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Resumen
A novel bacterial isolate with polysaccharides degrading activity was identified as Paenibacillus sp., andnamed Paenibacillus sp. A59. Even though it is a strict mesophile, optimal xylanase activity of the crudeenzymatic extract was achieved between 50◦C and 70◦C and more than 60% of the activity was retainedafter incubation for 48 h at 50◦C, indicating thermotolerance of the enzymes involved. The extract wasalso active on pre-treated sugarcane residue [ver mas...]
dc.contributor.authorGhio, Silvina
dc.contributor.authorInsani, Ester Marina
dc.contributor.authorPiccinni, Florencia Elizabeth
dc.contributor.authorTalia, Paola Mónica
dc.contributor.authorGrasso, Daniel Horacio
dc.contributor.authorCampos, Eleonora
dc.date.accessioned2017-08-16T17:23:17Z
dc.date.available2017-08-16T17:23:17Z
dc.date.issued2016
dc.identifier.issn0944-5013
dc.identifier.otherhttps://doi.org/10.1016/j.micres.2016.02.006
dc.identifier.urihttp://hdl.handle.net/20.500.12123/986
dc.identifier.urihttp://ac.els-cdn.com/S0944501316300118/1-s2.0-S0944501316300118-main.pdf?_tid=348f0e86-82aa-11e7-9bba-00000aacb35f&acdnat=1502905499_64c4849fafdb4ab7e009d25de2bf5e73
dc.description.abstractA novel bacterial isolate with polysaccharides degrading activity was identified as Paenibacillus sp., andnamed Paenibacillus sp. A59. Even though it is a strict mesophile, optimal xylanase activity of the crudeenzymatic extract was achieved between 50◦C and 70◦C and more than 60% of the activity was retainedafter incubation for 48 h at 50◦C, indicating thermotolerance of the enzymes involved. The extract wasalso active on pre-treated sugarcane residue (SCR) and wheat straw, releasing xylobiose and xylose asthe main products, therefore confirming its predominantly xylanolytic activity. By zymograms and massspectrometry of crude enzymatic extracts of xylan or SCR cultures, a 32 kDa GH10 beta- 1,4- endoxylanasewith xylanase and no CMCase activity was identified. We named this enzyme XynA and it was the onlyxylanase identified under both conditions assayed, suggesting that it is a good candidate for recombinantexpression and evaluation in hemicelluloses deconstruction applications. Also, a protein with two S-layerhomology domains (SLH) and a large uncharacterized C-terminal domain as well as an ABC substratebinding protein were identified in crude extracts of SCR cultures. We propose that Paenibacillus sp. A59uses a system similar to anaerobic and other Gram positive bacteria, with SLH-domain proteins anchoringpolysaccharide-degrading enzymes close to the membrane and the substrate binding protein assistingtranslocation of simple sugars to the cell interior.
dc.formatapplication/pdfeng
dc.language.isoeng
dc.rightsinfo:eu-repo/semantics/openAccesseng
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.sourceMicrobiological research 186–187 : 16-26. (May–June 2016)eng
dc.subjectBiomasa
dc.subjectBiomasseng
dc.subjectPaenibacillus
dc.subjectLignocelluloseeng
dc.subjectLignocelulosa
dc.subjectXilanos
dc.subjectXylanseng
dc.titleGH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomasseng
dc.typeinfo:eu-repo/semantics/articleeng
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersioneng
dc.rights.licenseCreative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.description.origenInst. de Biotecnología
dc.gic151913
dc.description.filFil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
dc.description.filFil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
dc.description.filFil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
dc.description.filFil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina
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; Argentina
dc.description.filFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
dc.subtypecientifico


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