Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol

The potential biotecnological applications of both constitutive and inducible lipase sources from Aspergillus niger MYA 135 were evaluated. To this end, the effect of environmental conditions on mycelium-bound lipase production from this strain was studied, when cultured either in the absence or pre...

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Autores: Colin, Veronica Leticia, Baigori, Mario Domingo, Pera, Licia Maria
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2011
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/16916
Acceso en línea:http://hdl.handle.net/11336/16916
Access Level:acceso abierto
Palabra clave:Aspergillus Niger Mya 135
Transesterification
Biodiesel
Hydeolytic Activity
Mycelium-Bound Lipase
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
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spelling Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanolColin, Veronica LeticiaBaigori, Mario DomingoPera, Licia MariaAspergillus Niger Mya 135TransesterificationBiodieselHydeolytic ActivityMycelium-Bound Lipasehttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The potential biotecnological applications of both constitutive and inducible lipase sources from Aspergillus niger MYA 135 were evaluated. To this end, the effect of environmental conditions on mycelium-bound lipase production from this strain was studied, when cultured either in the absence or presence of 2% olive oil. It was previously reported that mycelium-bound lipase from Aspergillus niger MYA 135 possess high stability in reaction mixtures containing ethanol; which could be especially important for their use in biodiesel synthesis. In this connection, the performance of the lipase sources produced in the transesterification of ethanol using p-nitrophenyl palmitate as acyl donor was also explored. Under our assay conditions, hydrolytic and synthetic activity of the mycelia produced in the absence or presence of olive oil were not highly correlated. While the hydrolytic activity was strongly increased by the addition of lipid to the culture medium, the best performance in the transesterification reactions of ethanol were associated with mycelia produced in absence of olive oil. Interestingly, the supplementation of the culture medium with Fe+3 increased the transesterification activity by 71%, as compared to the activity previously reported for this strain. Therefore, the constitutive lipase sources from Aspergillus niger MYA 135 are considered to be promising for industrial biodiesel-fuel production.Fil: Colin, Veronica Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; ArgentinaFil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; ArgentinaFil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; ArgentinaWiley Vch Verlag2011-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/16916Colin, Veronica Leticia; Baigori, Mario Domingo; Pera, Licia Maria; Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol; Wiley Vch Verlag; Journal Of Basic Microbiology; 51; 3; 6-2011; 236-2420233-111Xenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/jobm.201000232info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jobm.201000232/fullinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:38:53Zoai:ri.conicet.gov.ar:11336/16916instacron: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:34982024-05-08 13:38:53.838CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol
title Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol
spellingShingle Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol
Colin, Veronica Leticia
Aspergillus Niger Mya 135
Transesterification
Biodiesel
Hydeolytic Activity
Mycelium-Bound Lipase
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
title_short Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol
title_full Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol
title_fullStr Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol
title_full_unstemmed Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol
title_sort Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol
dc.creator.none.fl_str_mv Colin, Veronica Leticia
Baigori, Mario Domingo
Pera, Licia Maria
author Colin, Veronica Leticia
author_facet Colin, Veronica Leticia
Baigori, Mario Domingo
Pera, Licia Maria
author_role author
author2 Baigori, Mario Domingo
Pera, Licia Maria
author2_role author
author
dc.subject.none.fl_str_mv Aspergillus Niger Mya 135
Transesterification
Biodiesel
Hydeolytic Activity
Mycelium-Bound Lipase
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
topic Aspergillus Niger Mya 135
Transesterification
Biodiesel
Hydeolytic Activity
Mycelium-Bound Lipase
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
description The potential biotecnological applications of both constitutive and inducible lipase sources from Aspergillus niger MYA 135 were evaluated. To this end, the effect of environmental conditions on mycelium-bound lipase production from this strain was studied, when cultured either in the absence or presence of 2% olive oil. It was previously reported that mycelium-bound lipase from Aspergillus niger MYA 135 possess high stability in reaction mixtures containing ethanol; which could be especially important for their use in biodiesel synthesis. In this connection, the performance of the lipase sources produced in the transesterification of ethanol using p-nitrophenyl palmitate as acyl donor was also explored. Under our assay conditions, hydrolytic and synthetic activity of the mycelia produced in the absence or presence of olive oil were not highly correlated. While the hydrolytic activity was strongly increased by the addition of lipid to the culture medium, the best performance in the transesterification reactions of ethanol were associated with mycelia produced in absence of olive oil. Interestingly, the supplementation of the culture medium with Fe+3 increased the transesterification activity by 71%, as compared to the activity previously reported for this strain. Therefore, the constitutive lipase sources from Aspergillus niger MYA 135 are considered to be promising for industrial biodiesel-fuel production.
publishDate 2011
dc.date.none.fl_str_mv 2011-06
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/11336/16916
Colin, Veronica Leticia; Baigori, Mario Domingo; Pera, Licia Maria; Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol; Wiley Vch Verlag; Journal Of Basic Microbiology; 51; 3; 6-2011; 236-242
0233-111X
url http://hdl.handle.net/11336/16916
identifier_str_mv Colin, Veronica Leticia; Baigori, Mario Domingo; Pera, Licia Maria; Mycelium-bound lipase production from Aspergillus niger MYA 135, and its potential applications for the transesterification of ethanol; Wiley Vch Verlag; Journal Of Basic Microbiology; 51; 3; 6-2011; 236-242
0233-111X
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/jobm.201000232
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jobm.201000232/full
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
application/pdf
dc.publisher.none.fl_str_mv Wiley Vch Verlag
publisher.none.fl_str_mv Wiley Vch Verlag
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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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