Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277

Autores
Barengo, Marcela Paola; Amerio, Natalia Soledad; Bich, Gustavo Angel; Zapata, Pedro Dario; Castrillo, María Lorena
Año de publicación
2026
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fungi of the genus Escovopsis are specialised mycoparasites of the mutualistic fungus Leucoagaricus gongylophorus, cultivated by leaf-cutter ants. Harnessing this natural antagonism represents a promising and environmentally friendly strategy for the indirect biological control of these agroforestry pests. This study optimised and characterised the production of cell wall-degrading enzymes (CWDEs), key effectors in the degradation of the host, by the Escovopsis primorosea LBM 277 strain. Using submergedfermentation and Box–Behnken response surface methodology (RSM-BBD), we identified optimal culture conditions, including the concentrations of carbon and nitrogen sources, initial pH and inoculum size. Under optimised conditions, protease, β-1,3- glucanase and chitinase activities increased by 3.5-, 6.7- and 6.8-fold, respectively. The enzymes remained active for at least 30 days at room temperature and in the pH range 4–6, resembling the microenvironment of ant fungal gardens. Zymographic analysis revealed one isoform of protease, one of β-1,3-glucanase and two chitinase isoenzymes. This is the first report combining RSM-based optimization with biochemical profiling of CWDEs in Escovopsis. These findings highlight the need for further functional assays to validate the role of these enzymes in the ant–symbiont fungus–mycoparasite interaction.
Fil: Barengo, Marcela Paola. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
Fil: Amerio, Natalia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina
Fil: Bich, Gustavo Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina
Fil: Zapata, Pedro Dario. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
Fil: Castrillo, María Lorena. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
Materia
chitinases
leaf-cutter ants
mycoparasitism
proteases
sugmerged fermentation
B-1,3-glucanases
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/289999
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/289999
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277Barengo, Marcela PaolaAmerio, Natalia SoledadBich, Gustavo AngelZapata, Pedro DarioCastrillo, María Lorenachitinasesleaf-cutter antsmycoparasitismproteasessugmerged fermentationB-1,3-glucanaseshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Fungi of the genus Escovopsis are specialised mycoparasites of the mutualistic fungus Leucoagaricus gongylophorus, cultivated by leaf-cutter ants. Harnessing this natural antagonism represents a promising and environmentally friendly strategy for the indirect biological control of these agroforestry pests. This study optimised and characterised the production of cell wall-degrading enzymes (CWDEs), key effectors in the degradation of the host, by the Escovopsis primorosea LBM 277 strain. Using submergedfermentation and Box–Behnken response surface methodology (RSM-BBD), we identified optimal culture conditions, including the concentrations of carbon and nitrogen sources, initial pH and inoculum size. Under optimised conditions, protease, β-1,3- glucanase and chitinase activities increased by 3.5-, 6.7- and 6.8-fold, respectively. The enzymes remained active for at least 30 days at room temperature and in the pH range 4–6, resembling the microenvironment of ant fungal gardens. Zymographic analysis revealed one isoform of protease, one of β-1,3-glucanase and two chitinase isoenzymes. This is the first report combining RSM-based optimization with biochemical profiling of CWDEs in Escovopsis. These findings highlight the need for further functional assays to validate the role of these enzymes in the ant–symbiont fungus–mycoparasite interaction.Fil: Barengo, Marcela Paola. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; ArgentinaFil: Amerio, Natalia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; ArgentinaFil: Bich, Gustavo Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; ArgentinaFil: Zapata, Pedro Dario. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; ArgentinaFil: Castrillo, María Lorena. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; ArgentinaJohn Wiley & Sons2026-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/289999Barengo, Marcela Paola; Amerio, Natalia Soledad; Bich, Gustavo Angel; Zapata, Pedro Dario; Castrillo, María Lorena; Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277; John Wiley & Sons; Environmental Microbiology Reports; 18; 2; 3-2026; 1-161758-2229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://sfamjournals.onlinelibrary.wiley.com/doi/10.1111/1758-2229.70271info:eu-repo/semantics/altIdentifier/doi/10.1111/1758-2229.70271info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-08-25T14:49:24Zoai:ri.conicet.gov.ar:11336/289999instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-08-25 14:49:24.298CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277
title Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277
spellingShingle Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277
Barengo, Marcela Paola
chitinases
leaf-cutter ants
mycoparasitism
proteases
sugmerged fermentation
B-1,3-glucanases
title_short Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277
title_full Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277
title_fullStr Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277
title_full_unstemmed Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277
title_sort Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277
dc.creator.none.fl_str_mv Barengo, Marcela Paola
Amerio, Natalia Soledad
Bich, Gustavo Angel
Zapata, Pedro Dario
Castrillo, María Lorena
author Barengo, Marcela Paola
author_facet Barengo, Marcela Paola
Amerio, Natalia Soledad
Bich, Gustavo Angel
Zapata, Pedro Dario
Castrillo, María Lorena
author_role author
author2 Amerio, Natalia Soledad
Bich, Gustavo Angel
Zapata, Pedro Dario
Castrillo, María Lorena
author2_role author
author
author
author
dc.subject.none.fl_str_mv chitinases
leaf-cutter ants
mycoparasitism
proteases
sugmerged fermentation
B-1,3-glucanases
topic chitinases
leaf-cutter ants
mycoparasitism
proteases
sugmerged fermentation
B-1,3-glucanases
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Fungi of the genus Escovopsis are specialised mycoparasites of the mutualistic fungus Leucoagaricus gongylophorus, cultivated by leaf-cutter ants. Harnessing this natural antagonism represents a promising and environmentally friendly strategy for the indirect biological control of these agroforestry pests. This study optimised and characterised the production of cell wall-degrading enzymes (CWDEs), key effectors in the degradation of the host, by the Escovopsis primorosea LBM 277 strain. Using submergedfermentation and Box–Behnken response surface methodology (RSM-BBD), we identified optimal culture conditions, including the concentrations of carbon and nitrogen sources, initial pH and inoculum size. Under optimised conditions, protease, β-1,3- glucanase and chitinase activities increased by 3.5-, 6.7- and 6.8-fold, respectively. The enzymes remained active for at least 30 days at room temperature and in the pH range 4–6, resembling the microenvironment of ant fungal gardens. Zymographic analysis revealed one isoform of protease, one of β-1,3-glucanase and two chitinase isoenzymes. This is the first report combining RSM-based optimization with biochemical profiling of CWDEs in Escovopsis. These findings highlight the need for further functional assays to validate the role of these enzymes in the ant–symbiont fungus–mycoparasite interaction.
Fil: Barengo, Marcela Paola. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
Fil: Amerio, Natalia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina
Fil: Bich, Gustavo Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina
Fil: Zapata, Pedro Dario. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
Fil: Castrillo, María Lorena. Universidad Nacional de Misiones. Facultad de Ciencias Exactas Químicas y Naturales. Departamento de Bioquímica Clínica. Laboratorio de Biotecnología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste; Argentina
description Fungi of the genus Escovopsis are specialised mycoparasites of the mutualistic fungus Leucoagaricus gongylophorus, cultivated by leaf-cutter ants. Harnessing this natural antagonism represents a promising and environmentally friendly strategy for the indirect biological control of these agroforestry pests. This study optimised and characterised the production of cell wall-degrading enzymes (CWDEs), key effectors in the degradation of the host, by the Escovopsis primorosea LBM 277 strain. Using submergedfermentation and Box–Behnken response surface methodology (RSM-BBD), we identified optimal culture conditions, including the concentrations of carbon and nitrogen sources, initial pH and inoculum size. Under optimised conditions, protease, β-1,3- glucanase and chitinase activities increased by 3.5-, 6.7- and 6.8-fold, respectively. The enzymes remained active for at least 30 days at room temperature and in the pH range 4–6, resembling the microenvironment of ant fungal gardens. Zymographic analysis revealed one isoform of protease, one of β-1,3-glucanase and two chitinase isoenzymes. This is the first report combining RSM-based optimization with biochemical profiling of CWDEs in Escovopsis. These findings highlight the need for further functional assays to validate the role of these enzymes in the ant–symbiont fungus–mycoparasite interaction.
publishDate 2026
dc.date.none.fl_str_mv 2026-03
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/11336/289999
Barengo, Marcela Paola; Amerio, Natalia Soledad; Bich, Gustavo Angel; Zapata, Pedro Dario; Castrillo, María Lorena; Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277; John Wiley & Sons; Environmental Microbiology Reports; 18; 2; 3-2026; 1-16
1758-2229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/289999
identifier_str_mv Barengo, Marcela Paola; Amerio, Natalia Soledad; Bich, Gustavo Angel; Zapata, Pedro Dario; Castrillo, María Lorena; Towards a Novel Biocontrol Strategy: High Performance of Optimised Cell Wall‐Degrading Enzymes Secreted by Escovopsis primorosea LBM 277; John Wiley & Sons; Environmental Microbiology Reports; 18; 2; 3-2026; 1-16
1758-2229
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://sfamjournals.onlinelibrary.wiley.com/doi/10.1111/1758-2229.70271
info:eu-repo/semantics/altIdentifier/doi/10.1111/1758-2229.70271
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons
publisher.none.fl_str_mv John Wiley & Sons
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.265058

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