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Artículo

Paenibacillus sp. A59 GH10 and GH11 Extracellular Endoxylanases: Application in Biomass Bioconversion

Ghio, Silvina; Ontañon, Ornella MailénIcon ; Piccinni, Florencia ElizabethIcon ; Marrero Díaz de Villegas, Rubén; Talia, Paola MonicaIcon ; Grasso, Daniel HectorIcon ; Campos, EleonoraIcon
Fecha de publicación: 12/2017
Editorial: Springer New York LLC
Revista: BioEnergy Research
ISSN: 1939-1242
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Agricultura

Resumen

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 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.
Palabras clave: Endoxylanases , Gh10 , Gh11 , Paenibacillus , Pre-Treated Biomass
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/41389
DOI: https://dx.doi.org/10.1007/s12155-017-9887-7
URL: https://link.springer.com/article/10.1007%2Fs12155-017-9887-7
Colecciones
Articulos(SEDE CENTRAL)
Articulos de SEDE CENTRAL
Citación
Ghio, Silvina; Ontañon, Ornella Mailén; Piccinni, Florencia Elizabeth; Marrero Díaz de Villegas, Rubén; Talia, Paola Monica; et al.; Paenibacillus sp. A59 GH10 and GH11 Extracellular Endoxylanases: Application in Biomass Bioconversion; Springer New York LLC; BioEnergy Research; 11; 1; 12-2017; 174-190
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