Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity
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...
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doaj-b0c986d4bc0c426aa47a834e51b500852021-05-12T04:10:18ZengElsevierComputational and Structural Biotechnology Journal2001-03702021-01-011926762686Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinityDavid Talens-Perales0Elena Jiménez-Ortega1Paloma Sánchez-Torres2Julia Sanz-Aparicio3Julio Polaina4Institute of Agrochemistry and Food Technology, Spanish National Research Council (CSIC), Paterna, Valencia, SpainInstitute of Physical-Chemistry Rocasolano, Spanish National Research Council (CSIC), Madrid, SpainInstitute of Agrochemistry and Food Technology, Spanish National Research Council (CSIC), Paterna, Valencia, SpainInstitute of Physical-Chemistry Rocasolano, Spanish National Research Council (CSIC), Madrid, Spain; Corresponding authors.Institute of Agrochemistry and Food Technology, Spanish National Research Council (CSIC), Paterna, Valencia, Spain; Corresponding authors.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.http://www.sciencedirect.com/science/article/pii/S2001037021001859Crystal structureGlycoside hydrolasePulp and paperXyloseXylooligosaccharides |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
David Talens-Perales Elena Jiménez-Ortega Paloma Sánchez-Torres Julia Sanz-Aparicio Julio Polaina |
spellingShingle |
David Talens-Perales Elena Jiménez-Ortega Paloma Sánchez-Torres Julia Sanz-Aparicio Julio Polaina Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity Computational and Structural Biotechnology Journal Crystal structure Glycoside hydrolase Pulp and paper Xylose Xylooligosaccharides |
author_facet |
David Talens-Perales Elena Jiménez-Ortega Paloma Sánchez-Torres Julia Sanz-Aparicio Julio Polaina |
author_sort |
David Talens-Perales |
title |
Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity |
title_short |
Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity |
title_full |
Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity |
title_fullStr |
Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity |
title_full_unstemmed |
Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity |
title_sort |
phylogenetic, functional and structural characterization of a gh10 xylanase active at extreme conditions of temperature and alkalinity |
publisher |
Elsevier |
series |
Computational and Structural Biotechnology Journal |
issn |
2001-0370 |
publishDate |
2021-01-01 |
description |
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. |
topic |
Crystal structure Glycoside hydrolase Pulp and paper Xylose Xylooligosaccharides |
url |
http://www.sciencedirect.com/science/article/pii/S2001037021001859 |
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