Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse

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....

Descripción completa

Detalles Bibliográficos
Autores principales: 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
Formato: Artículo
Lenguaje:Inglés
Publicado: Springer 2025
Materias:
Acceso en línea: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
_version_ 1855486876587130880
author 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_browse Alegre, Mariana
Bruno Baron, Camila Ayelen
Cattaneo, Andrea
Combina, Mariana
Di Donato, Paola
Finore, Ilaria
Marrero Diaz De Vill, Rubén
Mon, Maria Laura
Negri, Maria Emilia
Poli, Annarita
Rojo, Cecilia
Soria, Marcelo Abel
Talia, Paola Mónica
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_sort Bruno Baron, Camila Ayelen
collection INTA Digital
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.
format Artículo
id INTA22112
institution Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina)
language Inglés
publishDate 2025
publishDateRange 2025
publishDateSort 2025
publisher Springer
publisherStr Springer
record_format dspace
spelling INTA221122025-04-30T10:09:45Z Characterization of two GH10 enzymes with ability to hydrolyze pretreated Sorghum bicolor bagasse 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 Sorghum bicolor Antioxidants Enzymatic Hydrolysis Antioxidantes Hidrólisis Enzimática Xylanase 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 2025-04-30T09:58:19Z 2025-04-30T09:58:19Z 2025-04 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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 eng 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 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 Applied Microbiology and Biotechnology 109 (1) : 104 (Abril 2025)
spellingShingle Sorghum bicolor
Antioxidants
Enzymatic Hydrolysis
Antioxidantes
Hidrólisis Enzimática
Xylanase
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
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
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_short 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
topic Sorghum bicolor
Antioxidants
Enzymatic Hydrolysis
Antioxidantes
Hidrólisis Enzimática
Xylanase
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
work_keys_str_mv AT brunobaroncamilaayelen characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT monmarialaura characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT marrerodiazdevillruben characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT cattaneoandrea characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT didonatopaola characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT poliannarita characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT negrimariaemilia characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT alegremariana characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT soriamarceloabel characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT rojocecilia characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT combinamariana characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT finoreilaria characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse
AT taliapaolamonica characterizationoftwogh10enzymeswithabilitytohydrolyzepretreatedsorghumbicolorbagasse