Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome
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 expres...
| Autores principales: | , , , , |
|---|---|
| Formato: | info:ar-repo/semantics/artículo |
| Lenguaje: | Inglés |
| Publicado: |
Springer Open
2022
|
| Materias: | |
| Acceso en línea: | 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 |
| _version_ | 1855036808358789120 |
|---|---|
| author | Mon, Maria Laura Marrero Diaz De Vill, Rubén Campos, Eleonora Soria, Marcelo Abel Talia, Paola Mónica |
| author_browse | Campos, Eleonora Marrero Diaz De Vill, Rubén Mon, Maria Laura Soria, Marcelo Abel Talia, Paola Mónica |
| author_facet | Mon, Maria Laura Marrero Diaz De Vill, Rubén Campos, Eleonora Soria, Marcelo Abel Talia, Paola Mónica |
| author_sort | Mon, Maria Laura |
| collection | INTA Digital |
| 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. |
| format | info:ar-repo/semantics/artículo |
| id | INTA12705 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2022 |
| publishDateRange | 2022 |
| publishDateSort | 2022 |
| publisher | Springer Open |
| publisherStr | Springer Open |
| record_format | dspace |
| spelling | INTA127052022-08-26T13:13:14Z Characterization of a novel GH10 alkali‑thermostable xylanase from a termite microbiome Mon, Maria Laura Marrero Diaz De Vill, Rubén Campos, Eleonora Soria, Marcelo Abel Talia, Paola Mónica Molecular Genetics Isoptera Termitidae Microbiomes Biochemistry Alkalinity Temperature Prebiotics Genética Molecular Microbiomas Bioquímica Alcalinidad Temperatura Prebióticos Bioethanol Bioetanol 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 2022-08-26T13:05:28Z 2022-08-26T13:05:28Z 2022-08 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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 eng 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 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) application/pdf Springer Open Bioresources and Bioprocessing 9 : 84 (Agosto 2022) |
| spellingShingle | Molecular Genetics Isoptera Termitidae Microbiomes Biochemistry Alkalinity Temperature Prebiotics Genética Molecular Microbiomas Bioquímica Alcalinidad Temperatura Prebióticos Bioethanol Bioetanol Mon, Maria Laura Marrero Diaz De Vill, Rubén Campos, Eleonora Soria, Marcelo Abel Talia, Paola Mónica 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 |
| 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_short | 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 |
| topic | Molecular Genetics Isoptera Termitidae Microbiomes Biochemistry Alkalinity Temperature Prebiotics Genética Molecular Microbiomas Bioquímica Alcalinidad Temperatura Prebióticos Bioethanol Bioetanol |
| 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 |
| work_keys_str_mv | AT monmarialaura characterizationofanovelgh10alkalithermostablexylanasefromatermitemicrobiome AT marrerodiazdevillruben characterizationofanovelgh10alkalithermostablexylanasefromatermitemicrobiome AT camposeleonora characterizationofanovelgh10alkalithermostablexylanasefromatermitemicrobiome AT soriamarceloabel characterizationofanovelgh10alkalithermostablexylanasefromatermitemicrobiome AT taliapaolamonica characterizationofanovelgh10alkalithermostablexylanasefromatermitemicrobiome |