Interaction of catalase with carrageenan applied to its recovery from murine liver

Autores
Belluzo, María Soledad; Galante, Micaela; Picó, Guillermo Alfredo; Boeris, Valeria
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The complexes formation between acid and basic polyelectrolytes (carrageenan and Eudragit ® EPO) with catalase was evaluated in order to understand the mechanism of their interaction. Catalase was selected as the model enzyme since its application in several biotechnological processes. The study of this interaction had showed that the non soluble complexes take place in a pH interval which depends on the nature of the polyelectrolyte and salt presence. Carrageenan showed to be the best choice for the catalase affinity precipitation, since the amount needed for the full precipitation of the enzyme was lower, with a faster kinetic and a slight stabilization of the protein structure. After establishing the optimal conditions, we were able to purify catalase from murine liver, a natural source, with a purification factor of 6.4 and a yield of 19%, using only one step in the enzyme purification process.
Fil: Belluzo, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Galante, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Materia
Catalase
Carrageenan
Eudragit Epo
Affinity Precipitation
Purification
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/6026
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/6026
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Interaction of catalase with carrageenan applied to its recovery from murine liverBelluzo, María SoledadGalante, MicaelaPicó, Guillermo AlfredoBoeris, ValeriaCatalaseCarrageenanEudragit EpoAffinity PrecipitationPurificationhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The complexes formation between acid and basic polyelectrolytes (carrageenan and Eudragit ® EPO) with catalase was evaluated in order to understand the mechanism of their interaction. Catalase was selected as the model enzyme since its application in several biotechnological processes. The study of this interaction had showed that the non soluble complexes take place in a pH interval which depends on the nature of the polyelectrolyte and salt presence. Carrageenan showed to be the best choice for the catalase affinity precipitation, since the amount needed for the full precipitation of the enzyme was lower, with a faster kinetic and a slight stabilization of the protein structure. After establishing the optimal conditions, we were able to purify catalase from murine liver, a natural source, with a purification factor of 6.4 and a yield of 19%, using only one step in the enzyme purification process.Fil: Belluzo, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; ArgentinaFil: Galante, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; ArgentinaFil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; ArgentinaFil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; ArgentinaElsevier2013-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/6026Belluzo, María Soledad; Galante, Micaela; Picó, Guillermo Alfredo; Boeris, Valeria; Interaction of catalase with carrageenan applied to its recovery from murine liver; Elsevier; Separation and Purification Technology; 111; 6-2013; 125-1301383-5866enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1383586613001652info:eu-repo/semantics/altIdentifier/doi/10.1016/j.seppur.2013.03.027info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:47:49Zoai:ri.conicet.gov.ar:11336/6026instacron: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:34982025-10-22 11:47:49.734CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interaction of catalase with carrageenan applied to its recovery from murine liver
title Interaction of catalase with carrageenan applied to its recovery from murine liver
spellingShingle Interaction of catalase with carrageenan applied to its recovery from murine liver
Belluzo, María Soledad
Catalase
Carrageenan
Eudragit Epo
Affinity Precipitation
Purification
title_short Interaction of catalase with carrageenan applied to its recovery from murine liver
title_full Interaction of catalase with carrageenan applied to its recovery from murine liver
title_fullStr Interaction of catalase with carrageenan applied to its recovery from murine liver
title_full_unstemmed Interaction of catalase with carrageenan applied to its recovery from murine liver
title_sort Interaction of catalase with carrageenan applied to its recovery from murine liver
dc.creator.none.fl_str_mv Belluzo, María Soledad
Galante, Micaela
Picó, Guillermo Alfredo
Boeris, Valeria
author Belluzo, María Soledad
author_facet Belluzo, María Soledad
Galante, Micaela
Picó, Guillermo Alfredo
Boeris, Valeria
author_role author
author2 Galante, Micaela
Picó, Guillermo Alfredo
Boeris, Valeria
author2_role author
author
author
dc.subject.none.fl_str_mv Catalase
Carrageenan
Eudragit Epo
Affinity Precipitation
Purification
topic Catalase
Carrageenan
Eudragit Epo
Affinity Precipitation
Purification
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The complexes formation between acid and basic polyelectrolytes (carrageenan and Eudragit ® EPO) with catalase was evaluated in order to understand the mechanism of their interaction. Catalase was selected as the model enzyme since its application in several biotechnological processes. The study of this interaction had showed that the non soluble complexes take place in a pH interval which depends on the nature of the polyelectrolyte and salt presence. Carrageenan showed to be the best choice for the catalase affinity precipitation, since the amount needed for the full precipitation of the enzyme was lower, with a faster kinetic and a slight stabilization of the protein structure. After establishing the optimal conditions, we were able to purify catalase from murine liver, a natural source, with a purification factor of 6.4 and a yield of 19%, using only one step in the enzyme purification process.
Fil: Belluzo, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Galante, Micaela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
Fil: Boeris, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Química Rosario; Argentina
description The complexes formation between acid and basic polyelectrolytes (carrageenan and Eudragit ® EPO) with catalase was evaluated in order to understand the mechanism of their interaction. Catalase was selected as the model enzyme since its application in several biotechnological processes. The study of this interaction had showed that the non soluble complexes take place in a pH interval which depends on the nature of the polyelectrolyte and salt presence. Carrageenan showed to be the best choice for the catalase affinity precipitation, since the amount needed for the full precipitation of the enzyme was lower, with a faster kinetic and a slight stabilization of the protein structure. After establishing the optimal conditions, we were able to purify catalase from murine liver, a natural source, with a purification factor of 6.4 and a yield of 19%, using only one step in the enzyme purification process.
publishDate 2013
dc.date.none.fl_str_mv 2013-06
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/11336/6026
Belluzo, María Soledad; Galante, Micaela; Picó, Guillermo Alfredo; Boeris, Valeria; Interaction of catalase with carrageenan applied to its recovery from murine liver; Elsevier; Separation and Purification Technology; 111; 6-2013; 125-130
1383-5866
url http://hdl.handle.net/11336/6026
identifier_str_mv Belluzo, María Soledad; Galante, Micaela; Picó, Guillermo Alfredo; Boeris, Valeria; Interaction of catalase with carrageenan applied to its recovery from murine liver; Elsevier; Separation and Purification Technology; 111; 6-2013; 125-130
1383-5866
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1383586613001652
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.seppur.2013.03.027
info:eu-repo/semantics/altIdentifier/doi/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 12.982451

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