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               <dc:title>A glucuronoxylan-specific xylanase from a new Paenibacillus favisporus strain isolated from tropical soil of Brazil</dc:title>
               <dc:creator>Padilha, Itácio Q. M.</dc:creator>
               <dc:creator>Valenzuela Mayorga, Susana Valeria</dc:creator>
               <dc:creator>Grisi, Teresa</dc:creator>
               <dc:creator>Díaz Lucea, Pilar</dc:creator>
               <dc:creator>de Araújo, Demetrius</dc:creator>
               <dc:creator>Pastor Blasco, Francisco I. Javier</dc:creator>
               <dc:subject>Bacils</dc:subject>
               <dc:subject>Ecologia microbiana</dc:subject>
               <dc:subject>Enzims microbians</dc:subject>
               <dc:subject>Biopolímers</dc:subject>
               <dc:subject>Sòls</dc:subject>
               <dc:subject>Bacillus (Bacteria)</dc:subject>
               <dc:subject>Microbial ecology</dc:subject>
               <dc:subject>Microbial enzymes</dc:subject>
               <dc:subject>Biopolymers</dc:subject>
               <dc:subject>Soils</dc:subject>
               <dc:description>A new xylanolytic strain, Paenibacillus favisporus CC02-N2, was isolated from sugarcane plantation fi elds in Brazil. The strain had a xylan-degrading system with multiple enzymes, one of which, xylanase Xyn30A, was identifi ed and characterized. The enzyme is a single-domain xylanase belonging to family 30 of the glycosyl hydrolases (GH30). Xyn30A shows high activity on glucuronoxylans, with a Vmax of 267.2 U mg&lt;br>1, a Km of 4.0 mg/ml, and a kcat of 13,333 min&lt;br>1 on beechwood xylan, but it does not hydrolyze arabinoxylans. The three- dimensional structure of Xyn30A consists of a common (β/α)8 barrel linked to a side-chain-associated β-structure, similar to previously characterized GH30 xylanases. The hydrolysis products from glucuronoxylan were methylglucuronic-acid-substituted xylooligomers (acidic xylooligosaccharides). The enzyme bound to insoluble xylan but not to crystalline cellulose. Our results suggest a specifi c role for Xyn30A in xylan biodegradation in natural habitats. The enzyme is a good candidate for the production of tailored xylooligosaccharides for use in the food industry and in the biotechnological transformation of biomass. [Int Microbiol 2014; 17(3):175-184]</dc:description>
               <dc:date>2015-01-19T13:03:35Z</dc:date>
               <dc:date>2015-01-19T13:03:35Z</dc:date>
               <dc:date>2014</dc:date>
               <dc:date>2015-01-19T13:03:35Z</dc:date>
               <dc:type>info:eu-repo/semantics/article</dc:type>
               <dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
               <dc:relation>Reproducció del document publicat a: http://dx.doi.org/:10.2436/20.1501.01.220.</dc:relation>
               <dc:relation>International Microbiology, 2014, vol. 17, num. 3, p. 175-184</dc:relation>
               <dc:relation>http://dx.doi.org/10.2436/20.1501.01.220.</dc:relation>
               <dc:rights>cc-by-nc-sa (c) Spanish Society for Microbiology (SEM) and Viguera Editores SL, 2014</dc:rights>
               <dc:rights>http://creativecommons.org/licenses/by-nc-sa/3.0/es</dc:rights>
               <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
               <dc:publisher>Spanish Society for Microbiology (SEM) and Viguera Editores SL</dc:publisher>
               <dc:source>Articles publicats en revistes (Genètica, Microbiologia i Estadística)</dc:source>
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