Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity.

Computational and Structural Biotechnology Journal
David Talens-PeralesJulio Polaina

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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Citations

Sep 7, 2021·World Journal of Microbiology & Biotechnology·Caio Cesar de Mello CapettiIgor Polikarpov

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Software Mentioned

Batch Entrez Tool
FIJI
Protein Blast
VADAR
ExPASy )
ClustalO MSA
Quiagen
Dendroscope
Phobius Tool
COOT

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