Functional and biotechnological insights into diglycosidases

Autores
Mazzaferro, Laura; Breccia, Javier Dario
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
β-Glucosidases are reported to act in an exo manner and so are unable to hydrolyze the bond if another sugar is attached to a non-reducing terminus of glucose. However, endo-β-glucosidases recognizing the heterosidic linkage have been known to plant physiologists for eight decades, although they have been described in detail only recently. Because of the ability of these enzymes to split off a disaccharide they were named disaccharide-specific glycosidases or 'diglycosidases'. In contrast to the sequential mechanism of two monoglycosidases, the transformation of some secondary metabolites in one step was reported as responsible for the production of toxic compounds involved in plant defense mechanisms against herbivores, such as hydrogen cyanide. The current focus of interest is on the application of their unique substrate specificity for biotransformation of plant-based foods. Four activities have been described and characterized so far, recognizing the following disaccharidic sugar moieties: primeverose, acuminose, rutinose and vicianose. Moreover, three of these proteins have been fully sequenced and mutants of one of them constructed by site-directed mutagenesis, in order to elaborate the molecular basis of substrate recognition. The present paper reviews the role of these enzymes in plant and filamentous fungi, as well as their prospects for technological applications.
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
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
Materia
Α-Rhamnosyl-Β-Glucosidase
Β-Primeverosidase
Β-Rutinosidase
Furcatin Hydrolase
Vicianin Hydrolase
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:11336/81616
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Functional and biotechnological insights into diglycosidasesMazzaferro, LauraBreccia, Javier DarioΑ-Rhamnosyl-Β-GlucosidaseΒ-PrimeverosidaseΒ-RutinosidaseFurcatin HydrolaseVicianin Hydrolasehttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2β-Glucosidases are reported to act in an exo manner and so are unable to hydrolyze the bond if another sugar is attached to a non-reducing terminus of glucose. However, endo-β-glucosidases recognizing the heterosidic linkage have been known to plant physiologists for eight decades, although they have been described in detail only recently. Because of the ability of these enzymes to split off a disaccharide they were named disaccharide-specific glycosidases or 'diglycosidases'. In contrast to the sequential mechanism of two monoglycosidases, the transformation of some secondary metabolites in one step was reported as responsible for the production of toxic compounds involved in plant defense mechanisms against herbivores, such as hydrogen cyanide. The current focus of interest is on the application of their unique substrate specificity for biotransformation of plant-based foods. Four activities have been described and characterized so far, recognizing the following disaccharidic sugar moieties: primeverose, acuminose, rutinose and vicianose. Moreover, three of these proteins have been fully sequenced and mutants of one of them constructed by site-directed mutagenesis, in order to elaborate the molecular basis of substrate recognition. The present paper reviews the role of these enzymes in plant and filamentous fungi, as well as their prospects for technological applications.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; 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; ArgentinaTaylor & Francis Ltd2011-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/81616Mazzaferro, Laura; Breccia, Javier Dario; Functional and biotechnological insights into diglycosidases; Taylor & Francis Ltd; Biocatalysis and Biotransformation; 29; 4; 8-2011; 103-1121024-2422CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3109/10242422.2011.594882info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.3109/10242422.2011.594882info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:48:09Zoai:ri.conicet.gov.ar:11336/81616instacron: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 09:48:09.557CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Functional and biotechnological insights into diglycosidases
title Functional and biotechnological insights into diglycosidases
spellingShingle Functional and biotechnological insights into diglycosidases
Mazzaferro, Laura
Α-Rhamnosyl-Β-Glucosidase
Β-Primeverosidase
Β-Rutinosidase
Furcatin Hydrolase
Vicianin Hydrolase
title_short Functional and biotechnological insights into diglycosidases
title_full Functional and biotechnological insights into diglycosidases
title_fullStr Functional and biotechnological insights into diglycosidases
title_full_unstemmed Functional and biotechnological insights into diglycosidases
title_sort Functional and biotechnological insights into diglycosidases
dc.creator.none.fl_str_mv Mazzaferro, Laura
Breccia, Javier Dario
author Mazzaferro, Laura
author_facet Mazzaferro, Laura
Breccia, Javier Dario
author_role author
author2 Breccia, Javier Dario
author2_role author
dc.subject.none.fl_str_mv Α-Rhamnosyl-Β-Glucosidase
Β-Primeverosidase
Β-Rutinosidase
Furcatin Hydrolase
Vicianin Hydrolase
topic Α-Rhamnosyl-Β-Glucosidase
Β-Primeverosidase
Β-Rutinosidase
Furcatin Hydrolase
Vicianin Hydrolase
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv β-Glucosidases are reported to act in an exo manner and so are unable to hydrolyze the bond if another sugar is attached to a non-reducing terminus of glucose. However, endo-β-glucosidases recognizing the heterosidic linkage have been known to plant physiologists for eight decades, although they have been described in detail only recently. Because of the ability of these enzymes to split off a disaccharide they were named disaccharide-specific glycosidases or 'diglycosidases'. In contrast to the sequential mechanism of two monoglycosidases, the transformation of some secondary metabolites in one step was reported as responsible for the production of toxic compounds involved in plant defense mechanisms against herbivores, such as hydrogen cyanide. The current focus of interest is on the application of their unique substrate specificity for biotransformation of plant-based foods. Four activities have been described and characterized so far, recognizing the following disaccharidic sugar moieties: primeverose, acuminose, rutinose and vicianose. Moreover, three of these proteins have been fully sequenced and mutants of one of them constructed by site-directed mutagenesis, in order to elaborate the molecular basis of substrate recognition. The present paper reviews the role of these enzymes in plant and filamentous fungi, as well as their prospects for technological applications.
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
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
description β-Glucosidases are reported to act in an exo manner and so are unable to hydrolyze the bond if another sugar is attached to a non-reducing terminus of glucose. However, endo-β-glucosidases recognizing the heterosidic linkage have been known to plant physiologists for eight decades, although they have been described in detail only recently. Because of the ability of these enzymes to split off a disaccharide they were named disaccharide-specific glycosidases or 'diglycosidases'. In contrast to the sequential mechanism of two monoglycosidases, the transformation of some secondary metabolites in one step was reported as responsible for the production of toxic compounds involved in plant defense mechanisms against herbivores, such as hydrogen cyanide. The current focus of interest is on the application of their unique substrate specificity for biotransformation of plant-based foods. Four activities have been described and characterized so far, recognizing the following disaccharidic sugar moieties: primeverose, acuminose, rutinose and vicianose. Moreover, three of these proteins have been fully sequenced and mutants of one of them constructed by site-directed mutagenesis, in order to elaborate the molecular basis of substrate recognition. The present paper reviews the role of these enzymes in plant and filamentous fungi, as well as their prospects for technological applications.
publishDate 2011
dc.date.none.fl_str_mv 2011-08
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/11336/81616
Mazzaferro, Laura; Breccia, Javier Dario; Functional and biotechnological insights into diglycosidases; Taylor & Francis Ltd; Biocatalysis and Biotransformation; 29; 4; 8-2011; 103-112
1024-2422
CONICET Digital
CONICET
url http://hdl.handle.net/11336/81616
identifier_str_mv Mazzaferro, Laura; Breccia, Javier Dario; Functional and biotechnological insights into diglycosidases; Taylor & Francis Ltd; Biocatalysis and Biotransformation; 29; 4; 8-2011; 103-112
1024-2422
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3109/10242422.2011.594882
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.3109/10242422.2011.594882
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 Taylor & Francis Ltd
publisher.none.fl_str_mv Taylor & Francis Ltd
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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