GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass

Autores
Ghio, Silvina; Insani, Ester Marina; Piccinni, Florencia Elizabeth; Talia, Paola Mónica; Grasso, Daniel Horacio; Campos, Eleonora
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 (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.
Inst. de Biotecnología
Fil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina
Fil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fuente
Microbiological research 186–187 : 16-26. (May–June 2016)
Materia
Biomasa
Paenibacillus
Lignocelulosa
Xilanos
Biomass
Lignocellulose
Xylans
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/986
Acceder
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oai_identifier_str oai:localhost:20.500.12123/986
network_acronym_str INTADig
repository_id_str l
network_name_str INTA Digital (INTA)
spelling GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomassGhio, SilvinaInsani, Ester MarinaPiccinni, Florencia ElizabethTalia, Paola MónicaGrasso, Daniel HoracioCampos, EleonoraBiomasaPaenibacillusLignocelulosaXilanosBiomassLignocelluloseXylansA 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.Inst. de BiotecnologíaFil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; ArgentinaFil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina2017-08-16T17:23:17Z2017-08-16T17:23:17Z2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/986http://ac.els-cdn.com/S0944501316300118/1-s2.0-S0944501316300118-main.pdf?_tid=348f0e86-82aa-11e7-9bba-00000aacb35f&acdnat=1502905499_64c4849fafdb4ab7e009d25de2bf5e730944-5013https://doi.org/10.1016/j.micres.2016.02.006Microbiological research 186–187 : 16-26. (May–June 2016)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-09-29T13:44:09Zoai:localhost:20.500.12123/986instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-29 13:44:09.333INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
title GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
spellingShingle GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
Ghio, Silvina
Biomasa
Paenibacillus
Lignocelulosa
Xilanos
Biomass
Lignocellulose
Xylans
title_short GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
title_full GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
title_fullStr GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
title_full_unstemmed GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
title_sort GH10 XynA is the main xylanase identified in the crude enzymatic extract of Paenibacillus sp. A59 when grown on xylan or lignocellulosic biomass
dc.creator.none.fl_str_mv Ghio, Silvina
Insani, Ester Marina
Piccinni, Florencia Elizabeth
Talia, Paola Mónica
Grasso, Daniel Horacio
Campos, Eleonora
author Ghio, Silvina
author_facet Ghio, Silvina
Insani, Ester Marina
Piccinni, Florencia Elizabeth
Talia, Paola Mónica
Grasso, Daniel Horacio
Campos, Eleonora
author_role author
author2 Insani, Ester Marina
Piccinni, Florencia Elizabeth
Talia, Paola Mónica
Grasso, Daniel Horacio
Campos, Eleonora
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Biomasa
Paenibacillus
Lignocelulosa
Xilanos
Biomass
Lignocellulose
Xylans
topic Biomasa
Paenibacillus
Lignocelulosa
Xilanos
Biomass
Lignocellulose
Xylans
dc.description.none.fl_txt_mv 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 (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.
Inst. de Biotecnología
Fil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina
Fil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Suelos; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
description 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 (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.
publishDate 2016
dc.date.none.fl_str_mv 2016
2017-08-16T17:23:17Z
2017-08-16T17:23:17Z
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12123/986
http://ac.els-cdn.com/S0944501316300118/1-s2.0-S0944501316300118-main.pdf?_tid=348f0e86-82aa-11e7-9bba-00000aacb35f&acdnat=1502905499_64c4849fafdb4ab7e009d25de2bf5e73
0944-5013
https://doi.org/10.1016/j.micres.2016.02.006
url http://hdl.handle.net/20.500.12123/986
http://ac.els-cdn.com/S0944501316300118/1-s2.0-S0944501316300118-main.pdf?_tid=348f0e86-82aa-11e7-9bba-00000aacb35f&acdnat=1502905499_64c4849fafdb4ab7e009d25de2bf5e73
https://doi.org/10.1016/j.micres.2016.02.006
identifier_str_mv 0944-5013
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Microbiological research 186–187 : 16-26. (May–June 2016)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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