文章基本信息

标题：Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity
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作者：David Talens-Perales ; Elena Jiménez-Ortega ; Paloma Sánchez-Torres 等
期刊名称：Computational and Structural Biotechnology Journal
印刷版ISSN：2001-0370
出版年度：2021
卷号：19
页码：2676-2686
DOI：10.1016/j.csbj.2021.05.004
出版社：Computational and Structural Biotechnology Journal
摘要：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.
关键词：Crystal structure ; Glycoside hydrolase ; Pulp and paper ; Xylose ; Xylooligosaccharides