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

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 sulfox...

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Detalles Bibliográficos
Autores: Piñuel, Maria Lucrecia, Breccia, Javier Dario, Guisán, J. M., López Gallego, F.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2013
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/26743
Acceso en línea:http://hdl.handle.net/11336/26743
Access Level:acceso abierto
Palabra clave:Biocatalysis
Immobilization
Rutinose
Hesperidin
Biotransformation
Flavonoids
Citrus by Products
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
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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 Técnicas2024-05-08T13:54:22Zoai: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:34982024-05-08 13:54:23.08CONICET 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
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
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
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
topic Biocatalysis
Immobilization
Rutinose
Hesperidin
Biotransformation
Flavonoids
Citrus by Products
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
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
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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 15,811543

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