We carried out a comprehensive bioinformatics study of the GH10 family searching for enzymes able to replace the use of highly pollutant chemicals in the pulp and paper industry, . 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.
Ref.: "Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity". D.Talens-Perales, E. Jiménez-Ortega, P. Sánchez-Torres, J.Sanz-Aparicio, J. Polaina. RSC Advances, 19, 2676-2686 (2021) https://doi.org/10.1016/j.csbj.2021.05.004
