Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels

Autores
Mammarella, Enrique José; Rubiolo, Amelia Catalina
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The stability of ß-galactosidase entrapped in Ca-alginate–K-k-carrageenan gels under operation conditions was studied. The thermal deactivation of the immobilised enzyme and the biocatalyst protein loss due to gel swelling were taken into account in the mass balance of the enzymatic reaction rate expression. Time-temperature effect was the most important factor in the biocatalyst deactivation reaction. However, results showed that the enzyme entrapped in gels was partially lost by gel swelling, which was a source of error in predicting results in continuous processes. The enzyme loss determined in this work showed a non-linear behaviour and it depended on mixing conditions of the reactor. Values of protein loss were used in the modelling of a fixed-bed reactor with similar flow conditions to reduce the error in predicting the operation conditions to maintain a constant conversion. For reaction conditions similar to those analysed in this work, the ß-galactosidase was well entrapped in alginate-carrageenan matrices.
Fil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Rubiolo, Amelia Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Materia
Deactivation
Enzime
Entrapped
Carrageenan Gels
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/23591
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan GelsMammarella, Enrique JoséRubiolo, Amelia CatalinaDeactivationEnzimeEntrappedCarrageenan Gelshttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The stability of ß-galactosidase entrapped in Ca-alginate–K-k-carrageenan gels under operation conditions was studied. The thermal deactivation of the immobilised enzyme and the biocatalyst protein loss due to gel swelling were taken into account in the mass balance of the enzymatic reaction rate expression. Time-temperature effect was the most important factor in the biocatalyst deactivation reaction. However, results showed that the enzyme entrapped in gels was partially lost by gel swelling, which was a source of error in predicting results in continuous processes. The enzyme loss determined in this work showed a non-linear behaviour and it depended on mixing conditions of the reactor. Values of protein loss were used in the modelling of a fixed-bed reactor with similar flow conditions to reduce the error in predicting the operation conditions to maintain a constant conversion. For reaction conditions similar to those analysed in this work, the ß-galactosidase was well entrapped in alginate-carrageenan matrices.Fil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; ArgentinaFil: Rubiolo, Amelia Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; ArgentinaElsevier Science2005-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/23591Mammarella, Enrique José; Rubiolo, Amelia Catalina; Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 34; 1-6; 7-2005; 7-131381-1177CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2005.04.007info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117705000457info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:12Zoai:ri.conicet.gov.ar:11336/23591instacron: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:34982025-09-03 09:44:12.59CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels
title Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels
spellingShingle Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels
Mammarella, Enrique José
Deactivation
Enzime
Entrapped
Carrageenan Gels
title_short Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels
title_full Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels
title_fullStr Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels
title_full_unstemmed Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels
title_sort Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels
dc.creator.none.fl_str_mv Mammarella, Enrique José
Rubiolo, Amelia Catalina
author Mammarella, Enrique José
author_facet Mammarella, Enrique José
Rubiolo, Amelia Catalina
author_role author
author2 Rubiolo, Amelia Catalina
author2_role author
dc.subject.none.fl_str_mv Deactivation
Enzime
Entrapped
Carrageenan Gels
topic Deactivation
Enzime
Entrapped
Carrageenan Gels
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The stability of ß-galactosidase entrapped in Ca-alginate–K-k-carrageenan gels under operation conditions was studied. The thermal deactivation of the immobilised enzyme and the biocatalyst protein loss due to gel swelling were taken into account in the mass balance of the enzymatic reaction rate expression. Time-temperature effect was the most important factor in the biocatalyst deactivation reaction. However, results showed that the enzyme entrapped in gels was partially lost by gel swelling, which was a source of error in predicting results in continuous processes. The enzyme loss determined in this work showed a non-linear behaviour and it depended on mixing conditions of the reactor. Values of protein loss were used in the modelling of a fixed-bed reactor with similar flow conditions to reduce the error in predicting the operation conditions to maintain a constant conversion. For reaction conditions similar to those analysed in this work, the ß-galactosidase was well entrapped in alginate-carrageenan matrices.
Fil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Rubiolo, Amelia Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
description The stability of ß-galactosidase entrapped in Ca-alginate–K-k-carrageenan gels under operation conditions was studied. The thermal deactivation of the immobilised enzyme and the biocatalyst protein loss due to gel swelling were taken into account in the mass balance of the enzymatic reaction rate expression. Time-temperature effect was the most important factor in the biocatalyst deactivation reaction. However, results showed that the enzyme entrapped in gels was partially lost by gel swelling, which was a source of error in predicting results in continuous processes. The enzyme loss determined in this work showed a non-linear behaviour and it depended on mixing conditions of the reactor. Values of protein loss were used in the modelling of a fixed-bed reactor with similar flow conditions to reduce the error in predicting the operation conditions to maintain a constant conversion. For reaction conditions similar to those analysed in this work, the ß-galactosidase was well entrapped in alginate-carrageenan matrices.
publishDate 2005
dc.date.none.fl_str_mv 2005-07
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/11336/23591
Mammarella, Enrique José; Rubiolo, Amelia Catalina; Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 34; 1-6; 7-2005; 7-13
1381-1177
CONICET Digital
CONICET
url http://hdl.handle.net/11336/23591
identifier_str_mv Mammarella, Enrique José; Rubiolo, Amelia Catalina; Study of the Deactivation of ß-galactosidase Entrapped in Alginate-carrageenan Gels; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 34; 1-6; 7-2005; 7-13
1381-1177
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2005.04.007
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117705000457
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 Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
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 13.13397

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