A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A

Autores
Sánchez Arroyo, Ana; Plaza Vinuesa, Laura; Abeijon Mukdsi, Maria Claudia; de las Rivas, Blanca; Mancheño, José Miguel; Muñoz, Rosario
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The presence of ochratoxin A (OTA) in food and feed represents a serious concern since it raises severe health implications. Bacterial strains of the Acinetobacter genus hydrolyse the amide bond of OTA yielding non-toxic OTα and L-β-phenylalanine; in particular, the carboxypeptidase PJ15_1540 from Acinetobactersp. neg 1 has been identifed as an OTA-degrading enzyme. Here, we describe the ability to transform OTA of cell-free protein extracts from Acinetobacter tandoii DSM 14970T, a strain isolated from sludge plants, and also report on the finding of a new and promiscuous α/β hydrolase (ABH), with close homologs highly distributed within the Acinetobacter genus. ABH from A. tandoii (AtABH) exhibited amidase activity against OTA and OTB mycotoxins, as well as against several carboxypeptidase substrates. The predicted structure of AtABH reveals an α/β hydrolase core composed of a parallel, six-stranded β-sheet, with a large cap domain similar to the marine esterase EprEst. Further biochemical analyses of AtABH reveal that it is an efficient esterase with a similar specificity profile as EprEst. Molecular docking studies rendered a consistent OTA-binding mode. We proposed a potential procedure for preparing new OTA-degrading enzymes starting from promiscuous α/β hydrolases based on our results.
Fil: Sánchez Arroyo, Ana. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Fil: Plaza Vinuesa, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Fil: Abeijon Mukdsi, Maria Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Fil: de las Rivas, Blanca. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Fil: Mancheño, José Miguel. Consejo Superior de Investigaciones Científicas; España
Fil: Muñoz, Rosario. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Materia
AMIDOHYDROLASE
ESTERASE
MYCOTOXIN
OCHRATOXIN A
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/260683
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/260683
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin ASánchez Arroyo, AnaPlaza Vinuesa, LauraAbeijon Mukdsi, Maria Claudiade las Rivas, BlancaMancheño, José MiguelMuñoz, RosarioAMIDOHYDROLASEESTERASEMYCOTOXINOCHRATOXIN Ahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The presence of ochratoxin A (OTA) in food and feed represents a serious concern since it raises severe health implications. Bacterial strains of the Acinetobacter genus hydrolyse the amide bond of OTA yielding non-toxic OTα and L-β-phenylalanine; in particular, the carboxypeptidase PJ15_1540 from Acinetobactersp. neg 1 has been identifed as an OTA-degrading enzyme. Here, we describe the ability to transform OTA of cell-free protein extracts from Acinetobacter tandoii DSM 14970T, a strain isolated from sludge plants, and also report on the finding of a new and promiscuous α/β hydrolase (ABH), with close homologs highly distributed within the Acinetobacter genus. ABH from A. tandoii (AtABH) exhibited amidase activity against OTA and OTB mycotoxins, as well as against several carboxypeptidase substrates. The predicted structure of AtABH reveals an α/β hydrolase core composed of a parallel, six-stranded β-sheet, with a large cap domain similar to the marine esterase EprEst. Further biochemical analyses of AtABH reveal that it is an efficient esterase with a similar specificity profile as EprEst. Molecular docking studies rendered a consistent OTA-binding mode. We proposed a potential procedure for preparing new OTA-degrading enzymes starting from promiscuous α/β hydrolases based on our results.Fil: Sánchez Arroyo, Ana. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; EspañaFil: Plaza Vinuesa, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; EspañaFil: Abeijon Mukdsi, Maria Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; EspañaFil: de las Rivas, Blanca. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; EspañaFil: Mancheño, José Miguel. Consejo Superior de Investigaciones Científicas; EspañaFil: Muñoz, Rosario. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; EspañaSpringer2024-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/260683Sánchez Arroyo, Ana; Plaza Vinuesa, Laura; Abeijon Mukdsi, Maria Claudia; de las Rivas, Blanca; Mancheño, José Miguel; et al.; A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A; Springer; Applied Microbiology and Biotechnology; 108; 230; 2-2024; 1-120175-7598CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s00253-024-13073-xinfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00253-024-13073-xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:43:36Zoai:ri.conicet.gov.ar:11336/260683instacron: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:34982025-09-29 09:43:36.732CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A
title A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A
spellingShingle A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A
Sánchez Arroyo, Ana
AMIDOHYDROLASE
ESTERASE
MYCOTOXIN
OCHRATOXIN A
title_short A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A
title_full A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A
title_fullStr A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A
title_full_unstemmed A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A
title_sort A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A
dc.creator.none.fl_str_mv Sánchez Arroyo, Ana
Plaza Vinuesa, Laura
Abeijon Mukdsi, Maria Claudia
de las Rivas, Blanca
Mancheño, José Miguel
Muñoz, Rosario
author Sánchez Arroyo, Ana
author_facet Sánchez Arroyo, Ana
Plaza Vinuesa, Laura
Abeijon Mukdsi, Maria Claudia
de las Rivas, Blanca
Mancheño, José Miguel
Muñoz, Rosario
author_role author
author2 Plaza Vinuesa, Laura
Abeijon Mukdsi, Maria Claudia
de las Rivas, Blanca
Mancheño, José Miguel
Muñoz, Rosario
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv AMIDOHYDROLASE
ESTERASE
MYCOTOXIN
OCHRATOXIN A
topic AMIDOHYDROLASE
ESTERASE
MYCOTOXIN
OCHRATOXIN A
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The presence of ochratoxin A (OTA) in food and feed represents a serious concern since it raises severe health implications. Bacterial strains of the Acinetobacter genus hydrolyse the amide bond of OTA yielding non-toxic OTα and L-β-phenylalanine; in particular, the carboxypeptidase PJ15_1540 from Acinetobactersp. neg 1 has been identifed as an OTA-degrading enzyme. Here, we describe the ability to transform OTA of cell-free protein extracts from Acinetobacter tandoii DSM 14970T, a strain isolated from sludge plants, and also report on the finding of a new and promiscuous α/β hydrolase (ABH), with close homologs highly distributed within the Acinetobacter genus. ABH from A. tandoii (AtABH) exhibited amidase activity against OTA and OTB mycotoxins, as well as against several carboxypeptidase substrates. The predicted structure of AtABH reveals an α/β hydrolase core composed of a parallel, six-stranded β-sheet, with a large cap domain similar to the marine esterase EprEst. Further biochemical analyses of AtABH reveal that it is an efficient esterase with a similar specificity profile as EprEst. Molecular docking studies rendered a consistent OTA-binding mode. We proposed a potential procedure for preparing new OTA-degrading enzymes starting from promiscuous α/β hydrolases based on our results.
Fil: Sánchez Arroyo, Ana. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Fil: Plaza Vinuesa, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Fil: Abeijon Mukdsi, Maria Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Fil: de las Rivas, Blanca. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
Fil: Mancheño, José Miguel. Consejo Superior de Investigaciones Científicas; España
Fil: Muñoz, Rosario. Consejo Superior de Investigaciones Científicas. Instituto de Ciencia y Tecnologia de Alimentos y Nutrición; España
description The presence of ochratoxin A (OTA) in food and feed represents a serious concern since it raises severe health implications. Bacterial strains of the Acinetobacter genus hydrolyse the amide bond of OTA yielding non-toxic OTα and L-β-phenylalanine; in particular, the carboxypeptidase PJ15_1540 from Acinetobactersp. neg 1 has been identifed as an OTA-degrading enzyme. Here, we describe the ability to transform OTA of cell-free protein extracts from Acinetobacter tandoii DSM 14970T, a strain isolated from sludge plants, and also report on the finding of a new and promiscuous α/β hydrolase (ABH), with close homologs highly distributed within the Acinetobacter genus. ABH from A. tandoii (AtABH) exhibited amidase activity against OTA and OTB mycotoxins, as well as against several carboxypeptidase substrates. The predicted structure of AtABH reveals an α/β hydrolase core composed of a parallel, six-stranded β-sheet, with a large cap domain similar to the marine esterase EprEst. Further biochemical analyses of AtABH reveal that it is an efficient esterase with a similar specificity profile as EprEst. Molecular docking studies rendered a consistent OTA-binding mode. We proposed a potential procedure for preparing new OTA-degrading enzymes starting from promiscuous α/β hydrolases based on our results.
publishDate 2024
dc.date.none.fl_str_mv 2024-02
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/11336/260683
Sánchez Arroyo, Ana; Plaza Vinuesa, Laura; Abeijon Mukdsi, Maria Claudia; de las Rivas, Blanca; Mancheño, José Miguel; et al.; A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A; Springer; Applied Microbiology and Biotechnology; 108; 230; 2-2024; 1-12
0175-7598
CONICET Digital
CONICET
url http://hdl.handle.net/11336/260683
identifier_str_mv Sánchez Arroyo, Ana; Plaza Vinuesa, Laura; Abeijon Mukdsi, Maria Claudia; de las Rivas, Blanca; Mancheño, José Miguel; et al.; A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 T inactivates the mycotoxin ochratoxin A; Springer; Applied Microbiology and Biotechnology; 108; 230; 2-2024; 1-12
0175-7598
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s00253-024-13073-x
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s00253-024-13073-x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
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 13.070432

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