Characterization of thermophilic xylanases from Tengchong Qiaoquan hot spring for lignocellulose bioprocessing and prebiotic production.

ABSTRACT:

Introduction

Xylanases are key catalysts for valorizing lignocellulosic biomass, yet many available enzymes lack sufficient thermal stability and exhibit suboptimal activity on complex substrates. To address these limitations, we combined enrichment culturing with metagenomic analysis to discover and characterize two novel GH10 family xylanases, Tc15-Xyn6 and Tc15-Xyn10, from the Qiaoquan geothermal area in Tengchong, Yunnan Province.

Methods

Following molecular cloning, heterologous expression, and purification by Ni²⁺-chelating affinity chromatography, both enzymes were comprehensively profiled.

Results

Tc15-Xyn6 displayed optimal activity at 65 °C and pH 6.6 with a half-life of 2 h at 65 °C, while Tc15-Xyn10 exhibited optimal activity at 60 °C and pH 6.0

SUBMITTER: Li JL 

PROVIDER: S-EPMC12880817 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature