered in the Tengchong Rehai metagenome. The recombinant enzyme Y50Bg4 was obtained through PCR amplification, cloning, and expression. It was subsequently separated and purified using a Ni-NTA affinity chromatography column, and its enzymatic properties were analyzed.

Results

Enzymatic characterization revealed that Y50Bg4 efficiently hydrolyzes substrates like cellobiose, pNPGlc, and lactose. Y50Bg4 achieved optimal activity at 60°C and pH 6.0, maintaining 100% stability after 2 h of incub

SUBMITTER: Huang YY 

PROVIDER: S-EPMC12023779 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature