Cross-linked α-l-rhamnosidase aggregates with potential application in food industry
- Autores
- Alvarenga, Adriana Elizabet; Amoroso, María Julia; Illanes, Andrés; Castro, Guillermo Raúl
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- α-l-Rhamnosidase (E.C. 3.2.1.40) from Brevundimonas sp. Ci19 was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with acetone followed by glutaraldehyde cross-linking. The effects of precipitation and cross-linking on CLEA activity were investigated and characterized. Sixty percent acetone solution and 2.0 % glutaraldehyde were used at pH 7.0 for 1-h cross-linking reaction. The yield of rhamnosidase-CLEA was approximately 80 % starting from crude extracts or pure enzyme suggesting non-purification steps are required for extended use. No significant differences in optimum pH and temperature values of the enzyme were recorded after immobilization. The rham-CLEA recycled 4 times showed about 80 % rhamnosidase activity; meanwhile, in the fifth and six recycled time, the enzyme activity was reduced to about 40 and 20 %, respectively.
Centro de Investigación y Desarrollo en Fermentaciones Industriales - Materia
-
Biología
Immobilization
α-l-Rhamnosidase
Brevundimonas sp. Ci19
Cross-linked enzyme aggregate (CLEA) - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/143998
Ver los metadatos del registro completo
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Cross-linked α-l-rhamnosidase aggregates with potential application in food industryAlvarenga, Adriana ElizabetAmoroso, María JuliaIllanes, AndrésCastro, Guillermo RaúlBiologíaImmobilizationα-l-RhamnosidaseBrevundimonas sp. Ci19Cross-linked enzyme aggregate (CLEA)α-l-Rhamnosidase (E.C. 3.2.1.40) from Brevundimonas sp. Ci19 was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with acetone followed by glutaraldehyde cross-linking. The effects of precipitation and cross-linking on CLEA activity were investigated and characterized. Sixty percent acetone solution and 2.0 % glutaraldehyde were used at pH 7.0 for 1-h cross-linking reaction. The yield of rhamnosidase-CLEA was approximately 80 % starting from crude extracts or pure enzyme suggesting non-purification steps are required for extended use. No significant differences in optimum pH and temperature values of the enzyme were recorded after immobilization. The rham-CLEA recycled 4 times showed about 80 % rhamnosidase activity; meanwhile, in the fifth and six recycled time, the enzyme activity was reduced to about 40 and 20 %, respectively.Centro de Investigación y Desarrollo en Fermentaciones Industriales2014-01-22info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf797-801http://sedici.unlp.edu.ar/handle/10915/143998enginfo:eu-repo/semantics/altIdentifier/issn/1438-2377info:eu-repo/semantics/altIdentifier/issn/1438-2385info:eu-repo/semantics/altIdentifier/doi/10.1007/s00217-014-2157-4info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:32:16Zoai:sedici.unlp.edu.ar:10915/143998Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:17.155SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Cross-linked α-l-rhamnosidase aggregates with potential application in food industry |
title |
Cross-linked α-l-rhamnosidase aggregates with potential application in food industry |
spellingShingle |
Cross-linked α-l-rhamnosidase aggregates with potential application in food industry Alvarenga, Adriana Elizabet Biología Immobilization α-l-Rhamnosidase Brevundimonas sp. Ci19 Cross-linked enzyme aggregate (CLEA) |
title_short |
Cross-linked α-l-rhamnosidase aggregates with potential application in food industry |
title_full |
Cross-linked α-l-rhamnosidase aggregates with potential application in food industry |
title_fullStr |
Cross-linked α-l-rhamnosidase aggregates with potential application in food industry |
title_full_unstemmed |
Cross-linked α-l-rhamnosidase aggregates with potential application in food industry |
title_sort |
Cross-linked α-l-rhamnosidase aggregates with potential application in food industry |
dc.creator.none.fl_str_mv |
Alvarenga, Adriana Elizabet Amoroso, María Julia Illanes, Andrés Castro, Guillermo Raúl |
author |
Alvarenga, Adriana Elizabet |
author_facet |
Alvarenga, Adriana Elizabet Amoroso, María Julia Illanes, Andrés Castro, Guillermo Raúl |
author_role |
author |
author2 |
Amoroso, María Julia Illanes, Andrés Castro, Guillermo Raúl |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Biología Immobilization α-l-Rhamnosidase Brevundimonas sp. Ci19 Cross-linked enzyme aggregate (CLEA) |
topic |
Biología Immobilization α-l-Rhamnosidase Brevundimonas sp. Ci19 Cross-linked enzyme aggregate (CLEA) |
dc.description.none.fl_txt_mv |
α-l-Rhamnosidase (E.C. 3.2.1.40) from Brevundimonas sp. Ci19 was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with acetone followed by glutaraldehyde cross-linking. The effects of precipitation and cross-linking on CLEA activity were investigated and characterized. Sixty percent acetone solution and 2.0 % glutaraldehyde were used at pH 7.0 for 1-h cross-linking reaction. The yield of rhamnosidase-CLEA was approximately 80 % starting from crude extracts or pure enzyme suggesting non-purification steps are required for extended use. No significant differences in optimum pH and temperature values of the enzyme were recorded after immobilization. The rham-CLEA recycled 4 times showed about 80 % rhamnosidase activity; meanwhile, in the fifth and six recycled time, the enzyme activity was reduced to about 40 and 20 %, respectively. Centro de Investigación y Desarrollo en Fermentaciones Industriales |
description |
α-l-Rhamnosidase (E.C. 3.2.1.40) from Brevundimonas sp. Ci19 was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with acetone followed by glutaraldehyde cross-linking. The effects of precipitation and cross-linking on CLEA activity were investigated and characterized. Sixty percent acetone solution and 2.0 % glutaraldehyde were used at pH 7.0 for 1-h cross-linking reaction. The yield of rhamnosidase-CLEA was approximately 80 % starting from crude extracts or pure enzyme suggesting non-purification steps are required for extended use. No significant differences in optimum pH and temperature values of the enzyme were recorded after immobilization. The rham-CLEA recycled 4 times showed about 80 % rhamnosidase activity; meanwhile, in the fifth and six recycled time, the enzyme activity was reduced to about 40 and 20 %, respectively. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-01-22 |
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/10915/143998 |
url |
http://sedici.unlp.edu.ar/handle/10915/143998 |
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/s00217-014-2157-4 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
dc.format.none.fl_str_mv |
application/pdf 797-801 |
dc.source.none.fl_str_mv |
reponame:SEDICI (UNLP) instname:Universidad Nacional de La Plata instacron:UNLP |
reponame_str |
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Universidad Nacional de La Plata |
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UNLP |
repository.name.fl_str_mv |
SEDICI (UNLP) - Universidad Nacional de La Plata |
repository.mail.fl_str_mv |
alira@sedici.unlp.edu.ar |
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score |
13.070432 |