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
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/143998
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/143998
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling 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:UNLP2025-10-22T17:13:11Zoai: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:13292025-10-22 17:13:11.447SEDICI (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 SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution 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 12.718478

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