Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse
- Autores
- Bruno Baron, Camila Ayelen; Mon, Maria Laura; Marrero Diaz De Vill, Rubén; Cattaneo, Andrea; Di Donato, Paola; Poli, Annarita; Negri, Maria Emilia; Alegre, Mariana; Soria, Marcelo Abel; Rojo, Cecilia; Combina, Mariana; Finore, Ilaria; Talia, Paola Mónica
- Año de publicación
- 2025
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- In this study, we characterized two novel enzymes of the glycoside hydrolase family 10 (GH10), Xyl10 C and Xyl10E, identified in the termite gut microbiome. The activities of both enzymes were assayed using beechwood xylan, barley β-glucan, and pretreated Sorghum bicolor bagasse (SBB) as substrates. Both enzymes, assessed individually and in combination, showed activity on beechwood xylan and pretreated SBB, whereas Xyl10E also showed activity on barley β-glucan. The composition of pretreated SBB mainly consisted of xylose and arabinose content. Purified Xyl10 C showed optimum xylanase activity in the pH range 7.0–8.0 and at a temperature of 50–60 °C, while Xyl10E was active at a wider pH range (5.0–10.0) and at 50 °C. The residual activities of Xyl10 C and Xyl10E after 8 h of incubation at 40 °C were 85% and 70%, respectively. The enzymatic activity of Xyl10 C increased to 115% in the presence of 5 M NaCl, was only inhibited in the presence of 0.5% sodium dodecyl sulfate (SDS), and decreased with β-mercaptoethanol. The xylanase and glucanase activities of Xyl10E were inhibited only in the presence of MnSO4, NaCl, and SDS. The main hydrolysis enzymatic product of Xyl10 C and Xyl10E on pretreated SBB was xylobiose. In addition, the xylo-oligosaccharides produced by xylanase Xyl10E on pretreated SBB demonstrated promising antioxidant activity. Thus, the hydrolysis products using Xyl10E on pretreated SBB indicate potential for antioxidant activity and other valuable industrial applications.
Instituto de Biotecnología
Fil: Bruno Baron, Camila Ayelen. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina
Fil: Bruno Baron, Camila Ayelen. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bruno Baron, Camila Ayelen. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina
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: Cattaneo, Andrea. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); Italia
Fil: Di Donato, Paola. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); Italia
Fil: Di Donato, Paola. University of Naples “Parthenope”. Department of Science and Technology; Italia
Fil: Poli, Annarita. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); Italia
Fil: Negri, Maria Emilia. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Pergamino; Argentina
Fil: Alegre, Mariana. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Pergamino; Argentina
Fil: Alegre, Mariana. Universidad Nacional del Noroeste de La Provincia de Buenos Aires. Escuela de Ciencias Agrarias y Ambientales; Argentina
Fil: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; Argentina
Fil: Rojo, Cecilia. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Mendoza; Argentina
Fil: Rojo, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Combina, Mariana. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Mendoza; Argentina
Fil: Combina, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Finore, Ilaria. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); Italia
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
Fil: Talia, Paola Mónica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina - Fuente
- Applied Microbiology and Biotechnology 109 (1) : 104 (Abril 2025)
- Materia
-
Sorghum bicolor
Antioxidants
Enzymatic Hydrolysis
Antioxidantes
Hidrólisis Enzimática
Xylanase - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
.jpg)
- Institución
- Instituto Nacional de Tecnología Agropecuaria
- OAI Identificador
- oai:localhost:20.500.12123/22112
Ver los metadatos del registro completo
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Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasseBruno Baron, Camila AyelenMon, Maria LauraMarrero Diaz De Vill, RubénCattaneo, AndreaDi Donato, PaolaPoli, AnnaritaNegri, Maria EmiliaAlegre, MarianaSoria, Marcelo AbelRojo, CeciliaCombina, MarianaFinore, IlariaTalia, Paola MónicaSorghum bicolorAntioxidantsEnzymatic HydrolysisAntioxidantesHidrólisis EnzimáticaXylanaseIn this study, we characterized two novel enzymes of the glycoside hydrolase family 10 (GH10), Xyl10 C and Xyl10E, identified in the termite gut microbiome. The activities of both enzymes were assayed using beechwood xylan, barley β-glucan, and pretreated Sorghum bicolor bagasse (SBB) as substrates. Both enzymes, assessed individually and in combination, showed activity on beechwood xylan and pretreated SBB, whereas Xyl10E also showed activity on barley β-glucan. The composition of pretreated SBB mainly consisted of xylose and arabinose content. Purified Xyl10 C showed optimum xylanase activity in the pH range 7.0–8.0 and at a temperature of 50–60 °C, while Xyl10E was active at a wider pH range (5.0–10.0) and at 50 °C. The residual activities of Xyl10 C and Xyl10E after 8 h of incubation at 40 °C were 85% and 70%, respectively. The enzymatic activity of Xyl10 C increased to 115% in the presence of 5 M NaCl, was only inhibited in the presence of 0.5% sodium dodecyl sulfate (SDS), and decreased with β-mercaptoethanol. The xylanase and glucanase activities of Xyl10E were inhibited only in the presence of MnSO4, NaCl, and SDS. The main hydrolysis enzymatic product of Xyl10 C and Xyl10E on pretreated SBB was xylobiose. In addition, the xylo-oligosaccharides produced by xylanase Xyl10E on pretreated SBB demonstrated promising antioxidant activity. Thus, the hydrolysis products using Xyl10E on pretreated SBB indicate potential for antioxidant activity and other valuable industrial applications.Instituto de BiotecnologíaFil: Bruno Baron, Camila Ayelen. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); ArgentinaFil: Bruno Baron, Camila Ayelen. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Bruno Baron, Camila Ayelen. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; ArgentinaFil: 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: Cattaneo, Andrea. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); ItaliaFil: Di Donato, Paola. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); ItaliaFil: Di Donato, Paola. University of Naples “Parthenope”. Department of Science and Technology; ItaliaFil: Poli, Annarita. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); ItaliaFil: Negri, Maria Emilia. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Pergamino; ArgentinaFil: Alegre, Mariana. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Pergamino; ArgentinaFil: Alegre, Mariana. Universidad Nacional del Noroeste de La Provincia de Buenos Aires. Escuela de Ciencias Agrarias y Ambientales; ArgentinaFil: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; ArgentinaFil: Rojo, Cecilia. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Mendoza; ArgentinaFil: Rojo, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Combina, Mariana. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Mendoza; ArgentinaFil: Combina, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Finore, Ilaria. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); ItaliaFil: 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; ArgentinaFil: Talia, Paola Mónica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; ArgentinaSpringer2025-04-30T09:58:19Z2025-04-30T09:58:19Z2025-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/22112https://link.springer.com/article/10.1007/s00253-025-13484-41432-06140175-7598https://doi.org/10.1007/s00253-025-13484-4Applied Microbiology and Biotechnology 109 (1) : 104 (Abril 2025)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repograntAgreement/INTA/2023-PD-L01-I085, Identificación y caracterización funcional de genes interés biotecnológico para la sostenibilidad productiva y ambientalinfo:eu-repograntAgreement/INTA/2023-PD-L01-I089, Microbiomas en ecosistemas agropecuarios: la conexión integradora del enfoque Una Saludinfo:eu-repograntAgreement/INTA/2023-PD-L04-I122, Gestión de las biomasas del SAB y estrategias tecnológicas para su transformación en bioproductos de valor agregadoinfo:eu-repograntAgreement/INTA/2019-PT-E7-I159-001, 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)2025-09-29T13:47:15Zoai:localhost:20.500.12123/22112instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-29 13:47:16.211INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse |
| dc.title.none.fl_str_mv |
Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse |
| title |
Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse |
| spellingShingle |
Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse Bruno Baron, Camila Ayelen Sorghum bicolor Antioxidants Enzymatic Hydrolysis Antioxidantes Hidrólisis Enzimática Xylanase |
| title_short |
Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse |
| title_full |
Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse |
| title_fullStr |
Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse |
| title_full_unstemmed |
Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse |
| title_sort |
Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse |
| dc.creator.none.fl_str_mv |
Bruno Baron, Camila Ayelen Mon, Maria Laura Marrero Diaz De Vill, Rubén Cattaneo, Andrea Di Donato, Paola Poli, Annarita Negri, Maria Emilia Alegre, Mariana Soria, Marcelo Abel Rojo, Cecilia Combina, Mariana Finore, Ilaria Talia, Paola Mónica |
| author |
Bruno Baron, Camila Ayelen |
| author_facet |
Bruno Baron, Camila Ayelen Mon, Maria Laura Marrero Diaz De Vill, Rubén Cattaneo, Andrea Di Donato, Paola Poli, Annarita Negri, Maria Emilia Alegre, Mariana Soria, Marcelo Abel Rojo, Cecilia Combina, Mariana Finore, Ilaria Talia, Paola Mónica |
| author_role |
author |
| author2 |
Mon, Maria Laura Marrero Diaz De Vill, Rubén Cattaneo, Andrea Di Donato, Paola Poli, Annarita Negri, Maria Emilia Alegre, Mariana Soria, Marcelo Abel Rojo, Cecilia Combina, Mariana Finore, Ilaria Talia, Paola Mónica |
| author2_role |
author author author author author author author author author author author author |
| dc.subject.none.fl_str_mv |
Sorghum bicolor Antioxidants Enzymatic Hydrolysis Antioxidantes Hidrólisis Enzimática Xylanase |
| topic |
Sorghum bicolor Antioxidants Enzymatic Hydrolysis Antioxidantes Hidrólisis Enzimática Xylanase |
| dc.description.none.fl_txt_mv |
In this study, we characterized two novel enzymes of the glycoside hydrolase family 10 (GH10), Xyl10 C and Xyl10E, identified in the termite gut microbiome. The activities of both enzymes were assayed using beechwood xylan, barley β-glucan, and pretreated Sorghum bicolor bagasse (SBB) as substrates. Both enzymes, assessed individually and in combination, showed activity on beechwood xylan and pretreated SBB, whereas Xyl10E also showed activity on barley β-glucan. The composition of pretreated SBB mainly consisted of xylose and arabinose content. Purified Xyl10 C showed optimum xylanase activity in the pH range 7.0–8.0 and at a temperature of 50–60 °C, while Xyl10E was active at a wider pH range (5.0–10.0) and at 50 °C. The residual activities of Xyl10 C and Xyl10E after 8 h of incubation at 40 °C were 85% and 70%, respectively. The enzymatic activity of Xyl10 C increased to 115% in the presence of 5 M NaCl, was only inhibited in the presence of 0.5% sodium dodecyl sulfate (SDS), and decreased with β-mercaptoethanol. The xylanase and glucanase activities of Xyl10E were inhibited only in the presence of MnSO4, NaCl, and SDS. The main hydrolysis enzymatic product of Xyl10 C and Xyl10E on pretreated SBB was xylobiose. In addition, the xylo-oligosaccharides produced by xylanase Xyl10E on pretreated SBB demonstrated promising antioxidant activity. Thus, the hydrolysis products using Xyl10E on pretreated SBB indicate potential for antioxidant activity and other valuable industrial applications. Instituto de Biotecnología Fil: Bruno Baron, Camila Ayelen. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina Fil: Bruno Baron, Camila Ayelen. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Bruno Baron, Camila Ayelen. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina 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: Cattaneo, Andrea. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); Italia Fil: Di Donato, Paola. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); Italia Fil: Di Donato, Paola. University of Naples “Parthenope”. Department of Science and Technology; Italia Fil: Poli, Annarita. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); Italia Fil: Negri, Maria Emilia. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Pergamino; Argentina Fil: Alegre, Mariana. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Pergamino; Argentina Fil: Alegre, Mariana. Universidad Nacional del Noroeste de La Provincia de Buenos Aires. Escuela de Ciencias Agrarias y Ambientales; Argentina Fil: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; Argentina Fil: Rojo, Cecilia. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Mendoza; Argentina Fil: Rojo, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Combina, Mariana. Instituto Nacional de Tecnología Agropecuaria (INTA). Estación Experimental Agropecuaria Mendoza; Argentina Fil: Combina, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Finore, Ilaria. Consiglio Nazionale Delle Ricerche (CNR). Institute of Biomolecular Chemistry (ICB); Italia 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 Fil: Talia, Paola Mónica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina |
| description |
In this study, we characterized two novel enzymes of the glycoside hydrolase family 10 (GH10), Xyl10 C and Xyl10E, identified in the termite gut microbiome. The activities of both enzymes were assayed using beechwood xylan, barley β-glucan, and pretreated Sorghum bicolor bagasse (SBB) as substrates. Both enzymes, assessed individually and in combination, showed activity on beechwood xylan and pretreated SBB, whereas Xyl10E also showed activity on barley β-glucan. The composition of pretreated SBB mainly consisted of xylose and arabinose content. Purified Xyl10 C showed optimum xylanase activity in the pH range 7.0–8.0 and at a temperature of 50–60 °C, while Xyl10E was active at a wider pH range (5.0–10.0) and at 50 °C. The residual activities of Xyl10 C and Xyl10E after 8 h of incubation at 40 °C were 85% and 70%, respectively. The enzymatic activity of Xyl10 C increased to 115% in the presence of 5 M NaCl, was only inhibited in the presence of 0.5% sodium dodecyl sulfate (SDS), and decreased with β-mercaptoethanol. The xylanase and glucanase activities of Xyl10E were inhibited only in the presence of MnSO4, NaCl, and SDS. The main hydrolysis enzymatic product of Xyl10 C and Xyl10E on pretreated SBB was xylobiose. In addition, the xylo-oligosaccharides produced by xylanase Xyl10E on pretreated SBB demonstrated promising antioxidant activity. Thus, the hydrolysis products using Xyl10E on pretreated SBB indicate potential for antioxidant activity and other valuable industrial applications. |
| publishDate |
2025 |
| dc.date.none.fl_str_mv |
2025-04-30T09:58:19Z 2025-04-30T09:58:19Z 2025-04 |
| 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 |
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article |
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publishedVersion |
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http://hdl.handle.net/20.500.12123/22112 https://link.springer.com/article/10.1007/s00253-025-13484-4 1432-0614 0175-7598 https://doi.org/10.1007/s00253-025-13484-4 |
| url |
http://hdl.handle.net/20.500.12123/22112 https://link.springer.com/article/10.1007/s00253-025-13484-4 https://doi.org/10.1007/s00253-025-13484-4 |
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1432-0614 0175-7598 |
| dc.language.none.fl_str_mv |
eng |
| language |
eng |
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info:eu-repograntAgreement/INTA/2023-PD-L01-I085, Identificación y caracterización funcional de genes interés biotecnológico para la sostenibilidad productiva y ambiental info:eu-repograntAgreement/INTA/2023-PD-L01-I089, Microbiomas en ecosistemas agropecuarios: la conexión integradora del enfoque Una Salud info:eu-repograntAgreement/INTA/2023-PD-L04-I122, Gestión de las biomasas del SAB y estrategias tecnológicas para su transformación en bioproductos de valor agregado info:eu-repograntAgreement/INTA/2019-PT-E7-I159-001, Info e innovación p/ VA, agroind. y bioenergía |
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Springer |
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