Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697

Autores
Piñuel, Maria Lucrecia; Breccia, Javier Dario; Guisán, J. M.; López Gallego, F.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The diglycosidase α-rhamnosyl-β-glucosidase (EC 3.2.1.168) from the fungus Acremonium sp. DSM24697 was immobilized on several agarose-based supports. Covalent multipoint immobilization onto glyoxyl-activated agarose was selected as the more stable preparation at high concentration of dimethyl sulfoxide (DMSO) and high temperature. The optimal conditions for the immobilization process involved an incubation of the enzyme with agarose beads containing 220 μmol of glyoxyl groups per gram at pH 10 and 25°C for 24 h. The hydrolysis of hesperidin carried out in 10% v/v DMSO at 60°C for 2 h reached 64.6% substrate conversion and a specific productivity of 2.40 mmol h-1 g-1. Under these conditions, the process was performed reutilizing the catalyst for up to 18 cycles, maintaining >80% of the initial activity and a constant productivity 2.96 ± 0.42 µmol-1 h-1 g-1. To the best of our knowledge, such productivity is the highest achieved for hesperetin production through an enzymatic approach.
Fil: Piñuel, Maria Lucrecia. 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: Guisán, J. M.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: López Gallego, F.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Materia
Biocatalysis
Immobilization
Rutinose
Hesperidin
Biotransformation
Flavonoids
Citrus by Products
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:11336/26743
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/26743
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697Piñuel, Maria LucreciaBreccia, Javier DarioGuisán, J. M.López Gallego, F.BiocatalysisImmobilizationRutinoseHesperidinBiotransformationFlavonoidsCitrus by Productshttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The diglycosidase α-rhamnosyl-β-glucosidase (EC 3.2.1.168) from the fungus Acremonium sp. DSM24697 was immobilized on several agarose-based supports. Covalent multipoint immobilization onto glyoxyl-activated agarose was selected as the more stable preparation at high concentration of dimethyl sulfoxide (DMSO) and high temperature. The optimal conditions for the immobilization process involved an incubation of the enzyme with agarose beads containing 220 μmol of glyoxyl groups per gram at pH 10 and 25°C for 24 h. The hydrolysis of hesperidin carried out in 10% v/v DMSO at 60°C for 2 h reached 64.6% substrate conversion and a specific productivity of 2.40 mmol h-1 g-1. Under these conditions, the process was performed reutilizing the catalyst for up to 18 cycles, maintaining >80% of the initial activity and a constant productivity 2.96 ± 0.42 µmol-1 h-1 g-1. To the best of our knowledge, such productivity is the highest achieved for hesperetin production through an enzymatic approach.Fil: Piñuel, Maria Lucrecia. 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: Guisán, J. M.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaFil: López Gallego, F.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaKarger2013-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/26743Piñuel, Maria Lucrecia; Breccia, Javier Dario; Guisán, J. M.; López Gallego, F.; Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697; Karger; Journal of Molecular Microbiology and Biotechnology; 23; 6; 5-2013; 410-4171464-18011660-2412enginfo:eu-repo/semantics/altIdentifier/doi/10.1159/000353208info:eu-repo/semantics/altIdentifier/url/https://www.karger.com/Article/Abstract/353208info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:56:30Zoai:ri.conicet.gov.ar:11336/26743instacron: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:34982025-09-03 09:56:30.91CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697
title Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697
spellingShingle Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697
Piñuel, Maria Lucrecia
Biocatalysis
Immobilization
Rutinose
Hesperidin
Biotransformation
Flavonoids
Citrus by Products
title_short Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697
title_full Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697
title_fullStr Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697
title_full_unstemmed Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697
title_sort Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697
dc.creator.none.fl_str_mv Piñuel, Maria Lucrecia
Breccia, Javier Dario
Guisán, J. M.
López Gallego, F.
author Piñuel, Maria Lucrecia
author_facet Piñuel, Maria Lucrecia
Breccia, Javier Dario
Guisán, J. M.
López Gallego, F.
author_role author
author2 Breccia, Javier Dario
Guisán, J. M.
López Gallego, F.
author2_role author
author
author
dc.subject.none.fl_str_mv Biocatalysis
Immobilization
Rutinose
Hesperidin
Biotransformation
Flavonoids
Citrus by Products
topic Biocatalysis
Immobilization
Rutinose
Hesperidin
Biotransformation
Flavonoids
Citrus by Products
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The diglycosidase α-rhamnosyl-β-glucosidase (EC 3.2.1.168) from the fungus Acremonium sp. DSM24697 was immobilized on several agarose-based supports. Covalent multipoint immobilization onto glyoxyl-activated agarose was selected as the more stable preparation at high concentration of dimethyl sulfoxide (DMSO) and high temperature. The optimal conditions for the immobilization process involved an incubation of the enzyme with agarose beads containing 220 μmol of glyoxyl groups per gram at pH 10 and 25°C for 24 h. The hydrolysis of hesperidin carried out in 10% v/v DMSO at 60°C for 2 h reached 64.6% substrate conversion and a specific productivity of 2.40 mmol h-1 g-1. Under these conditions, the process was performed reutilizing the catalyst for up to 18 cycles, maintaining >80% of the initial activity and a constant productivity 2.96 ± 0.42 µmol-1 h-1 g-1. To the best of our knowledge, such productivity is the highest achieved for hesperetin production through an enzymatic approach.
Fil: Piñuel, Maria Lucrecia. 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: Guisán, J. M.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: López Gallego, F.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
description The diglycosidase α-rhamnosyl-β-glucosidase (EC 3.2.1.168) from the fungus Acremonium sp. DSM24697 was immobilized on several agarose-based supports. Covalent multipoint immobilization onto glyoxyl-activated agarose was selected as the more stable preparation at high concentration of dimethyl sulfoxide (DMSO) and high temperature. The optimal conditions for the immobilization process involved an incubation of the enzyme with agarose beads containing 220 μmol of glyoxyl groups per gram at pH 10 and 25°C for 24 h. The hydrolysis of hesperidin carried out in 10% v/v DMSO at 60°C for 2 h reached 64.6% substrate conversion and a specific productivity of 2.40 mmol h-1 g-1. Under these conditions, the process was performed reutilizing the catalyst for up to 18 cycles, maintaining >80% of the initial activity and a constant productivity 2.96 ± 0.42 µmol-1 h-1 g-1. To the best of our knowledge, such productivity is the highest achieved for hesperetin production through an enzymatic approach.
publishDate 2013
dc.date.none.fl_str_mv 2013-05
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/11336/26743
Piñuel, Maria Lucrecia; Breccia, Javier Dario; Guisán, J. M.; López Gallego, F.; Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697; Karger; Journal of Molecular Microbiology and Biotechnology; 23; 6; 5-2013; 410-417
1464-1801
1660-2412
url http://hdl.handle.net/11336/26743
identifier_str_mv Piñuel, Maria Lucrecia; Breccia, Javier Dario; Guisán, J. M.; López Gallego, F.; Production of hesperetin using a covalently multipoint immobilized diglycosidase from Acremonium sp. DSM24697; Karger; Journal of Molecular Microbiology and Biotechnology; 23; 6; 5-2013; 410-417
1464-1801
1660-2412
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1159/000353208
info:eu-repo/semantics/altIdentifier/url/https://www.karger.com/Article/Abstract/353208
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 Karger
publisher.none.fl_str_mv Karger
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
_version_ 1842269406643617792
score 13.13397

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