ArticleBioresources and bioprocessing2022
Characterization of a novel GH10 alkali-thermostable xylanase from a termite microbiome.
Article in Bioresources and bioprocessing, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Molecular cloning and characterization of a GH10 thermophilic xylanase from hot spring and its potential application in promoting probiotic growth.BMC biotechnology · 2026Article
- Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse.Applied microbiology and biotechnology · 2025Article
- Characterization of thermophilic xylanases from Tengchong Qiaoquan hot spring for lignocellulose bioprocessing and prebiotic production.Frontiers in microbiology · 2025Article
- Heterologous expression and structure prediction of a xylanase identified from a compost metagenomic library.Applied microbiology and biotechnology · 2024Article
- Precision enzyme discovery through targeted mining of metagenomic data.Natural products and bioprospecting · 2024Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The aim of the present study was to assess the biochemical and molecular structural characteristics of a novel alkali-thermostable GH10 xylanase (Xyl10B) identified in a termite gut microbiome by a shotgun metagenomic approach. This endoxylanase candidate was amplified, cloned, heterologously expressed in Escherichia coli and purified. The recombinant enzyme was active at a broad range of temperatures (37-60 ºC) and pH values (4-10), with optimal activity at 50 ºC and pH 9. Moreover, its activity remained at more than 80% of its maximum at 50 °C for 8 h. In addition, Xyl10B was found to be stable in the presence of salt and several ions and chemical reagents frequently used in the industry. These characteristics make this enzyme an interesting candidate for pulp and paper bleaching industries, since this process requires enzymes without cellulase activity and resistant to high temperatures and alkaline pH (thermo-alkaliphilic enzymes). The products of xylan hydrolysis by Xyl10B (short xylooligosaccharides, xylose and xylobiose) could be suitable for application as prebiotics and in the production of bioethanol.
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Registered trials
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