Registro completo de metadatos
Campo DC Valor Lengua/Idioma
dc.provenanceCONICET-
dc.creatorGhio, Silvina-
dc.creatorInsani, Ester Marina-
dc.creatorPiccinni, Florencia Elizabeth-
dc.creatorTalia, Paola Monica-
dc.creatorGrasso, Daniel Horacio-
dc.creatorCampos, Eleonora-
dc.date2018-05-14T18:30:44Z-
dc.date2018-05-14T18:30:44Z-
dc.date2016-07-
dc.date2018-05-11T20:39:45Z-
dc.date.accessioned2019-04-29T15:30:29Z-
dc.date.available2019-04-29T15:30:29Z-
dc.date.issued2016-07-
dc.identifierGhio, Silvina; Insani, Ester Marina; Piccinni, Florencia Elizabeth; Talia, Paola Monica; Grasso, Daniel Horacio; et al.; GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass; Elsevier Gmbh; Microbiological Research; 186-187; 7-2016; 16-26-
dc.identifier0944-5013-
dc.identifierhttp://hdl.handle.net/11336/45118-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/295376-
dc.descriptionA 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.descriptionFil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Suelos; Argentina-
dc.descriptionFil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina-
dc.descriptionFil: Piccinni, Florencia Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina-
dc.descriptionFil: Talia, Paola Monica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina-
dc.descriptionFil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Suelos; Argentina-
dc.descriptionFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherElsevier Gmbh-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.micres.2016.02.006-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0944501316300118-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/45118-
dc.subjectPAENIBACILLUS-
dc.subjectXYLANASE-
dc.subjectGH10-
dc.subjectSLH DOMAIN-
dc.subjectLIGNOCELLULOSIC BIOMASS-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleGH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: CONICET

Ficheros en este ítem:
No hay ficheros asociados a este ítem.