Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation

Autores
Romero, Cintia Mariana; Pera, Licia Maria; Olivaro, Cristina; Vazquez, Alvaro; Baigori, Mario Domingo
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The use of biocatalysts in fuel industry is an interesting and greener alternative. In this connection, it was found that the chain-length selectivity profile of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 determined in both hydrolytic and synthetic reactions depended on the way that the enzyme was prepared. Indeed, a mycelium-bound (Mb) lipase activity obtained either in presence or absence of 2% olive oil as well as a lyophilized supernatant extract obtained in presence of 2% olive oil showed different specificity constants (1/α). Thus, the highest substrate specificity in hydrolysis reaction was observed toward a long-chain fatty acid (C18; 1/α = 1.0) with the constitutive Mb-lipase in organic medium. In addition, this lipase preparation was specific toward the synthesis of methyl palmitate during esterification (1/α = 1.00) and ethyl palmitate in transesterification (1/α = 0.93). Interestingly, the induced Mb-lipase was a highly reactive biocatalyst preparation in both transesterification (58% of the reactions displayed 1/α > 0.5) and esterification (88% of the reactions displayed 1/α > 0.7) reactions. On the contrary, the induced lyophilized supernatant was the most specific enzymatic system showing a clear preference for linoleic acid in esterification reactions (1/α around of 0.77 for all acyl acceptors tested).
Fil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina
Fil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina
Fil: Olivaro, Cristina. Universidad de la República; Uruguay
Fil: Vazquez, Alvaro. Universidad de la República; Uruguay
Fil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina
Materia
Aspergillus Niger
Biodiesel Component
Lipase
Substrate Specificity
Whole-Cell
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:11336/37695
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/37695
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentationRomero, Cintia MarianaPera, Licia MariaOlivaro, CristinaVazquez, AlvaroBaigori, Mario DomingoAspergillus NigerBiodiesel ComponentLipaseSubstrate SpecificityWhole-Cellhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The use of biocatalysts in fuel industry is an interesting and greener alternative. In this connection, it was found that the chain-length selectivity profile of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 determined in both hydrolytic and synthetic reactions depended on the way that the enzyme was prepared. Indeed, a mycelium-bound (Mb) lipase activity obtained either in presence or absence of 2% olive oil as well as a lyophilized supernatant extract obtained in presence of 2% olive oil showed different specificity constants (1/α). Thus, the highest substrate specificity in hydrolysis reaction was observed toward a long-chain fatty acid (C18; 1/α = 1.0) with the constitutive Mb-lipase in organic medium. In addition, this lipase preparation was specific toward the synthesis of methyl palmitate during esterification (1/α = 1.00) and ethyl palmitate in transesterification (1/α = 0.93). Interestingly, the induced Mb-lipase was a highly reactive biocatalyst preparation in both transesterification (58% of the reactions displayed 1/α > 0.5) and esterification (88% of the reactions displayed 1/α > 0.7) reactions. On the contrary, the induced lyophilized supernatant was the most specific enzymatic system showing a clear preference for linoleic acid in esterification reactions (1/α around of 0.77 for all acyl acceptors tested).Fil: Romero, Cintia Mariana. 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; ArgentinaFil: Olivaro, Cristina. Universidad de la República; UruguayFil: Vazquez, Alvaro. Universidad de la República; UruguayFil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; ArgentinaElsevier Science2012-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/37695Romero, Cintia Mariana; Pera, Licia Maria; Olivaro, Cristina; Vazquez, Alvaro; Baigori, Mario Domingo; Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation; Elsevier Science; Fuel Processing Technology; 98; 6-2012; 23-290378-3820CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.fuproc.2012.01.020info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0378382012000379info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:00Zoai:ri.conicet.gov.ar:11336/37695instacron: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 09:59:01.251CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
title Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
spellingShingle Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
Romero, Cintia Mariana
Aspergillus Niger
Biodiesel Component
Lipase
Substrate Specificity
Whole-Cell
title_short Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
title_full Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
title_fullStr Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
title_full_unstemmed Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
title_sort Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
dc.creator.none.fl_str_mv Romero, Cintia Mariana
Pera, Licia Maria
Olivaro, Cristina
Vazquez, Alvaro
Baigori, Mario Domingo
author Romero, Cintia Mariana
author_facet Romero, Cintia Mariana
Pera, Licia Maria
Olivaro, Cristina
Vazquez, Alvaro
Baigori, Mario Domingo
author_role author
author2 Pera, Licia Maria
Olivaro, Cristina
Vazquez, Alvaro
Baigori, Mario Domingo
author2_role author
author
author
author
dc.subject.none.fl_str_mv Aspergillus Niger
Biodiesel Component
Lipase
Substrate Specificity
Whole-Cell
topic Aspergillus Niger
Biodiesel Component
Lipase
Substrate Specificity
Whole-Cell
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The use of biocatalysts in fuel industry is an interesting and greener alternative. In this connection, it was found that the chain-length selectivity profile of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 determined in both hydrolytic and synthetic reactions depended on the way that the enzyme was prepared. Indeed, a mycelium-bound (Mb) lipase activity obtained either in presence or absence of 2% olive oil as well as a lyophilized supernatant extract obtained in presence of 2% olive oil showed different specificity constants (1/α). Thus, the highest substrate specificity in hydrolysis reaction was observed toward a long-chain fatty acid (C18; 1/α = 1.0) with the constitutive Mb-lipase in organic medium. In addition, this lipase preparation was specific toward the synthesis of methyl palmitate during esterification (1/α = 1.00) and ethyl palmitate in transesterification (1/α = 0.93). Interestingly, the induced Mb-lipase was a highly reactive biocatalyst preparation in both transesterification (58% of the reactions displayed 1/α > 0.5) and esterification (88% of the reactions displayed 1/α > 0.7) reactions. On the contrary, the induced lyophilized supernatant was the most specific enzymatic system showing a clear preference for linoleic acid in esterification reactions (1/α around of 0.77 for all acyl acceptors tested).
Fil: Romero, Cintia Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina
Fil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina
Fil: Olivaro, Cristina. Universidad de la República; Uruguay
Fil: Vazquez, Alvaro. Universidad de la República; Uruguay
Fil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Planta Piloto de Procesos Industriales Microbiologicos; Argentina
description The use of biocatalysts in fuel industry is an interesting and greener alternative. In this connection, it was found that the chain-length selectivity profile of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 determined in both hydrolytic and synthetic reactions depended on the way that the enzyme was prepared. Indeed, a mycelium-bound (Mb) lipase activity obtained either in presence or absence of 2% olive oil as well as a lyophilized supernatant extract obtained in presence of 2% olive oil showed different specificity constants (1/α). Thus, the highest substrate specificity in hydrolysis reaction was observed toward a long-chain fatty acid (C18; 1/α = 1.0) with the constitutive Mb-lipase in organic medium. In addition, this lipase preparation was specific toward the synthesis of methyl palmitate during esterification (1/α = 1.00) and ethyl palmitate in transesterification (1/α = 0.93). Interestingly, the induced Mb-lipase was a highly reactive biocatalyst preparation in both transesterification (58% of the reactions displayed 1/α > 0.5) and esterification (88% of the reactions displayed 1/α > 0.7) reactions. On the contrary, the induced lyophilized supernatant was the most specific enzymatic system showing a clear preference for linoleic acid in esterification reactions (1/α around of 0.77 for all acyl acceptors tested).
publishDate 2012
dc.date.none.fl_str_mv 2012-06
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/11336/37695
Romero, Cintia Mariana; Pera, Licia Maria; Olivaro, Cristina; Vazquez, Alvaro; Baigori, Mario Domingo; Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation; Elsevier Science; Fuel Processing Technology; 98; 6-2012; 23-29
0378-3820
CONICET Digital
CONICET
url http://hdl.handle.net/11336/37695
identifier_str_mv Romero, Cintia Mariana; Pera, Licia Maria; Olivaro, Cristina; Vazquez, Alvaro; Baigori, Mario Domingo; Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation; Elsevier Science; Fuel Processing Technology; 98; 6-2012; 23-29
0378-3820
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.fuproc.2012.01.020
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0378382012000379
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
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
_version_ 1842269556261781504
score 13.13397

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