Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system

Autores
Martini, María Carla; Berini, Francesca; Ausec, Luka; Casciello, Carmine; Vacca, Carolina; Pistorio, Mariano; Lagares, Antonio; Mandic Mulec, Ines; Marinelli, Flavia; del Papa, Maria Florencia
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Research background. In recent decades, laccases (p-diphenol-dioxygen oxidoreductases; EC 1.10.3.2) have attracted the attention of researchers due to their wide range of biotechnological and industrial applications. Laccases can oxidize a variety of organic and inorganic compounds, making them suitable as biocatalysts in biotechnological processes. Even though the most traditionally used laccases in the industry are of fungal origin, bacterial laccases have shown an enormous potential given their ability to act on several substrates and in multiple conditions. The present study aims to characterize a plasmid-encoded laccase-like multicopper oxidase (LMCO) from Ochrobactrum sp. BF15, a bacterial strain previously isolated from polluted soil. Experimental approach. We used in silico profile hidden Markov models to identify novel laccase-like genes in Ochrobactrum sp. BF15. For laccase characterization, we performed heterologous expression in Escherichia coli, purification and activity measurement on typical laccase substrates. Results and conclusions. Profile hidden Markov models allowed us to identify a novel LMCO, named Lac80. In silico analysis of Lac80 revealed the presence of three conserved copper oxidase domains characteristic of three-domain laccases. We successfully expressed Lac80 heterologously in E. coli, allowing us to purify the protein for further activity evaluation. Of thirteen typical laccase substrates tested, Lac80 showed lower activity on 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), pyrocatechol, pyrogallol and vanillic acid, and higher activity on 2,6-dimethoxyphenol. Novelty and scientific contribution. Our results show Lac80 as a promising laccase for use in industrial applications. The present work shows the relevance of bacterial laccases and highlights the importance of environmental plasmids as valuable sources of new genes encoding enzymes with potential use in biotechnological processes.
Fil: Martini, María Carla. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Berini, Francesca. Università Degli Studi Dell'insubria; Italia
Fil: Ausec, Luka. Univerza V Ljubljani; Eslovenia
Fil: Casciello, Carmine. Università Degli Studi Dell'insubria; Italia
Fil: Vacca, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Pistorio, Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Lagares, Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Mandic Mulec, Ines. Univerza V Ljubljani; Eslovenia
Fil: Marinelli, Flavia. Università Degli Studi Dell'insubria; Italia
Fil: del Papa, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Materia
BIODEGRADATION
BIOPURIFICATION SYSTEM
HETEROLOGOUS EXPRESSION
LACCASE-LIKE MULTICOPPER OXIDASES
OCHROBACTRUM
PLASMID
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:11336/181562
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/181562
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification systemMartini, María CarlaBerini, FrancescaAusec, LukaCasciello, CarmineVacca, CarolinaPistorio, MarianoLagares, AntonioMandic Mulec, InesMarinelli, Flaviadel Papa, Maria FlorenciaBIODEGRADATIONBIOPURIFICATION SYSTEMHETEROLOGOUS EXPRESSIONLACCASE-LIKE MULTICOPPER OXIDASESOCHROBACTRUMPLASMIDhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Research background. In recent decades, laccases (p-diphenol-dioxygen oxidoreductases; EC 1.10.3.2) have attracted the attention of researchers due to their wide range of biotechnological and industrial applications. Laccases can oxidize a variety of organic and inorganic compounds, making them suitable as biocatalysts in biotechnological processes. Even though the most traditionally used laccases in the industry are of fungal origin, bacterial laccases have shown an enormous potential given their ability to act on several substrates and in multiple conditions. The present study aims to characterize a plasmid-encoded laccase-like multicopper oxidase (LMCO) from Ochrobactrum sp. BF15, a bacterial strain previously isolated from polluted soil. Experimental approach. We used in silico profile hidden Markov models to identify novel laccase-like genes in Ochrobactrum sp. BF15. For laccase characterization, we performed heterologous expression in Escherichia coli, purification and activity measurement on typical laccase substrates. Results and conclusions. Profile hidden Markov models allowed us to identify a novel LMCO, named Lac80. In silico analysis of Lac80 revealed the presence of three conserved copper oxidase domains characteristic of three-domain laccases. We successfully expressed Lac80 heterologously in E. coli, allowing us to purify the protein for further activity evaluation. Of thirteen typical laccase substrates tested, Lac80 showed lower activity on 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), pyrocatechol, pyrogallol and vanillic acid, and higher activity on 2,6-dimethoxyphenol. Novelty and scientific contribution. Our results show Lac80 as a promising laccase for use in industrial applications. The present work shows the relevance of bacterial laccases and highlights the importance of environmental plasmids as valuable sources of new genes encoding enzymes with potential use in biotechnological processes.Fil: Martini, María Carla. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaFil: Berini, Francesca. Università Degli Studi Dell'insubria; ItaliaFil: Ausec, Luka. Univerza V Ljubljani; EsloveniaFil: Casciello, Carmine. Università Degli Studi Dell'insubria; ItaliaFil: Vacca, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaFil: Pistorio, Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaFil: Lagares, Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaFil: Mandic Mulec, Ines. Univerza V Ljubljani; EsloveniaFil: Marinelli, Flavia. Università Degli Studi Dell'insubria; ItaliaFil: del Papa, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; ArgentinaUniversity of Zagreb. Faculty of Food Technology and Biotechnology2021-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/181562Martini, María Carla; Berini, Francesca; Ausec, Luka; Casciello, Carmine; Vacca, Carolina; et al.; Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system; University of Zagreb. Faculty of Food Technology and Biotechnology; Food Technology and Biotechnology; 59; 4; 10-2021; 519-5291330-98621334-2606CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://ftb.com.hr/archives/187-volume-59-issue-no-4/1740-identification-and-characterization-of-a-novel-plasmid-encoded-laccase-like-multicopper-oxidase-from-ochrobactrum-sp-bf15-isolated-from-an-on-farm-bio-purification-systeminfo:eu-repo/semantics/altIdentifier/doi/10.17113/ftb.59.04.21.7253info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:43:20Zoai:ri.conicet.gov.ar:11336/181562instacron: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:34982025-10-15 15:43:20.8CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system
title Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system
spellingShingle Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system
Martini, María Carla
BIODEGRADATION
BIOPURIFICATION SYSTEM
HETEROLOGOUS EXPRESSION
LACCASE-LIKE MULTICOPPER OXIDASES
OCHROBACTRUM
PLASMID
title_short Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system
title_full Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system
title_fullStr Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system
title_full_unstemmed Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system
title_sort Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system
dc.creator.none.fl_str_mv Martini, María Carla
Berini, Francesca
Ausec, Luka
Casciello, Carmine
Vacca, Carolina
Pistorio, Mariano
Lagares, Antonio
Mandic Mulec, Ines
Marinelli, Flavia
del Papa, Maria Florencia
author Martini, María Carla
author_facet Martini, María Carla
Berini, Francesca
Ausec, Luka
Casciello, Carmine
Vacca, Carolina
Pistorio, Mariano
Lagares, Antonio
Mandic Mulec, Ines
Marinelli, Flavia
del Papa, Maria Florencia
author_role author
author2 Berini, Francesca
Ausec, Luka
Casciello, Carmine
Vacca, Carolina
Pistorio, Mariano
Lagares, Antonio
Mandic Mulec, Ines
Marinelli, Flavia
del Papa, Maria Florencia
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BIODEGRADATION
BIOPURIFICATION SYSTEM
HETEROLOGOUS EXPRESSION
LACCASE-LIKE MULTICOPPER OXIDASES
OCHROBACTRUM
PLASMID
topic BIODEGRADATION
BIOPURIFICATION SYSTEM
HETEROLOGOUS EXPRESSION
LACCASE-LIKE MULTICOPPER OXIDASES
OCHROBACTRUM
PLASMID
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Research background. In recent decades, laccases (p-diphenol-dioxygen oxidoreductases; EC 1.10.3.2) have attracted the attention of researchers due to their wide range of biotechnological and industrial applications. Laccases can oxidize a variety of organic and inorganic compounds, making them suitable as biocatalysts in biotechnological processes. Even though the most traditionally used laccases in the industry are of fungal origin, bacterial laccases have shown an enormous potential given their ability to act on several substrates and in multiple conditions. The present study aims to characterize a plasmid-encoded laccase-like multicopper oxidase (LMCO) from Ochrobactrum sp. BF15, a bacterial strain previously isolated from polluted soil. Experimental approach. We used in silico profile hidden Markov models to identify novel laccase-like genes in Ochrobactrum sp. BF15. For laccase characterization, we performed heterologous expression in Escherichia coli, purification and activity measurement on typical laccase substrates. Results and conclusions. Profile hidden Markov models allowed us to identify a novel LMCO, named Lac80. In silico analysis of Lac80 revealed the presence of three conserved copper oxidase domains characteristic of three-domain laccases. We successfully expressed Lac80 heterologously in E. coli, allowing us to purify the protein for further activity evaluation. Of thirteen typical laccase substrates tested, Lac80 showed lower activity on 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), pyrocatechol, pyrogallol and vanillic acid, and higher activity on 2,6-dimethoxyphenol. Novelty and scientific contribution. Our results show Lac80 as a promising laccase for use in industrial applications. The present work shows the relevance of bacterial laccases and highlights the importance of environmental plasmids as valuable sources of new genes encoding enzymes with potential use in biotechnological processes.
Fil: Martini, María Carla. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Berini, Francesca. Università Degli Studi Dell'insubria; Italia
Fil: Ausec, Luka. Univerza V Ljubljani; Eslovenia
Fil: Casciello, Carmine. Università Degli Studi Dell'insubria; Italia
Fil: Vacca, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Pistorio, Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Lagares, Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
Fil: Mandic Mulec, Ines. Univerza V Ljubljani; Eslovenia
Fil: Marinelli, Flavia. Università Degli Studi Dell'insubria; Italia
Fil: del Papa, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina
description Research background. In recent decades, laccases (p-diphenol-dioxygen oxidoreductases; EC 1.10.3.2) have attracted the attention of researchers due to their wide range of biotechnological and industrial applications. Laccases can oxidize a variety of organic and inorganic compounds, making them suitable as biocatalysts in biotechnological processes. Even though the most traditionally used laccases in the industry are of fungal origin, bacterial laccases have shown an enormous potential given their ability to act on several substrates and in multiple conditions. The present study aims to characterize a plasmid-encoded laccase-like multicopper oxidase (LMCO) from Ochrobactrum sp. BF15, a bacterial strain previously isolated from polluted soil. Experimental approach. We used in silico profile hidden Markov models to identify novel laccase-like genes in Ochrobactrum sp. BF15. For laccase characterization, we performed heterologous expression in Escherichia coli, purification and activity measurement on typical laccase substrates. Results and conclusions. Profile hidden Markov models allowed us to identify a novel LMCO, named Lac80. In silico analysis of Lac80 revealed the presence of three conserved copper oxidase domains characteristic of three-domain laccases. We successfully expressed Lac80 heterologously in E. coli, allowing us to purify the protein for further activity evaluation. Of thirteen typical laccase substrates tested, Lac80 showed lower activity on 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), pyrocatechol, pyrogallol and vanillic acid, and higher activity on 2,6-dimethoxyphenol. Novelty and scientific contribution. Our results show Lac80 as a promising laccase for use in industrial applications. The present work shows the relevance of bacterial laccases and highlights the importance of environmental plasmids as valuable sources of new genes encoding enzymes with potential use in biotechnological processes.
publishDate 2021
dc.date.none.fl_str_mv 2021-10
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/11336/181562
Martini, María Carla; Berini, Francesca; Ausec, Luka; Casciello, Carmine; Vacca, Carolina; et al.; Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system; University of Zagreb. Faculty of Food Technology and Biotechnology; Food Technology and Biotechnology; 59; 4; 10-2021; 519-529
1330-9862
1334-2606
CONICET Digital
CONICET
url http://hdl.handle.net/11336/181562
identifier_str_mv Martini, María Carla; Berini, Francesca; Ausec, Luka; Casciello, Carmine; Vacca, Carolina; et al.; Identification and characterization of a novel plasmid-encoded laccase-like multicopper oxidase from Ochrobactrum sp. BF15 isolated from an on-farm bio-purification system; University of Zagreb. Faculty of Food Technology and Biotechnology; Food Technology and Biotechnology; 59; 4; 10-2021; 519-529
1330-9862
1334-2606
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://ftb.com.hr/archives/187-volume-59-issue-no-4/1740-identification-and-characterization-of-a-novel-plasmid-encoded-laccase-like-multicopper-oxidase-from-ochrobactrum-sp-bf15-isolated-from-an-on-farm-bio-purification-system
info:eu-repo/semantics/altIdentifier/doi/10.17113/ftb.59.04.21.7253
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
dc.publisher.none.fl_str_mv University of Zagreb. Faculty of Food Technology and Biotechnology
publisher.none.fl_str_mv University of Zagreb. Faculty of Food Technology and Biotechnology
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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