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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/143732
Ver los metadatos del registro completo
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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 |
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info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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openAccess |
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