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Abstract
The cost-efficient degradation of xylan to fermentable sugars is of particular interest in second generation bioethanol production, feed, food, and pulp and paper industries. Multiple potentially secreted enzymes involved in polysaccharide deconstruction are encoded in the genome of Paenibacillus sp. A59, a xylanolytic soil bacterium, such as three endoxylanases, seven GH43 β-xylosidases, and two GH30 glucuronoxylanases. In secretome analysis of xylan [ver mas...]
dc.contributor.authorGhio, Silvina
dc.contributor.authorOntañon, Ornella Mailén
dc.contributor.authorPiccinni, Florencia Elizabeth
dc.contributor.authorMarrero Diaz De Vill, Rubén
dc.contributor.authorTalia, Paola Mónica
dc.contributor.authorGrasso, Daniel Horacio
dc.contributor.authorCampos, Eleonora
dc.date.accessioned2018-07-30T13:42:37Z
dc.date.available2018-07-30T13:42:37Z
dc.date.issued2018-03
dc.identifier.issn1939-1234
dc.identifier.otherhttps://doi.org/10.1007/s12155-017-9887-7
dc.identifier.urihttp://hdl.handle.net/20.500.12123/2913
dc.identifier.urihttps://link.springer.com/article/10.1007%2Fs12155-017-9887-7
dc.description.abstractThe cost-efficient degradation of xylan to fermentable sugars is of particular interest in second generation bioethanol production, feed, food, and pulp and paper industries. Multiple potentially secreted enzymes involved in polysaccharide deconstruction are encoded in the genome of Paenibacillus sp. A59, a xylanolytic soil bacterium, such as three endoxylanases, seven GH43 β-xylosidases, and two GH30 glucuronoxylanases. In secretome analysis of xylan cultures, ten glycoside hydrolases were identified, including the three predicted endoxylanases, confirming their active role. The two uni-modular xylanases, a 32-KDa GH10 and a 20-KDa GH11, were recombinantly expressed and their activity on xylan was confirmed (106 and 85 IU/mg, respectively), with differences in their activity pattern. Both endoxylanases released mainly xylobiose (X2) and xylotriose (X3) from xylan and pre-treated biomasses (wheat straw, barley straw, and sweet corn cob), although only rGH10XynA released xylose (X1). rGH10XynA presented optimal conditions at pH 6, with thermal stability at 45–50 °C, while rGH11XynB showed activity in a wider range of pH, from 5 to 9, and was thermostable only at 45 °C. Moreover, GH11XynB presented sigmoidal kinetics on xylan, indicating possible cooperative binding, which was further supported by the structural model. This study provides a detailed analysis of the complete set of carbohydrate-active enzymes encoded in Paenibacillus sp. A59 genome and those effectively implicated in hemicellulose hydrolysis, contributing to understanding the mechanisms necessary for the bioconversion of this polysaccharide. Moreover, the two main free secreted xylanases, rGH10XynA and rGH11XynB, were fully characterized, supporting their potential application in industrial bioprocesses on lignocellulosic biomass.eng
dc.formatapplication/pdfeng
dc.language.isoeng
dc.publisherSpringer
dc.rightsinfo:eu-repo/semantics/restrictedAccesseng
dc.sourceBioEnergy research 11 (1) : 174–190. (March 2018)eng
dc.subjectPaenibacilluses_AR
dc.subjectBioconversiónes_AR
dc.subjectBiomasaes_AR
dc.subjectBiomasseng
dc.subjectBioconversioneng
dc.subject.otherEndoxylanaseses_AR
dc.subject.otherGH10es_AR
dc.subject.otherGH11es_AR
dc.titlePaenibacillus sp. A59 GH10 and GH11 extracellular endoxylanases: application in biomass bioconversioneng
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articleeng
dc.typeinfo:eu-repo/semantics/publishedVersioneng
dc.description.origenInstituto de Sueloses_AR
dc.description.filFil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentinaes_AR
dc.description.filFil: Ontañon, Ornella Mailén. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Marrero Diaz de Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentinaes_AR
dc.description.filFil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentinaes_AR
dc.description.filFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.subtypecientifico


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