Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome

Autores
Mon, Maria Laura; Marrero Diaz De Vill, Rubén; Campos, Eleonora; Soria, Marcelo Abel; Talia, Paola Mónica
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The aim of the present study was to assess the biochemical and molecular structural characteristics of a novel alkali-thermostable GH10 xylanase (Xyl10B) identified in a termite gut microbiome by a shotgun metagenomic approach. This endoxylanase candidate was amplified, cloned, heterologously expressed in Escherichia coli and purified. The recombinant enzyme was active at a broad range of temperatures (37–60 ºC) and pH values (4–10), with optimal activity at 50 ºC and pH 9. Moreover, its activity remained at more than 80% of its maximum at 50 °C for 8 h. In addition, Xyl10B was found to be stable in the presence of salt and several ions and chemical reagents frequently used in the industry. These characteristics make this enzyme an interesting candidate for pulp and paper bleaching industries, since this process requires enzymes without cellulase activity and resistant to high temperatures and alkaline pH (thermo-alkaliphilic enzymes). The products of xylan hydrolysis by Xyl10B (short xylooligosaccharides, xylose and xylobiose) could be suitable for application as prebiotics and in the production of bioethanol.
Instituto de Biotecnología
Fil: Mon, Maria Laura. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Mon, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marrero Diaz De Vill, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Marrero Diaz De Vill, Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; Argentina
Fil: Soria, Marcelo Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Talia, Paola Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fuente
Bioresources and Bioprocessing 9 : 84 (Agosto 2022)
Materia
Molecular Genetics
Isoptera
Termitidae
Microbiomes
Biochemistry
Alkalinity
Temperature
Prebiotics
Genética Molecular
Microbiomas
Bioquímica
Alcalinidad
Temperatura
Prebióticos
Bioethanol
Bioetanol
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:20.500.12123/12705
Acceder
id INTADig_d2cd9ae16398d1942dc424643aefaa63
oai_identifier_str oai:localhost:20.500.12123/12705
network_acronym_str INTADig
repository_id_str l
network_name_str INTA Digital (INTA)
spelling Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiomeMon, Maria LauraMarrero Diaz De Vill, RubénCampos, EleonoraSoria, Marcelo AbelTalia, Paola MónicaMolecular GeneticsIsopteraTermitidaeMicrobiomesBiochemistryAlkalinityTemperaturePrebioticsGenética MolecularMicrobiomasBioquímicaAlcalinidadTemperaturaPrebióticosBioethanolBioetanolThe aim of the present study was to assess the biochemical and molecular structural characteristics of a novel alkali-thermostable GH10 xylanase (Xyl10B) identified in a termite gut microbiome by a shotgun metagenomic approach. This endoxylanase candidate was amplified, cloned, heterologously expressed in Escherichia coli and purified. The recombinant enzyme was active at a broad range of temperatures (37–60 ºC) and pH values (4–10), with optimal activity at 50 ºC and pH 9. Moreover, its activity remained at more than 80% of its maximum at 50 °C for 8 h. In addition, Xyl10B was found to be stable in the presence of salt and several ions and chemical reagents frequently used in the industry. These characteristics make this enzyme an interesting candidate for pulp and paper bleaching industries, since this process requires enzymes without cellulase activity and resistant to high temperatures and alkaline pH (thermo-alkaliphilic enzymes). The products of xylan hydrolysis by Xyl10B (short xylooligosaccharides, xylose and xylobiose) could be suitable for application as prebiotics and in the production of bioethanol.Instituto de BiotecnologíaFil: Mon, Maria Laura. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); ArgentinaFil: Mon, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Marrero Diaz De Vill, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); ArgentinaFil: Marrero Diaz De Vill, Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); ArgentinaFil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; ArgentinaFil: Soria, Marcelo Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); ArgentinaFil: Talia, Paola Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaSpringer Open2022-08-26T13:05:28Z2022-08-26T13:05:28Z2022-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/12705https://bioresourcesbioprocessing.springeropen.com/articles/10.1186/s40643-022-00572-w2197-4365https://doi.org/10.1186/s40643-022-00572-wBioresources and Bioprocessing 9 : 84 (Agosto 2022)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repograntAgreement/INTA/2019-PD-E5-I102-001/2019-PD-E5-I102-001/AR./Desarrollo de vacunas y tecnologías para mejorar las estrategias profilácticas y terapéuticas de las enfermedades que afectan la producción animal y la salud públicainfo:eu-repograntAgreement/INTA/2019-PD-E5-I106-001/2019-PD-E5-I106-001/AR./Estudios metagenómicos en animales y medio ambiente para modular la microbiota, desarrollar probióticos y mitigar el impacto ambiental de la producción pecuariainfo: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-PE-E7-I149-001/2019-PE-E7-I149-001/AR./Bioenergía generada en origen como aporte al desarrollo territorialinfo:eu-repograntAgreement/INTA/2019-PT-E7-I159-001/2019-PT-E7-I159-001/AR./Info e innovación p/ VA, agroind. y bioenergíainfo: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)2025-10-16T09:30:53Zoai:localhost:20.500.12123/12705instacron: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 09:30:53.562INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
title Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
spellingShingle Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
Mon, Maria Laura
Molecular Genetics
Isoptera
Termitidae
Microbiomes
Biochemistry
Alkalinity
Temperature
Prebiotics
Genética Molecular
Microbiomas
Bioquímica
Alcalinidad
Temperatura
Prebióticos
Bioethanol
Bioetanol
title_short Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
title_full Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
title_fullStr Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
title_full_unstemmed Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
title_sort Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
dc.creator.none.fl_str_mv Mon, Maria Laura
Marrero Diaz De Vill, Rubén
Campos, Eleonora
Soria, Marcelo Abel
Talia, Paola Mónica
author Mon, Maria Laura
author_facet Mon, Maria Laura
Marrero Diaz De Vill, Rubén
Campos, Eleonora
Soria, Marcelo Abel
Talia, Paola Mónica
author_role author
author2 Marrero Diaz De Vill, Rubén
Campos, Eleonora
Soria, Marcelo Abel
Talia, Paola Mónica
author2_role author
author
author
author
dc.subject.none.fl_str_mv Molecular Genetics
Isoptera
Termitidae
Microbiomes
Biochemistry
Alkalinity
Temperature
Prebiotics
Genética Molecular
Microbiomas
Bioquímica
Alcalinidad
Temperatura
Prebióticos
Bioethanol
Bioetanol
topic Molecular Genetics
Isoptera
Termitidae
Microbiomes
Biochemistry
Alkalinity
Temperature
Prebiotics
Genética Molecular
Microbiomas
Bioquímica
Alcalinidad
Temperatura
Prebióticos
Bioethanol
Bioetanol
dc.description.none.fl_txt_mv The aim of the present study was to assess the biochemical and molecular structural characteristics of a novel alkali-thermostable GH10 xylanase (Xyl10B) identified in a termite gut microbiome by a shotgun metagenomic approach. This endoxylanase candidate was amplified, cloned, heterologously expressed in Escherichia coli and purified. The recombinant enzyme was active at a broad range of temperatures (37–60 ºC) and pH values (4–10), with optimal activity at 50 ºC and pH 9. Moreover, its activity remained at more than 80% of its maximum at 50 °C for 8 h. In addition, Xyl10B was found to be stable in the presence of salt and several ions and chemical reagents frequently used in the industry. These characteristics make this enzyme an interesting candidate for pulp and paper bleaching industries, since this process requires enzymes without cellulase activity and resistant to high temperatures and alkaline pH (thermo-alkaliphilic enzymes). The products of xylan hydrolysis by Xyl10B (short xylooligosaccharides, xylose and xylobiose) could be suitable for application as prebiotics and in the production of bioethanol.
Instituto de Biotecnología
Fil: Mon, Maria Laura. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Mon, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Marrero Diaz De Vill, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Marrero Diaz De Vill, Rubén. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Campos, Eleonora. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Campos, Eleonora. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; Argentina
Fil: Soria, Marcelo Abel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Talia, Paola Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Talia, Paola Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The aim of the present study was to assess the biochemical and molecular structural characteristics of a novel alkali-thermostable GH10 xylanase (Xyl10B) identified in a termite gut microbiome by a shotgun metagenomic approach. This endoxylanase candidate was amplified, cloned, heterologously expressed in Escherichia coli and purified. The recombinant enzyme was active at a broad range of temperatures (37–60 ºC) and pH values (4–10), with optimal activity at 50 ºC and pH 9. Moreover, its activity remained at more than 80% of its maximum at 50 °C for 8 h. In addition, Xyl10B was found to be stable in the presence of salt and several ions and chemical reagents frequently used in the industry. These characteristics make this enzyme an interesting candidate for pulp and paper bleaching industries, since this process requires enzymes without cellulase activity and resistant to high temperatures and alkaline pH (thermo-alkaliphilic enzymes). The products of xylan hydrolysis by Xyl10B (short xylooligosaccharides, xylose and xylobiose) could be suitable for application as prebiotics and in the production of bioethanol.
publishDate 2022
dc.date.none.fl_str_mv 2022-08-26T13:05:28Z
2022-08-26T13:05:28Z
2022-08
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/20.500.12123/12705
https://bioresourcesbioprocessing.springeropen.com/articles/10.1186/s40643-022-00572-w
2197-4365
https://doi.org/10.1186/s40643-022-00572-w
url http://hdl.handle.net/20.500.12123/12705
https://bioresourcesbioprocessing.springeropen.com/articles/10.1186/s40643-022-00572-w
https://doi.org/10.1186/s40643-022-00572-w
identifier_str_mv 2197-4365
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repograntAgreement/INTA/2019-PD-E5-I102-001/2019-PD-E5-I102-001/AR./Desarrollo de vacunas y tecnologías para mejorar las estrategias profilácticas y terapéuticas de las enfermedades que afectan la producción animal y la salud pública
info:eu-repograntAgreement/INTA/2019-PD-E5-I106-001/2019-PD-E5-I106-001/AR./Estudios metagenómicos en animales y medio ambiente para modular la microbiota, desarrollar probióticos y mitigar el impacto ambiental de la producción pecuaria
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-PE-E7-I149-001/2019-PE-E7-I149-001/AR./Bioenergía generada en origen como aporte al desarrollo territorial
info:eu-repograntAgreement/INTA/2019-PT-E7-I159-001/2019-PT-E7-I159-001/AR./Info e innovación p/ VA, agroind. y bioenergía
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.publisher.none.fl_str_mv Springer Open
publisher.none.fl_str_mv Springer Open
dc.source.none.fl_str_mv Bioresources and Bioprocessing 9 : 84 (Agosto 2022)
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
_version_ 1846143551459557376
score 12.712165

Publicaciones similares