Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract

Autores
Llerena Suster, Carlos Rafael; Briand, Laura Estefanía; Morcelle del Valle, Susana Raquel
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
This paper presents a rational strategy to purify the lipase B of Candida antarctica of the commercial extract Lipozyme® through size exclusion coupled with anionic exchange chromatography using a non conventional, easy to remove buffer system such as ammonia-ammonium. In this context, each step of the purification was followed through the determination of the protein content, esterase activity measurements, SDS-PAGE, agarose electrophoresis, UVspectroscopy and isoelectric focusing. The purification of the commercial extract afforded a sample that retains 47% of the proteins (being CALB the major enzymatic component of the purified sample) with a hydrolytic activity higher than the starting crude extract.
Centro de Investigación de Proteínas Vegetales
Materia
Biología
Protein purification
CALB
UV absorbance
Bradford
Size exclusion chromatography
Ion exchange chromatography
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:10915/191973
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/191973
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic ExtractLlerena Suster, Carlos RafaelBriand, Laura EstefaníaMorcelle del Valle, Susana RaquelBiologíaProtein purificationCALBUV absorbanceBradfordSize exclusion chromatographyIon exchange chromatographyThis paper presents a rational strategy to purify the lipase B of Candida antarctica of the commercial extract Lipozyme® through size exclusion coupled with anionic exchange chromatography using a non conventional, easy to remove buffer system such as ammonia-ammonium. In this context, each step of the purification was followed through the determination of the protein content, esterase activity measurements, SDS-PAGE, agarose electrophoresis, UVspectroscopy and isoelectric focusing. The purification of the commercial extract afforded a sample that retains 47% of the proteins (being CALB the major enzymatic component of the purified sample) with a hydrolytic activity higher than the starting crude extract.Centro de Investigación de Proteínas Vegetales2014info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf155-160http://sedici.unlp.edu.ar/handle/10915/191973enginfo:eu-repo/semantics/altIdentifier/issn/2211-5455info:eu-repo/semantics/altIdentifier/doi/10.2174/2211544702666131224234223info: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:UNLP2026-03-26T09:21:46Zoai:sedici.unlp.edu.ar:10915/191973Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292026-03-26 09:21:47.192SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract
title Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract
spellingShingle Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract
Llerena Suster, Carlos Rafael
Biología
Protein purification
CALB
UV absorbance
Bradford
Size exclusion chromatography
Ion exchange chromatography
title_short Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract
title_full Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract
title_fullStr Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract
title_full_unstemmed Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract
title_sort Purification of The Lipase B of Candida antarctica from a Commercial Enzymatic Extract
dc.creator.none.fl_str_mv Llerena Suster, Carlos Rafael
Briand, Laura Estefanía
Morcelle del Valle, Susana Raquel
author Llerena Suster, Carlos Rafael
author_facet Llerena Suster, Carlos Rafael
Briand, Laura Estefanía
Morcelle del Valle, Susana Raquel
author_role author
author2 Briand, Laura Estefanía
Morcelle del Valle, Susana Raquel
author2_role author
author
dc.subject.none.fl_str_mv Biología
Protein purification
CALB
UV absorbance
Bradford
Size exclusion chromatography
Ion exchange chromatography
topic Biología
Protein purification
CALB
UV absorbance
Bradford
Size exclusion chromatography
Ion exchange chromatography
dc.description.none.fl_txt_mv This paper presents a rational strategy to purify the lipase B of Candida antarctica of the commercial extract Lipozyme® through size exclusion coupled with anionic exchange chromatography using a non conventional, easy to remove buffer system such as ammonia-ammonium. In this context, each step of the purification was followed through the determination of the protein content, esterase activity measurements, SDS-PAGE, agarose electrophoresis, UVspectroscopy and isoelectric focusing. The purification of the commercial extract afforded a sample that retains 47% of the proteins (being CALB the major enzymatic component of the purified sample) with a hydrolytic activity higher than the starting crude extract.
Centro de Investigación de Proteínas Vegetales
description This paper presents a rational strategy to purify the lipase B of Candida antarctica of the commercial extract Lipozyme® through size exclusion coupled with anionic exchange chromatography using a non conventional, easy to remove buffer system such as ammonia-ammonium. In this context, each step of the purification was followed through the determination of the protein content, esterase activity measurements, SDS-PAGE, agarose electrophoresis, UVspectroscopy and isoelectric focusing. The purification of the commercial extract afforded a sample that retains 47% of the proteins (being CALB the major enzymatic component of the purified sample) with a hydrolytic activity higher than the starting crude extract.
publishDate 2014
dc.date.none.fl_str_mv 2014
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/10915/191973
url http://sedici.unlp.edu.ar/handle/10915/191973
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/2211-5455
info:eu-repo/semantics/altIdentifier/doi/10.2174/2211544702666131224234223
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
155-160
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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