Peculiarities and systematics of microbial diglycosidases, and their applications in food technology

Autores
Baglioni, Micaela; Breccia, Javier Dario; Mazzaferro, Laura
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Diglycosidases are endo-β-glucosidases that hydrolyze the heterosidic linkage of diglycoconjugates, thereby releasing in a single reaction the disaccharide and the aglycone. Plant diglycosidases belong to the glycoside hydrolase family 1 and are associated with defense mechanisms. Microbial diglycosidases exhibit higher diversity—they belong to the families 3, 5, and 55—and play a catabolic role. As diglycoconjugates are widespread in the environments, so are the microbial diglycosidases, which allow their utilization as nutritional source and carbon recycling. In the last 10 years, six microbial diglycosidases have been sequenced, and for two of them, the three-dimensional structure has been elucidated. This knowledge allowed the identification of their diverse phylogenetic origin, and gave insights into the understanding of the substrate specificity. Here, the last advances and the applications of microbial diglycosidases are reviewed. Key points: • Substrate specificity and phylogenetic relationships of diglycosidases are reviewed. • On-going and potential applications of diglycosidases are discussed.
Fil: Baglioni, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
Fil: Mazzaferro, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
Materia
HESPERIDIN
HESPERIDIN 6-O-Α-L-RHAMNOSYL-Β-D-GLUCOSIDASE
RUTIN
Β-PRIMEVEROSIDASE
Β-RUTINOSIDASE
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:11336/183447
Acceder
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spelling Peculiarities and systematics of microbial diglycosidases, and their applications in food technologyBaglioni, MicaelaBreccia, Javier DarioMazzaferro, LauraHESPERIDINHESPERIDIN 6-O-Α-L-RHAMNOSYL-Β-D-GLUCOSIDASERUTINΒ-PRIMEVEROSIDASEΒ-RUTINOSIDASEhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Diglycosidases are endo-β-glucosidases that hydrolyze the heterosidic linkage of diglycoconjugates, thereby releasing in a single reaction the disaccharide and the aglycone. Plant diglycosidases belong to the glycoside hydrolase family 1 and are associated with defense mechanisms. Microbial diglycosidases exhibit higher diversity—they belong to the families 3, 5, and 55—and play a catabolic role. As diglycoconjugates are widespread in the environments, so are the microbial diglycosidases, which allow their utilization as nutritional source and carbon recycling. In the last 10 years, six microbial diglycosidases have been sequenced, and for two of them, the three-dimensional structure has been elucidated. This knowledge allowed the identification of their diverse phylogenetic origin, and gave insights into the understanding of the substrate specificity. Here, the last advances and the applications of microbial diglycosidases are reviewed. Key points: • Substrate specificity and phylogenetic relationships of diglycosidases are reviewed. • On-going and potential applications of diglycosidases are discussed.Fil: Baglioni, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; ArgentinaFil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; ArgentinaFil: Mazzaferro, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; ArgentinaSpringer2021-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/183447Baglioni, Micaela; Breccia, Javier Dario; Mazzaferro, Laura; Peculiarities and systematics of microbial diglycosidases, and their applications in food technology; Springer; Applied Microbiology and Biotechnology; 105; 7; 4-2021; 2693-27000175-7598CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://link.springer.com/10.1007/s00253-021-11219-9info:eu-repo/semantics/altIdentifier/doi/10.1007/s00253-021-11219-9info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:16:51Zoai:ri.conicet.gov.ar:11336/183447instacron: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 10:16:52.123CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
title Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
spellingShingle Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
Baglioni, Micaela
HESPERIDIN
HESPERIDIN 6-O-Α-L-RHAMNOSYL-Β-D-GLUCOSIDASE
RUTIN
Β-PRIMEVEROSIDASE
Β-RUTINOSIDASE
title_short Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
title_full Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
title_fullStr Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
title_full_unstemmed Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
title_sort Peculiarities and systematics of microbial diglycosidases, and their applications in food technology
dc.creator.none.fl_str_mv Baglioni, Micaela
Breccia, Javier Dario
Mazzaferro, Laura
author Baglioni, Micaela
author_facet Baglioni, Micaela
Breccia, Javier Dario
Mazzaferro, Laura
author_role author
author2 Breccia, Javier Dario
Mazzaferro, Laura
author2_role author
author
dc.subject.none.fl_str_mv HESPERIDIN
HESPERIDIN 6-O-Α-L-RHAMNOSYL-Β-D-GLUCOSIDASE
RUTIN
Β-PRIMEVEROSIDASE
Β-RUTINOSIDASE
topic HESPERIDIN
HESPERIDIN 6-O-Α-L-RHAMNOSYL-Β-D-GLUCOSIDASE
RUTIN
Β-PRIMEVEROSIDASE
Β-RUTINOSIDASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Diglycosidases are endo-β-glucosidases that hydrolyze the heterosidic linkage of diglycoconjugates, thereby releasing in a single reaction the disaccharide and the aglycone. Plant diglycosidases belong to the glycoside hydrolase family 1 and are associated with defense mechanisms. Microbial diglycosidases exhibit higher diversity—they belong to the families 3, 5, and 55—and play a catabolic role. As diglycoconjugates are widespread in the environments, so are the microbial diglycosidases, which allow their utilization as nutritional source and carbon recycling. In the last 10 years, six microbial diglycosidases have been sequenced, and for two of them, the three-dimensional structure has been elucidated. This knowledge allowed the identification of their diverse phylogenetic origin, and gave insights into the understanding of the substrate specificity. Here, the last advances and the applications of microbial diglycosidases are reviewed. Key points: • Substrate specificity and phylogenetic relationships of diglycosidases are reviewed. • On-going and potential applications of diglycosidases are discussed.
Fil: Baglioni, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
Fil: Breccia, Javier Dario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
Fil: Mazzaferro, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
description Diglycosidases are endo-β-glucosidases that hydrolyze the heterosidic linkage of diglycoconjugates, thereby releasing in a single reaction the disaccharide and the aglycone. Plant diglycosidases belong to the glycoside hydrolase family 1 and are associated with defense mechanisms. Microbial diglycosidases exhibit higher diversity—they belong to the families 3, 5, and 55—and play a catabolic role. As diglycoconjugates are widespread in the environments, so are the microbial diglycosidases, which allow their utilization as nutritional source and carbon recycling. In the last 10 years, six microbial diglycosidases have been sequenced, and for two of them, the three-dimensional structure has been elucidated. This knowledge allowed the identification of their diverse phylogenetic origin, and gave insights into the understanding of the substrate specificity. Here, the last advances and the applications of microbial diglycosidases are reviewed. Key points: • Substrate specificity and phylogenetic relationships of diglycosidases are reviewed. • On-going and potential applications of diglycosidases are discussed.
publishDate 2021
dc.date.none.fl_str_mv 2021-04
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/11336/183447
Baglioni, Micaela; Breccia, Javier Dario; Mazzaferro, Laura; Peculiarities and systematics of microbial diglycosidases, and their applications in food technology; Springer; Applied Microbiology and Biotechnology; 105; 7; 4-2021; 2693-2700
0175-7598
CONICET Digital
CONICET
url http://hdl.handle.net/11336/183447
identifier_str_mv Baglioni, Micaela; Breccia, Javier Dario; Mazzaferro, Laura; Peculiarities and systematics of microbial diglycosidases, and their applications in food technology; Springer; Applied Microbiology and Biotechnology; 105; 7; 4-2021; 2693-2700
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/url/http://link.springer.com/10.1007/s00253-021-11219-9
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00253-021-11219-9
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
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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