GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass

Autores
Ghio, Silvina; Insani, Ester Marina; Piccinni, Florencia Elizabeth; Talia, Paola Monica; 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.
Fil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Suelos; Argentina
Fil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina
Fil: 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
Fil: 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
Fil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Suelos; Argentina
Fil: 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
Materia
Paenibacillus
Xylanase
Gh10
Slh Domain
Lignocellulosic Biomass
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/45118
Acceder
id CONICETDig_180a8c0e0ea861041c8a7bde90332259
oai_identifier_str oai:ri.conicet.gov.ar:11336/45118
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomassGhio, SilvinaInsani, Ester MarinaPiccinni, Florencia ElizabethTalia, Paola MonicaGrasso, Daniel HoracioCampos, EleonoraPaenibacillusXylanaseGh10Slh DomainLignocellulosic Biomasshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A 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.Fil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Suelos; ArgentinaFil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; ArgentinaFil: 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; ArgentinaFil: 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; ArgentinaFil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Suelos; ArgentinaFil: 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; ArgentinaElsevier Gmbh2016-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/45118Ghio, 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; 16-260944-5013CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.micres.2016.02.006info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0944501316300118info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:43:47Zoai:ri.conicet.gov.ar:11336/45118instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:43:47.607CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass
title GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass
spellingShingle GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass
Ghio, Silvina
Paenibacillus
Xylanase
Gh10
Slh Domain
Lignocellulosic Biomass
title_short GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass
title_full GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass
title_fullStr GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass
title_full_unstemmed GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass
title_sort GH10 XynA is the main xylanase identified in the crude enzymaticextract of Paenibacillus sp. A59 when grown on xylan orlignocellulosic biomass
dc.creator.none.fl_str_mv Ghio, Silvina
Insani, Ester Marina
Piccinni, Florencia Elizabeth
Talia, Paola Monica
Grasso, Daniel Horacio
Campos, Eleonora
author Ghio, Silvina
author_facet Ghio, Silvina
Insani, Ester Marina
Piccinni, Florencia Elizabeth
Talia, Paola Monica
Grasso, Daniel Horacio
Campos, Eleonora
author_role author
author2 Insani, Ester Marina
Piccinni, Florencia Elizabeth
Talia, Paola Monica
Grasso, Daniel Horacio
Campos, Eleonora
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Paenibacillus
Xylanase
Gh10
Slh Domain
Lignocellulosic Biomass
topic Paenibacillus
Xylanase
Gh10
Slh Domain
Lignocellulosic Biomass
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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.
Fil: Ghio, Silvina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Suelos; Argentina
Fil: Insani, Ester Marina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina
Fil: 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
Fil: 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
Fil: Grasso, Daniel Horacio. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Recursos Naturales. Instituto de Suelos; Argentina
Fil: 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
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 2016-07
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/11336/45118
Ghio, 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
0944-5013
CONICET Digital
CONICET
url http://hdl.handle.net/11336/45118
identifier_str_mv Ghio, 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
0944-5013
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.micres.2016.02.006
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0944501316300118
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Gmbh
publisher.none.fl_str_mv Elsevier Gmbh
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842268622894923776
score 13.13397

Publicaciones similares