Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A

Autores
Garrido, Mercedes Maria; Piccinni, Florencia Elizabeth; Landoni, Malena; Peña, María Jesús; Topalian, Juliana; Couto, Alicia; Wirth, Sonia Alejandra; Urbanowicz, Breeanna Rae; Campos, Eleonora
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Valorization of the hemicellulose fraction of plant biomass is crucial for the sustainability of lignocellulosic biorefineries. The Cellulomonas genus comprises Gram-positive Actinobacteria that degrade cellulose and other polysaccharides by secreting a complex array of enzymes. In this work, we studied the specificity and synergy of two enzymes, CsXyn10A and CsAbf62A, which were identified as highly abundant in the extracellular proteome of Cellulomonas sp. B6 when grown on wheat bran. To explore their potential for bioprocessing, the recombinant enzymes were expressed and their activities were thoroughly characterized. rCsXyn10A is a GH10 endo-xylanase (EC 3.2.1.8), active across a broad pH range (5 to 9), at temperatures up to 55 °C. rCsAbf62A is an α-L-arabinofuranosidase (ABF) (EC 3.2.1.55) that specifically removes α-1,2 and α-1,3-L-arabinosyl substituents from arabino-xylo-oligosaccharides (AXOS), xylan, and arabinan backbones, but it cannot act on double-substituted residues. It also has activity on pNPA. No differences were observed regarding activity when CsAbf62A was expressed with its appended CBM13 module or only the catalytic domain. The amount of xylobiose released from either wheat arabinoxylan or arabino-xylo-oligosaccharides increased significantly when rCsXyn10A was supplemented with rCsAbf62A, indicating that the removal of arabinosyl residues by rCsAbf62A improved rCsXyn10A accessibility to β-1,4-xylose linkages, but no synergism was observed in the deconstruction of wheat bran. These results contribute to designing tailor-made, substrate-specific, enzymatic cocktails for xylan valorization.
Instituto de Biotecnología
Fil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Garrido, Mercedes Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Garrido, Mercedes Maria. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Piccinni, Florencia Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Piccinni, Florencia Elizabeth. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Landoni, Malena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigación en Hidratos de Carbono; Argentina
Fil: Landoni, Malena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Peña, María Jesús. University of Georgia. Complex Carbohydrate Research Center; Estados Unidos
Fil: Topalian, Juliana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Topalian, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Couto, Alicia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigación en Hidratos de Carbono; Argentina
Fil: Wirth, Sonia Alejandra. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Urbanowicz, Breeanna Rae. University of Georgia. Department of Biochemistry and Molecular Biology; Estados Unidos
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fuente
Applied Microbiology and Biotechnology (Published: 08 July 2022)
Materia
Hemicellulose
Xylans
Hemicelulosa
Cellulomonas
Xilanos
Nivel de accesibilidad
acceso restringido
Condiciones de uso
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/12415
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spelling Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62AGarrido, Mercedes MariaPiccinni, Florencia ElizabethLandoni, MalenaPeña, María JesúsTopalian, JulianaCouto, AliciaWirth, Sonia AlejandraUrbanowicz, Breeanna RaeCampos, EleonoraHemicelluloseXylansHemicelulosaCellulomonasXilanosValorization of the hemicellulose fraction of plant biomass is crucial for the sustainability of lignocellulosic biorefineries. The Cellulomonas genus comprises Gram-positive Actinobacteria that degrade cellulose and other polysaccharides by secreting a complex array of enzymes. In this work, we studied the specificity and synergy of two enzymes, CsXyn10A and CsAbf62A, which were identified as highly abundant in the extracellular proteome of Cellulomonas sp. B6 when grown on wheat bran. To explore their potential for bioprocessing, the recombinant enzymes were expressed and their activities were thoroughly characterized. rCsXyn10A is a GH10 endo-xylanase (EC 3.2.1.8), active across a broad pH range (5 to 9), at temperatures up to 55 °C. rCsAbf62A is an α-L-arabinofuranosidase (ABF) (EC 3.2.1.55) that specifically removes α-1,2 and α-1,3-L-arabinosyl substituents from arabino-xylo-oligosaccharides (AXOS), xylan, and arabinan backbones, but it cannot act on double-substituted residues. It also has activity on pNPA. No differences were observed regarding activity when CsAbf62A was expressed with its appended CBM13 module or only the catalytic domain. The amount of xylobiose released from either wheat arabinoxylan or arabino-xylo-oligosaccharides increased significantly when rCsXyn10A was supplemented with rCsAbf62A, indicating that the removal of arabinosyl residues by rCsAbf62A improved rCsXyn10A accessibility to β-1,4-xylose linkages, but no synergism was observed in the deconstruction of wheat bran. These results contribute to designing tailor-made, substrate-specific, enzymatic cocktails for xylan valorization.Instituto de BiotecnologíaFil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; ArgentinaFil: Garrido, Mercedes Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Garrido, Mercedes Maria. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; ArgentinaFil: Piccinni, Florencia Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Piccinni, Florencia Elizabeth. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Landoni, Malena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigación en Hidratos de Carbono; ArgentinaFil: Landoni, Malena. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Peña, María Jesús. University of Georgia. Complex Carbohydrate Research Center; Estados UnidosFil: Topalian, Juliana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; ArgentinaFil: Topalian, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Couto, Alicia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigación en Hidratos de Carbono; ArgentinaFil: Wirth, Sonia Alejandra. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Urbanowicz, Breeanna Rae. University of Georgia. Department of Biochemistry and Molecular Biology; Estados UnidosFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; ArgentinaFil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaSpringer2022-07-27T11:10:21Z2022-07-27T11:10:21Z2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/12415https://link.springer.com/article/10.1007/s00253-022-12061-31432-0614https://doi.org/10.1007/s00253-022-12061-3Applied Microbiology and Biotechnology (Published: 08 July 2022)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repograntAgreement/INTA/2019-PD-E6-I116-001/2019-PD-E6-I116-001/AR./Identificación y análisis funcional de genes o redes génicas de interés biotecnológico con fin agropecuario, forestal, agroalimentario y/o agroindustrial.info:eu-repograntAgreement/INTA/2019-PD-E7-I152-001/2019-PD-E7-I152-001/AR./Alimentos nutracéuticos, funcionales o para regímenes especiales.info:eu-repograntAgreement/INTA/2019-PE-E7-I149-001/2019-PE-E7-I149-001/AR./Bioenergía generada en origen como aporte al desarrollo territorialinfo:eu-repo/semantics/restrictedAccess2025-10-16T09:30:49Zoai:localhost:20.500.12123/12415instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-10-16 09:30:50.302INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
title Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
spellingShingle Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
Garrido, Mercedes Maria
Hemicellulose
Xylans
Hemicelulosa
Cellulomonas
Xilanos
title_short Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
title_full Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
title_fullStr Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
title_full_unstemmed Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
title_sort Insights into the xylan degradation system of Cellulomonas sp. B6 : biochemical characterization of rCsXyn10A and rCsAbf62A
dc.creator.none.fl_str_mv Garrido, Mercedes Maria
Piccinni, Florencia Elizabeth
Landoni, Malena
Peña, María Jesús
Topalian, Juliana
Couto, Alicia
Wirth, Sonia Alejandra
Urbanowicz, Breeanna Rae
Campos, Eleonora
author Garrido, Mercedes Maria
author_facet Garrido, Mercedes Maria
Piccinni, Florencia Elizabeth
Landoni, Malena
Peña, María Jesús
Topalian, Juliana
Couto, Alicia
Wirth, Sonia Alejandra
Urbanowicz, Breeanna Rae
Campos, Eleonora
author_role author
author2 Piccinni, Florencia Elizabeth
Landoni, Malena
Peña, María Jesús
Topalian, Juliana
Couto, Alicia
Wirth, Sonia Alejandra
Urbanowicz, Breeanna Rae
Campos, Eleonora
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Hemicellulose
Xylans
Hemicelulosa
Cellulomonas
Xilanos
topic Hemicellulose
Xylans
Hemicelulosa
Cellulomonas
Xilanos
dc.description.none.fl_txt_mv Valorization of the hemicellulose fraction of plant biomass is crucial for the sustainability of lignocellulosic biorefineries. The Cellulomonas genus comprises Gram-positive Actinobacteria that degrade cellulose and other polysaccharides by secreting a complex array of enzymes. In this work, we studied the specificity and synergy of two enzymes, CsXyn10A and CsAbf62A, which were identified as highly abundant in the extracellular proteome of Cellulomonas sp. B6 when grown on wheat bran. To explore their potential for bioprocessing, the recombinant enzymes were expressed and their activities were thoroughly characterized. rCsXyn10A is a GH10 endo-xylanase (EC 3.2.1.8), active across a broad pH range (5 to 9), at temperatures up to 55 °C. rCsAbf62A is an α-L-arabinofuranosidase (ABF) (EC 3.2.1.55) that specifically removes α-1,2 and α-1,3-L-arabinosyl substituents from arabino-xylo-oligosaccharides (AXOS), xylan, and arabinan backbones, but it cannot act on double-substituted residues. It also has activity on pNPA. No differences were observed regarding activity when CsAbf62A was expressed with its appended CBM13 module or only the catalytic domain. The amount of xylobiose released from either wheat arabinoxylan or arabino-xylo-oligosaccharides increased significantly when rCsXyn10A was supplemented with rCsAbf62A, indicating that the removal of arabinosyl residues by rCsAbf62A improved rCsXyn10A accessibility to β-1,4-xylose linkages, but no synergism was observed in the deconstruction of wheat bran. These results contribute to designing tailor-made, substrate-specific, enzymatic cocktails for xylan valorization.
Instituto de Biotecnología
Fil: Garrido, Mercedes Maria. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Garrido, Mercedes Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Garrido, Mercedes Maria. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Piccinni, Florencia Elizabeth. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Piccinni, Florencia Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Piccinni, Florencia Elizabeth. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Landoni, Malena. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigación en Hidratos de Carbono; Argentina
Fil: Landoni, Malena. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Peña, María Jesús. University of Georgia. Complex Carbohydrate Research Center; Estados Unidos
Fil: Topalian, Juliana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Topalian, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Couto, Alicia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigación en Hidratos de Carbono; Argentina
Fil: Wirth, Sonia Alejandra. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Wirth, Sonia Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Urbanowicz, Breeanna Rae. University of Georgia. Department of Biochemistry and Molecular Biology; Estados Unidos
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Valorization of the hemicellulose fraction of plant biomass is crucial for the sustainability of lignocellulosic biorefineries. The Cellulomonas genus comprises Gram-positive Actinobacteria that degrade cellulose and other polysaccharides by secreting a complex array of enzymes. In this work, we studied the specificity and synergy of two enzymes, CsXyn10A and CsAbf62A, which were identified as highly abundant in the extracellular proteome of Cellulomonas sp. B6 when grown on wheat bran. To explore their potential for bioprocessing, the recombinant enzymes were expressed and their activities were thoroughly characterized. rCsXyn10A is a GH10 endo-xylanase (EC 3.2.1.8), active across a broad pH range (5 to 9), at temperatures up to 55 °C. rCsAbf62A is an α-L-arabinofuranosidase (ABF) (EC 3.2.1.55) that specifically removes α-1,2 and α-1,3-L-arabinosyl substituents from arabino-xylo-oligosaccharides (AXOS), xylan, and arabinan backbones, but it cannot act on double-substituted residues. It also has activity on pNPA. No differences were observed regarding activity when CsAbf62A was expressed with its appended CBM13 module or only the catalytic domain. The amount of xylobiose released from either wheat arabinoxylan or arabino-xylo-oligosaccharides increased significantly when rCsXyn10A was supplemented with rCsAbf62A, indicating that the removal of arabinosyl residues by rCsAbf62A improved rCsXyn10A accessibility to β-1,4-xylose linkages, but no synergism was observed in the deconstruction of wheat bran. These results contribute to designing tailor-made, substrate-specific, enzymatic cocktails for xylan valorization.
publishDate 2022
dc.date.none.fl_str_mv 2022-07-27T11:10:21Z
2022-07-27T11:10:21Z
2022
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/20.500.12123/12415
https://link.springer.com/article/10.1007/s00253-022-12061-3
1432-0614
https://doi.org/10.1007/s00253-022-12061-3
url http://hdl.handle.net/20.500.12123/12415
https://link.springer.com/article/10.1007/s00253-022-12061-3
https://doi.org/10.1007/s00253-022-12061-3
identifier_str_mv 1432-0614
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repograntAgreement/INTA/2019-PD-E6-I116-001/2019-PD-E6-I116-001/AR./Identificación y análisis funcional de genes o redes génicas de interés biotecnológico con fin agropecuario, forestal, agroalimentario y/o agroindustrial.
info:eu-repograntAgreement/INTA/2019-PD-E7-I152-001/2019-PD-E7-I152-001/AR./Alimentos nutracéuticos, funcionales o para regímenes especiales.
info:eu-repograntAgreement/INTA/2019-PE-E7-I149-001/2019-PE-E7-I149-001/AR./Bioenergía generada en origen como aporte al desarrollo territorial
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
eu_rights_str_mv restrictedAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv Applied Microbiology and Biotechnology (Published: 08 July 2022)
reponame:INTA Digital (INTA)
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