ArticleComputational and structural biotechnology journal2021
Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Channel-Directed Enzymatic Depolymerization within a Metal-Organic Framework.ACS applied materials & interfaces · 2025Article
- Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse.Applied microbiology and biotechnology · 2025Article
- Embedding a feruloyl esterase active site into a thermophilic endoxylanase scaffold for the degradation of feruloylated xylans.Computational and structural biotechnology journal · 2025Article
- Fungal Laccases: Fundamentals, Engineering and Classification Update.Biomolecules · 2023Review
- Use of a Novel Extremophilic Xylanase for an Environmentally Friendly Industrial Bleaching of Kraft Pulps.International journal of molecular sciences · 2022Article
- Expression of an extremophilic xylanase in Nicotiana benthamiana and its use for the production of prebiotic xylooligosaccharides.Scientific reports · 2022Article
- A thermostable and CBM2-linked GH10 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- Engineering mesophilic GH11 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- Recent advances in the enzymatic production and applications of xylooligosaccharides.World journal of microbiology & biotechnology · 2021Review
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Authors and funding
5 authors.
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Abstract
Endoxylanases active under extreme conditions of temperature and alkalinity can replace the use of highly pollutant chemicals in the pulp and paper industry. Searching for enzymes with these properties, we carried out a comprehensive bioinformatics study of the GH10 family. The phylogenetic analysis allowed the construction of a radial cladogram in which protein sequences putatively ascribed as thermophilic and alkaliphilic appeared grouped in a well-defined region of the cladogram, designated TAK Cluster. One among five TAK sequences selected for experimental analysis (Xyn11) showed extraordinary xylanolytic activity under simultaneous conditions of high temperature (90 °C) and alkalinity (pH 10.5). Addition of a carbohydrate binding domain (CBM2) at the C-terminus of the protein sequence further improved the activity of the enzyme at high pH. Xyn11 structure, which has been solved at 1.8 Å resolution by X-ray crystallography, reveals an unusually high number of hydrophobic, ionic and hydrogen bond atomic interactions that could account for the enzyme's extremophilic nature.
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