A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking

Autores
Alvarenga, Adriana Elizabet; Romero, Cintia Mariana; Castro, Guillermo Raúl
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The production of monoglycosylated flavonoids by α-l-rhamnosidases (EC 3.2.1.40) is an interesting development in biocatalysis. Applications of rhamnosidases in industry include removal of bitterness caused by naringin from citrus juices. In the present work, a psychrotolerant bacterial strain with α-l-rhamnosidase activity was isolated. The α-l-rhamnosidase was found to be able to degrade naringin and was purified and characterized. The α-l-rhamnosidase from Brevundimonas sp. Ci19 was able to release both rhamnose and prunin from naringin. The enzyme was partially purified with a performance of 2.7-fold purification. The α-l-rhamnosidase showed an optimum pH between 6.00 and 7.00 with substantial residual activity at pH 5.00 (85.3 %). The optimum temperature was between 20 and 37 °C. The enzyme showed activation in the presence of Ca2+ and Cd2+ ions and at a high ethanol concentration level (10 % v/v). Activity was found for β-d-glucosidase (EC 3.2.1.21) in the partially purified extract, but it was inactive in the acid pH region. This result indicates the potential for inactivation of β-d-glucosidase along with the high level of α-l-rhamnosidase activity necessary for the production of flavonoid glycosides. The α-l-rhamnosidase from Brevundimonas sp. Ci19 showed interesting properties for potential use not only in the citrus juice industry but also in winemaking.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Química
α-l-rhamnosidase
β-d-glucosidase
Brevundimonas sp
Naringin
Purification
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/143732

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network_name_str SEDICI (UNLP)
spelling A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemakingAlvarenga, Adriana ElizabetRomero, Cintia MarianaCastro, Guillermo RaúlQuímicaα-l-rhamnosidaseβ-d-glucosidaseBrevundimonas spNaringinPurificationThe production of monoglycosylated flavonoids by α-l-rhamnosidases (EC 3.2.1.40) is an interesting development in biocatalysis. Applications of rhamnosidases in industry include removal of bitterness caused by naringin from citrus juices. In the present work, a psychrotolerant bacterial strain with α-l-rhamnosidase activity was isolated. The α-l-rhamnosidase was found to be able to degrade naringin and was purified and characterized. The α-l-rhamnosidase from Brevundimonas sp. Ci19 was able to release both rhamnose and prunin from naringin. The enzyme was partially purified with a performance of 2.7-fold purification. The α-l-rhamnosidase showed an optimum pH between 6.00 and 7.00 with substantial residual activity at pH 5.00 (85.3 %). The optimum temperature was between 20 and 37 °C. The enzyme showed activation in the presence of Ca2+ and Cd2+ ions and at a high ethanol concentration level (10 % v/v). Activity was found for β-d-glucosidase (EC 3.2.1.21) in the partially purified extract, but it was inactive in the acid pH region. This result indicates the potential for inactivation of β-d-glucosidase along with the high level of α-l-rhamnosidase activity necessary for the production of flavonoid glycosides. The α-l-rhamnosidase from Brevundimonas sp. Ci19 showed interesting properties for potential use not only in the citrus juice industry but also in winemaking.Centro de Investigación y Desarrollo en Fermentaciones Industriales2013-08-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf977-985http://sedici.unlp.edu.ar/handle/10915/143732enginfo:eu-repo/semantics/altIdentifier/issn/1438-2377info:eu-repo/semantics/altIdentifier/issn/1438-2385info:eu-repo/semantics/altIdentifier/doi/10.1007/s00217-013-2074-yinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:32:17Zoai:sedici.unlp.edu.ar:10915/143732Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:18.08SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking
title A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking
spellingShingle A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking
Alvarenga, Adriana Elizabet
Química
α-l-rhamnosidase
β-d-glucosidase
Brevundimonas sp
Naringin
Purification
title_short A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking
title_full A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking
title_fullStr A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking
title_full_unstemmed A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking
title_sort A novel α‑l‑rhamnosidase with potential applications in citrus juice industry and in winemaking
dc.creator.none.fl_str_mv Alvarenga, Adriana Elizabet
Romero, Cintia Mariana
Castro, Guillermo Raúl
author Alvarenga, Adriana Elizabet
author_facet Alvarenga, Adriana Elizabet
Romero, Cintia Mariana
Castro, Guillermo Raúl
author_role author
author2 Romero, Cintia Mariana
Castro, Guillermo Raúl
author2_role author
author
dc.subject.none.fl_str_mv Química
α-l-rhamnosidase
β-d-glucosidase
Brevundimonas sp
Naringin
Purification
topic Química
α-l-rhamnosidase
β-d-glucosidase
Brevundimonas sp
Naringin
Purification
dc.description.none.fl_txt_mv The production of monoglycosylated flavonoids by α-l-rhamnosidases (EC 3.2.1.40) is an interesting development in biocatalysis. Applications of rhamnosidases in industry include removal of bitterness caused by naringin from citrus juices. In the present work, a psychrotolerant bacterial strain with α-l-rhamnosidase activity was isolated. The α-l-rhamnosidase was found to be able to degrade naringin and was purified and characterized. The α-l-rhamnosidase from Brevundimonas sp. Ci19 was able to release both rhamnose and prunin from naringin. The enzyme was partially purified with a performance of 2.7-fold purification. The α-l-rhamnosidase showed an optimum pH between 6.00 and 7.00 with substantial residual activity at pH 5.00 (85.3 %). The optimum temperature was between 20 and 37 °C. The enzyme showed activation in the presence of Ca2+ and Cd2+ ions and at a high ethanol concentration level (10 % v/v). Activity was found for β-d-glucosidase (EC 3.2.1.21) in the partially purified extract, but it was inactive in the acid pH region. This result indicates the potential for inactivation of β-d-glucosidase along with the high level of α-l-rhamnosidase activity necessary for the production of flavonoid glycosides. The α-l-rhamnosidase from Brevundimonas sp. Ci19 showed interesting properties for potential use not only in the citrus juice industry but also in winemaking.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description The production of monoglycosylated flavonoids by α-l-rhamnosidases (EC 3.2.1.40) is an interesting development in biocatalysis. Applications of rhamnosidases in industry include removal of bitterness caused by naringin from citrus juices. In the present work, a psychrotolerant bacterial strain with α-l-rhamnosidase activity was isolated. The α-l-rhamnosidase was found to be able to degrade naringin and was purified and characterized. The α-l-rhamnosidase from Brevundimonas sp. Ci19 was able to release both rhamnose and prunin from naringin. The enzyme was partially purified with a performance of 2.7-fold purification. The α-l-rhamnosidase showed an optimum pH between 6.00 and 7.00 with substantial residual activity at pH 5.00 (85.3 %). The optimum temperature was between 20 and 37 °C. The enzyme showed activation in the presence of Ca2+ and Cd2+ ions and at a high ethanol concentration level (10 % v/v). Activity was found for β-d-glucosidase (EC 3.2.1.21) in the partially purified extract, but it was inactive in the acid pH region. This result indicates the potential for inactivation of β-d-glucosidase along with the high level of α-l-rhamnosidase activity necessary for the production of flavonoid glycosides. The α-l-rhamnosidase from Brevundimonas sp. Ci19 showed interesting properties for potential use not only in the citrus juice industry but also in winemaking.
publishDate 2013
dc.date.none.fl_str_mv 2013-08-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/143732
url http://sedici.unlp.edu.ar/handle/10915/143732
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1438-2377
info:eu-repo/semantics/altIdentifier/issn/1438-2385
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00217-013-2074-y
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
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