Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion

Autores
Farace, Pablo Daniel; Marrero Diaz De Vill, Rubén; Mon, Maria Laura; Soria, Marcelo Abel; Talia, Paola Mónica
Año de publicación
2026
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lignocellulosic biomass can be converted into biofuels and other valuable bioproducts, but it must first undergo physicochemical and enzymatic degradation. Among the various enzymes involved in lignocellulose degradation, thermophilic glycoside hydrolase family 5 (GH5) cellulases have gained significant attention given their ability to sustain enzymatic activity at temperatures exceeding 60 °C. These high temperatures not only accelerate enzymatic reactions, improving reaction rates and process efficiency, but also enhance substrate solubility and reduce the risk of microbial contamination, making them highly valuable for the paper, food, feed, pharmaceutical, and biofuel industries. In this work, we identified five GH5 cellulases with predicted thermophilic properties from termite gut metagenomes and evaluated their structural features using machine-learning classification, comparative structural modeling, interatomic contact analysis, and temperature-dependent flexibility simulations. The candidates, spanning GH5 subfamilies 2, 25, 37, 39, and 40, displayed high structural confidence (pLDDT > 90) and aliphatic indices comparable to those of thermophilic references. Analysis of amino acid composition analysis revealed enrichment in aromatic and charged residues. Hydrophobic contact densities were consistently higher than in mesophilic controls and aligned with thermophilic benchmarks. Temperature-dependent flexibility simulations showed restrained RMSF profiles, more closely resembling the thermophilic reference enzyme than to the mesophilic control. These findings are consistent with a thermophilic profile, pending experimental confirmation, and provide useful insights for the selection and engineering of GH5 cellulases for high-temperature biotechnological applications.
Instituto de Biotecnología
Fil: Farace, Pablo Daniel. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Farace, Pablo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Farace, Pablo Daniel. University of Vermont. Department of Nutrition and Food Sciences; Estados Unidos
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: 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: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; 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
Journal of Biomolecular Structure and Dynamics : 1-23 (Published online: 07 Jun 2026)
Materia
Cellulase
Glycosides
Hydrolases
Bioconversion
Celulasa
Glicosido
Hidrolasa
Bioconversión
Thermophilicity
Termofilia
Nivel de accesibilidad
acceso restringido
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:20.500.12123/26532
Acceder
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oai_identifier_str oai:localhost:20.500.12123/26532
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network_name_str INTA Digital (INTA)
spelling Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversionFarace, Pablo DanielMarrero Diaz De Vill, RubénMon, Maria LauraSoria, Marcelo AbelTalia, Paola MónicaCellulaseGlycosidesHydrolasesBioconversionCelulasaGlicosidoHidrolasaBioconversiónThermophilicityTermofiliaLignocellulosic biomass can be converted into biofuels and other valuable bioproducts, but it must first undergo physicochemical and enzymatic degradation. Among the various enzymes involved in lignocellulose degradation, thermophilic glycoside hydrolase family 5 (GH5) cellulases have gained significant attention given their ability to sustain enzymatic activity at temperatures exceeding 60 °C. These high temperatures not only accelerate enzymatic reactions, improving reaction rates and process efficiency, but also enhance substrate solubility and reduce the risk of microbial contamination, making them highly valuable for the paper, food, feed, pharmaceutical, and biofuel industries. In this work, we identified five GH5 cellulases with predicted thermophilic properties from termite gut metagenomes and evaluated their structural features using machine-learning classification, comparative structural modeling, interatomic contact analysis, and temperature-dependent flexibility simulations. The candidates, spanning GH5 subfamilies 2, 25, 37, 39, and 40, displayed high structural confidence (pLDDT > 90) and aliphatic indices comparable to those of thermophilic references. Analysis of amino acid composition analysis revealed enrichment in aromatic and charged residues. Hydrophobic contact densities were consistently higher than in mesophilic controls and aligned with thermophilic benchmarks. Temperature-dependent flexibility simulations showed restrained RMSF profiles, more closely resembling the thermophilic reference enzyme than to the mesophilic control. These findings are consistent with a thermophilic profile, pending experimental confirmation, and provide useful insights for the selection and engineering of GH5 cellulases for high-temperature biotechnological applications.Instituto de BiotecnologíaFil: Farace, Pablo Daniel. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; ArgentinaFil: Farace, Pablo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Farace, Pablo Daniel. University of Vermont. Department of Nutrition and Food Sciences; Estados UnidosFil: 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: 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: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; 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; ArgentinaTaylor and Francis2026-06-09T10:15:58Z2026-06-09T10:15:58Z2026-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/26532https://www.tandfonline.com/doi/full/10.1080/07391102.2026.26838721538-02540739-1102https://doi.org/10.1080/07391102.2026.2683872Journal of Biomolecular Structure and Dynamics : 1-23 (Published online: 07 Jun 2026)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/restrictedAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2026-06-18T09:34:28Zoai:localhost:20.500.12123/26532instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2026-06-18 09:34:29.257INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion
title Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion
spellingShingle Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion
Farace, Pablo Daniel
Cellulase
Glycosides
Hydrolases
Bioconversion
Celulasa
Glicosido
Hidrolasa
Bioconversión
Thermophilicity
Termofilia
title_short Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion
title_full Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion
title_fullStr Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion
title_full_unstemmed Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion
title_sort Structural insights into predicted thermophilic GH5 cellulases for industrial lignocellulose bioconversion
dc.creator.none.fl_str_mv Farace, Pablo Daniel
Marrero Diaz De Vill, Rubén
Mon, Maria Laura
Soria, Marcelo Abel
Talia, Paola Mónica
author Farace, Pablo Daniel
author_facet Farace, Pablo Daniel
Marrero Diaz De Vill, Rubén
Mon, Maria Laura
Soria, Marcelo Abel
Talia, Paola Mónica
author_role author
author2 Marrero Diaz De Vill, Rubén
Mon, Maria Laura
Soria, Marcelo Abel
Talia, Paola Mónica
author2_role author
author
author
author
dc.subject.none.fl_str_mv Cellulase
Glycosides
Hydrolases
Bioconversion
Celulasa
Glicosido
Hidrolasa
Bioconversión
Thermophilicity
Termofilia
topic Cellulase
Glycosides
Hydrolases
Bioconversion
Celulasa
Glicosido
Hidrolasa
Bioconversión
Thermophilicity
Termofilia
dc.description.none.fl_txt_mv Lignocellulosic biomass can be converted into biofuels and other valuable bioproducts, but it must first undergo physicochemical and enzymatic degradation. Among the various enzymes involved in lignocellulose degradation, thermophilic glycoside hydrolase family 5 (GH5) cellulases have gained significant attention given their ability to sustain enzymatic activity at temperatures exceeding 60 °C. These high temperatures not only accelerate enzymatic reactions, improving reaction rates and process efficiency, but also enhance substrate solubility and reduce the risk of microbial contamination, making them highly valuable for the paper, food, feed, pharmaceutical, and biofuel industries. In this work, we identified five GH5 cellulases with predicted thermophilic properties from termite gut metagenomes and evaluated their structural features using machine-learning classification, comparative structural modeling, interatomic contact analysis, and temperature-dependent flexibility simulations. The candidates, spanning GH5 subfamilies 2, 25, 37, 39, and 40, displayed high structural confidence (pLDDT > 90) and aliphatic indices comparable to those of thermophilic references. Analysis of amino acid composition analysis revealed enrichment in aromatic and charged residues. Hydrophobic contact densities were consistently higher than in mesophilic controls and aligned with thermophilic benchmarks. Temperature-dependent flexibility simulations showed restrained RMSF profiles, more closely resembling the thermophilic reference enzyme than to the mesophilic control. These findings are consistent with a thermophilic profile, pending experimental confirmation, and provide useful insights for the selection and engineering of GH5 cellulases for high-temperature biotechnological applications.
Instituto de Biotecnología
Fil: Farace, Pablo Daniel. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular; Argentina
Fil: Farace, Pablo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Farace, Pablo Daniel. University of Vermont. Department of Nutrition and Food Sciences; Estados Unidos
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: 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: Soria, Marcelo Abel. Universidad de Buenos Aires. Facultad de Agronomía. Cátedra de Microbiología Agrícola; 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 Lignocellulosic biomass can be converted into biofuels and other valuable bioproducts, but it must first undergo physicochemical and enzymatic degradation. Among the various enzymes involved in lignocellulose degradation, thermophilic glycoside hydrolase family 5 (GH5) cellulases have gained significant attention given their ability to sustain enzymatic activity at temperatures exceeding 60 °C. These high temperatures not only accelerate enzymatic reactions, improving reaction rates and process efficiency, but also enhance substrate solubility and reduce the risk of microbial contamination, making them highly valuable for the paper, food, feed, pharmaceutical, and biofuel industries. In this work, we identified five GH5 cellulases with predicted thermophilic properties from termite gut metagenomes and evaluated their structural features using machine-learning classification, comparative structural modeling, interatomic contact analysis, and temperature-dependent flexibility simulations. The candidates, spanning GH5 subfamilies 2, 25, 37, 39, and 40, displayed high structural confidence (pLDDT > 90) and aliphatic indices comparable to those of thermophilic references. Analysis of amino acid composition analysis revealed enrichment in aromatic and charged residues. Hydrophobic contact densities were consistently higher than in mesophilic controls and aligned with thermophilic benchmarks. Temperature-dependent flexibility simulations showed restrained RMSF profiles, more closely resembling the thermophilic reference enzyme than to the mesophilic control. These findings are consistent with a thermophilic profile, pending experimental confirmation, and provide useful insights for the selection and engineering of GH5 cellulases for high-temperature biotechnological applications.
publishDate 2026
dc.date.none.fl_str_mv 2026-06-09T10:15:58Z
2026-06-09T10:15:58Z
2026-06
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/20.500.12123/26532
https://www.tandfonline.com/doi/full/10.1080/07391102.2026.2683872
1538-0254
0739-1102
https://doi.org/10.1080/07391102.2026.2683872
url http://hdl.handle.net/20.500.12123/26532
https://www.tandfonline.com/doi/full/10.1080/07391102.2026.2683872
https://doi.org/10.1080/07391102.2026.2683872
identifier_str_mv 1538-0254
0739-1102
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 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
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
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 restrictedAccess
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 Taylor and Francis
publisher.none.fl_str_mv Taylor and Francis
dc.source.none.fl_str_mv Journal of Biomolecular Structure and Dynamics : 1-23 (Published online: 07 Jun 2026)
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
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