Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis

Autores
Romero, Cintia Mariana; Pera, Licia Maria; Loto, Flavia del Valle; Vallejos, Alicia Cecilia; Castro, Guillermo Raul; Baigori, Mario Domingo
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
An organic solvent-tolerant lipase from olive oil-induced Aspergillus niger MYA 135 supernatant was purified using two methods: electroelution and ion-exchange chromatography. With electroelution purification was 8.4-fold and recovery 47% and with ion-exchange 16.6-fold and 53.4%, respectively. The purified enzyme showed a prominent single band with SDS-PAGE and was a monomeric protein of 68 kDa. The isoelectric point (pI) of the lipase was 5.1 and optimum pH and temperature for activity were 7.0 and 37 1C, respectively. The lipase showed affinity for esters with long acyl chains, with a Km of 0.99 mM for C18. Substrate specificity of the immobilized lipase was highest for C18 among the various a- and b-naphthyl esters assayed. Substrate specificity agreed with kinetics parameters of long-chain fatty acids (C18). Transesterification activity of the A. niger MYA 135 lipase indicates that it could be a potential biocatalyst for biodiesel production.
Fil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Loto, Flavia del Valle. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Vallejos, Alicia Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
Fil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Materia
LIPASE
Aspergillus niger
Purification
Organic solvent-tolerant
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:11336/274267
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/274267
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesisRomero, Cintia MarianaPera, Licia MariaLoto, Flavia del ValleVallejos, Alicia CeciliaCastro, Guillermo RaulBaigori, Mario DomingoLIPASEAspergillus nigerPurificationOrganic solvent-toleranthttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1An organic solvent-tolerant lipase from olive oil-induced Aspergillus niger MYA 135 supernatant was purified using two methods: electroelution and ion-exchange chromatography. With electroelution purification was 8.4-fold and recovery 47% and with ion-exchange 16.6-fold and 53.4%, respectively. The purified enzyme showed a prominent single band with SDS-PAGE and was a monomeric protein of 68 kDa. The isoelectric point (pI) of the lipase was 5.1 and optimum pH and temperature for activity were 7.0 and 37 1C, respectively. The lipase showed affinity for esters with long acyl chains, with a Km of 0.99 mM for C18. Substrate specificity of the immobilized lipase was highest for C18 among the various a- and b-naphthyl esters assayed. Substrate specificity agreed with kinetics parameters of long-chain fatty acids (C18). Transesterification activity of the A. niger MYA 135 lipase indicates that it could be a potential biocatalyst for biodiesel production.Fil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Loto, Flavia del Valle. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Vallejos, Alicia Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaElsevier2012-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/274267Romero, Cintia Mariana; Pera, Licia Maria; Loto, Flavia del Valle; Vallejos, Alicia Cecilia; Castro, Guillermo Raul; et al.; Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis; Elsevier; Biocatalysis and Agricultural Biotechnology; 1; 1; 1-2012; 25-311878-8181CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1878818111000144info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2011.08.013info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:57:24Zoai:ri.conicet.gov.ar:11336/274267instacron: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:34982025-11-12 09:57:24.77CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis
title Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis
spellingShingle Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis
Romero, Cintia Mariana
LIPASE
Aspergillus niger
Purification
Organic solvent-tolerant
title_short Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis
title_full Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis
title_fullStr Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis
title_full_unstemmed Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis
title_sort Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis
dc.creator.none.fl_str_mv Romero, Cintia Mariana
Pera, Licia Maria
Loto, Flavia del Valle
Vallejos, Alicia Cecilia
Castro, Guillermo Raul
Baigori, Mario Domingo
author Romero, Cintia Mariana
author_facet Romero, Cintia Mariana
Pera, Licia Maria
Loto, Flavia del Valle
Vallejos, Alicia Cecilia
Castro, Guillermo Raul
Baigori, Mario Domingo
author_role author
author2 Pera, Licia Maria
Loto, Flavia del Valle
Vallejos, Alicia Cecilia
Castro, Guillermo Raul
Baigori, Mario Domingo
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv LIPASE
Aspergillus niger
Purification
Organic solvent-tolerant
topic LIPASE
Aspergillus niger
Purification
Organic solvent-tolerant
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv An organic solvent-tolerant lipase from olive oil-induced Aspergillus niger MYA 135 supernatant was purified using two methods: electroelution and ion-exchange chromatography. With electroelution purification was 8.4-fold and recovery 47% and with ion-exchange 16.6-fold and 53.4%, respectively. The purified enzyme showed a prominent single band with SDS-PAGE and was a monomeric protein of 68 kDa. The isoelectric point (pI) of the lipase was 5.1 and optimum pH and temperature for activity were 7.0 and 37 1C, respectively. The lipase showed affinity for esters with long acyl chains, with a Km of 0.99 mM for C18. Substrate specificity of the immobilized lipase was highest for C18 among the various a- and b-naphthyl esters assayed. Substrate specificity agreed with kinetics parameters of long-chain fatty acids (C18). Transesterification activity of the A. niger MYA 135 lipase indicates that it could be a potential biocatalyst for biodiesel production.
Fil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Loto, Flavia del Valle. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Vallejos, Alicia Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
Fil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
description An organic solvent-tolerant lipase from olive oil-induced Aspergillus niger MYA 135 supernatant was purified using two methods: electroelution and ion-exchange chromatography. With electroelution purification was 8.4-fold and recovery 47% and with ion-exchange 16.6-fold and 53.4%, respectively. The purified enzyme showed a prominent single band with SDS-PAGE and was a monomeric protein of 68 kDa. The isoelectric point (pI) of the lipase was 5.1 and optimum pH and temperature for activity were 7.0 and 37 1C, respectively. The lipase showed affinity for esters with long acyl chains, with a Km of 0.99 mM for C18. Substrate specificity of the immobilized lipase was highest for C18 among the various a- and b-naphthyl esters assayed. Substrate specificity agreed with kinetics parameters of long-chain fatty acids (C18). Transesterification activity of the A. niger MYA 135 lipase indicates that it could be a potential biocatalyst for biodiesel production.
publishDate 2012
dc.date.none.fl_str_mv 2012-01
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/11336/274267
Romero, Cintia Mariana; Pera, Licia Maria; Loto, Flavia del Valle; Vallejos, Alicia Cecilia; Castro, Guillermo Raul; et al.; Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis; Elsevier; Biocatalysis and Agricultural Biotechnology; 1; 1; 1-2012; 25-31
1878-8181
CONICET Digital
CONICET
url http://hdl.handle.net/11336/274267
identifier_str_mv Romero, Cintia Mariana; Pera, Licia Maria; Loto, Flavia del Valle; Vallejos, Alicia Cecilia; Castro, Guillermo Raul; et al.; Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis; Elsevier; Biocatalysis and Agricultural Biotechnology; 1; 1; 1-2012; 25-31
1878-8181
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1878818111000144
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcab.2011.08.013
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
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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