Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205

Autores
Linares Pastén, Javier A.; Hero, Johan Sebastian; Pisa, José Horacio; Teixeira, Cristina; Nyman, Margareta; Patrick Adlercreutz; Martinez, Maria Alejandra; Nordberg Karlsson, Eva
Año de publicación
2020
Idioma
español castellano
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Prevotella copri DSM18205 is a bacterium, classified under Bacteroidetes that can be found in the human gastrointestinal tract (GIT). The role of P. copri in the GIT is unclear, and elevated numbers of the microbe have been reported both in dietary fiber-induced improvement in glucose metabolism but also in conjunction with certain inflammatory conditions. These findings raised our interest in investigating the possibility of P. copri to grow on xylan, and identify the enzyme systems playing a role in digestion of xylan-based dietary fibers in P. copri, which currently are unexplored. Two xylan degrading polysaccharide utilizing loci (PUL10 and 15) were found in the genome, with three and eight GH-encoding genes, respectively. Three of the eight gene products were successfully produced in Escherichia coli: One monomeric two-domain extracellular enzyme from GH43 (subfamily 12, in PUL10, 60 kDa) and two dimeric single module enzymes from PUL15, one extracellular GH10 (41 kDa), and one intracellular GH43 subfamily 1 enzyme (37 kDa). The GH43_12 enzyme was hydrolysing arabinofuranose residues from different substrates, and a model of the 3D-structure revealed a single arabinose binding pocket. The GH10 (1) and GH43_1 are cleaving the xylan backbone. Hydrolysis products of GH10 (1) were DP2-4, and seven subsites (−3 to +4) were predicted in the 3D-model of the GH10 active site. GH43_1 mainly produced xylose (in line with its intracellular location). Based on our results we propose that in PUL15, GH10 (1) is an extracellular endo-1,4-β-xylanase, that hydrolyses mainly glucuronosylated xylan polymers to xylooligosaccharides (XOS); while, GH43_1 in the same PUL, is an intracellular β-xylosidase, catalysing complete hydrolysis of the XOS to xylose. In PUL10, the characterized GH43_12 is an arabinofuranosidase, with a role in degradation of arabinoxylan, catalysing removal of arabinose-residues on xylan polymers.
Fil: Linares Pastén, Javier A.. Lund University. Biotechnology Department; Suecia
Fil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Pisa, José Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Teixeira, Cristina. Lund University. Biotechnology Department; Suecia
Fil: Nyman, Margareta. Department Food Technology, Engineering And Nutrition; Suecia
Fil: Patrick Adlercreutz. Lund University. Biotechnology Department; Suecia
Fil: Martinez, Maria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Universidad Nacional de Tucumán. Facultad de Ciencias Exactas y Tecnología; Argentina
Fil: Nordberg Karlsson, Eva. Lund University. Biotechnology Department; Suecia
Materia
POLYSACCHARIDE UTILIZING LOCI
PREVOTELLA COPRI
XYLANASE
XYLOSIDASE
ARABINOFURANOSIDASE
GH43
GH10
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/126795
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/126795
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205Linares Pastén, Javier A.Hero, Johan SebastianPisa, José HoracioTeixeira, CristinaNyman, MargaretaPatrick AdlercreutzMartinez, Maria AlejandraNordberg Karlsson, EvaPOLYSACCHARIDE UTILIZING LOCIPREVOTELLA COPRIXYLANASEXYLOSIDASEARABINOFURANOSIDASEGH43GH10https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Prevotella copri DSM18205 is a bacterium, classified under Bacteroidetes that can be found in the human gastrointestinal tract (GIT). The role of P. copri in the GIT is unclear, and elevated numbers of the microbe have been reported both in dietary fiber-induced improvement in glucose metabolism but also in conjunction with certain inflammatory conditions. These findings raised our interest in investigating the possibility of P. copri to grow on xylan, and identify the enzyme systems playing a role in digestion of xylan-based dietary fibers in P. copri, which currently are unexplored. Two xylan degrading polysaccharide utilizing loci (PUL10 and 15) were found in the genome, with three and eight GH-encoding genes, respectively. Three of the eight gene products were successfully produced in Escherichia coli: One monomeric two-domain extracellular enzyme from GH43 (subfamily 12, in PUL10, 60 kDa) and two dimeric single module enzymes from PUL15, one extracellular GH10 (41 kDa), and one intracellular GH43 subfamily 1 enzyme (37 kDa). The GH43_12 enzyme was hydrolysing arabinofuranose residues from different substrates, and a model of the 3D-structure revealed a single arabinose binding pocket. The GH10 (1) and GH43_1 are cleaving the xylan backbone. Hydrolysis products of GH10 (1) were DP2-4, and seven subsites (−3 to +4) were predicted in the 3D-model of the GH10 active site. GH43_1 mainly produced xylose (in line with its intracellular location). Based on our results we propose that in PUL15, GH10 (1) is an extracellular endo-1,4-β-xylanase, that hydrolyses mainly glucuronosylated xylan polymers to xylooligosaccharides (XOS); while, GH43_1 in the same PUL, is an intracellular β-xylosidase, catalysing complete hydrolysis of the XOS to xylose. In PUL10, the characterized GH43_12 is an arabinofuranosidase, with a role in degradation of arabinoxylan, catalysing removal of arabinose-residues on xylan polymers.Fil: Linares Pastén, Javier A.. Lund University. Biotechnology Department; SueciaFil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Pisa, José Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Teixeira, Cristina. Lund University. Biotechnology Department; SueciaFil: Nyman, Margareta. Department Food Technology, Engineering And Nutrition; SueciaFil: Patrick Adlercreutz. Lund University. Biotechnology Department; SueciaFil: Martinez, Maria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Universidad Nacional de Tucumán. Facultad de Ciencias Exactas y Tecnología; ArgentinaFil: Nordberg Karlsson, Eva. Lund University. Biotechnology Department; SueciaCold Spring Harbor Laboratory Press2020-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/126795Linares Pastén, Javier A.; Hero, Johan Sebastian; Pisa, José Horacio; Teixeira, Cristina; Nyman, Margareta; et al.; Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205; Cold Spring Harbor Laboratory Press; bioRxiv; 12-20202692-8205CONICET DigitalCONICETspainfo:eu-repo/semantics/altIdentifier/doi/10.1101/2020.12.10.419226info:eu-repo/semantics/altIdentifier/url/https://www.biorxiv.org/content/10.1101/2020.12.10.419226v1info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:28:06Zoai:ri.conicet.gov.ar:11336/126795instacron: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:34982025-09-29 10:28:07.08CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
title Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
spellingShingle Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
Linares Pastén, Javier A.
POLYSACCHARIDE UTILIZING LOCI
PREVOTELLA COPRI
XYLANASE
XYLOSIDASE
ARABINOFURANOSIDASE
GH43
GH10
title_short Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
title_full Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
title_fullStr Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
title_full_unstemmed Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
title_sort Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205
dc.creator.none.fl_str_mv Linares Pastén, Javier A.
Hero, Johan Sebastian
Pisa, José Horacio
Teixeira, Cristina
Nyman, Margareta
Patrick Adlercreutz
Martinez, Maria Alejandra
Nordberg Karlsson, Eva
author Linares Pastén, Javier A.
author_facet Linares Pastén, Javier A.
Hero, Johan Sebastian
Pisa, José Horacio
Teixeira, Cristina
Nyman, Margareta
Patrick Adlercreutz
Martinez, Maria Alejandra
Nordberg Karlsson, Eva
author_role author
author2 Hero, Johan Sebastian
Pisa, José Horacio
Teixeira, Cristina
Nyman, Margareta
Patrick Adlercreutz
Martinez, Maria Alejandra
Nordberg Karlsson, Eva
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv POLYSACCHARIDE UTILIZING LOCI
PREVOTELLA COPRI
XYLANASE
XYLOSIDASE
ARABINOFURANOSIDASE
GH43
GH10
topic POLYSACCHARIDE UTILIZING LOCI
PREVOTELLA COPRI
XYLANASE
XYLOSIDASE
ARABINOFURANOSIDASE
GH43
GH10
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Prevotella copri DSM18205 is a bacterium, classified under Bacteroidetes that can be found in the human gastrointestinal tract (GIT). The role of P. copri in the GIT is unclear, and elevated numbers of the microbe have been reported both in dietary fiber-induced improvement in glucose metabolism but also in conjunction with certain inflammatory conditions. These findings raised our interest in investigating the possibility of P. copri to grow on xylan, and identify the enzyme systems playing a role in digestion of xylan-based dietary fibers in P. copri, which currently are unexplored. Two xylan degrading polysaccharide utilizing loci (PUL10 and 15) were found in the genome, with three and eight GH-encoding genes, respectively. Three of the eight gene products were successfully produced in Escherichia coli: One monomeric two-domain extracellular enzyme from GH43 (subfamily 12, in PUL10, 60 kDa) and two dimeric single module enzymes from PUL15, one extracellular GH10 (41 kDa), and one intracellular GH43 subfamily 1 enzyme (37 kDa). The GH43_12 enzyme was hydrolysing arabinofuranose residues from different substrates, and a model of the 3D-structure revealed a single arabinose binding pocket. The GH10 (1) and GH43_1 are cleaving the xylan backbone. Hydrolysis products of GH10 (1) were DP2-4, and seven subsites (−3 to +4) were predicted in the 3D-model of the GH10 active site. GH43_1 mainly produced xylose (in line with its intracellular location). Based on our results we propose that in PUL15, GH10 (1) is an extracellular endo-1,4-β-xylanase, that hydrolyses mainly glucuronosylated xylan polymers to xylooligosaccharides (XOS); while, GH43_1 in the same PUL, is an intracellular β-xylosidase, catalysing complete hydrolysis of the XOS to xylose. In PUL10, the characterized GH43_12 is an arabinofuranosidase, with a role in degradation of arabinoxylan, catalysing removal of arabinose-residues on xylan polymers.
Fil: Linares Pastén, Javier A.. Lund University. Biotechnology Department; Suecia
Fil: Hero, Johan Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Pisa, José Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Teixeira, Cristina. Lund University. Biotechnology Department; Suecia
Fil: Nyman, Margareta. Department Food Technology, Engineering And Nutrition; Suecia
Fil: Patrick Adlercreutz. Lund University. Biotechnology Department; Suecia
Fil: Martinez, Maria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Universidad Nacional de Tucumán. Facultad de Ciencias Exactas y Tecnología; Argentina
Fil: Nordberg Karlsson, Eva. Lund University. Biotechnology Department; Suecia
description Prevotella copri DSM18205 is a bacterium, classified under Bacteroidetes that can be found in the human gastrointestinal tract (GIT). The role of P. copri in the GIT is unclear, and elevated numbers of the microbe have been reported both in dietary fiber-induced improvement in glucose metabolism but also in conjunction with certain inflammatory conditions. These findings raised our interest in investigating the possibility of P. copri to grow on xylan, and identify the enzyme systems playing a role in digestion of xylan-based dietary fibers in P. copri, which currently are unexplored. Two xylan degrading polysaccharide utilizing loci (PUL10 and 15) were found in the genome, with three and eight GH-encoding genes, respectively. Three of the eight gene products were successfully produced in Escherichia coli: One monomeric two-domain extracellular enzyme from GH43 (subfamily 12, in PUL10, 60 kDa) and two dimeric single module enzymes from PUL15, one extracellular GH10 (41 kDa), and one intracellular GH43 subfamily 1 enzyme (37 kDa). The GH43_12 enzyme was hydrolysing arabinofuranose residues from different substrates, and a model of the 3D-structure revealed a single arabinose binding pocket. The GH10 (1) and GH43_1 are cleaving the xylan backbone. Hydrolysis products of GH10 (1) were DP2-4, and seven subsites (−3 to +4) were predicted in the 3D-model of the GH10 active site. GH43_1 mainly produced xylose (in line with its intracellular location). Based on our results we propose that in PUL15, GH10 (1) is an extracellular endo-1,4-β-xylanase, that hydrolyses mainly glucuronosylated xylan polymers to xylooligosaccharides (XOS); while, GH43_1 in the same PUL, is an intracellular β-xylosidase, catalysing complete hydrolysis of the XOS to xylose. In PUL10, the characterized GH43_12 is an arabinofuranosidase, with a role in degradation of arabinoxylan, catalysing removal of arabinose-residues on xylan polymers.
publishDate 2020
dc.date.none.fl_str_mv 2020-12
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/11336/126795
Linares Pastén, Javier A.; Hero, Johan Sebastian; Pisa, José Horacio; Teixeira, Cristina; Nyman, Margareta; et al.; Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205; Cold Spring Harbor Laboratory Press; bioRxiv; 12-2020
2692-8205
CONICET Digital
CONICET
url http://hdl.handle.net/11336/126795
identifier_str_mv Linares Pastén, Javier A.; Hero, Johan Sebastian; Pisa, José Horacio; Teixeira, Cristina; Nyman, Margareta; et al.; Novel xylan degrading enzymes from polysaccharide utilizing loci of Prevotella copri DSM18205; Cold Spring Harbor Laboratory Press; bioRxiv; 12-2020
2692-8205
CONICET Digital
CONICET
dc.language.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1101/2020.12.10.419226
info:eu-repo/semantics/altIdentifier/url/https://www.biorxiv.org/content/10.1101/2020.12.10.419226v1
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cold Spring Harbor Laboratory Press
publisher.none.fl_str_mv Cold Spring Harbor Laboratory Press
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
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