Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex

Autores
Di Santo Metzler, Paula; Fait, María Elisa; Foresti, María Laura; Morcelle del Valle, Susana Raquel
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lipase activity found in the insoluble fraction of Araujia sericifera Brot.(Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and synthetic substrates and towards fatty acid esterifications, was assayed at different temperatures, pH, and biocatalyst load. In the case of natural substrates (cottonseed oil), highest lipase activity was found at pH 8.5 and 60 ºC. In the hydrolysis of synthetic substrates (p-nitrophenyl esters) the lipase showed preference for the lowest molecular-weight p-nitrophenyl ester assayed (butyrate). Results of the direct esterification of fatty acids of different chain length in organic media showed that esterification levels of up to 45% could be obtained in one hour of reaction. Activity results were compared with the activity shown by the commercial immobilized lipase Novozym 435 under definite reaction conditions. The high activity exhibited by ASL in the hydrolysis of natural substrates and particularly in the direct esterification of different fatty acids in organic medium, together with its high storage stability, suggest this plant lipase as a promising biocatalyst for various biotechnological applications.
Fil: Di Santo Metzler, Paula. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Fait, María Elisa. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Tecnologia En Polimeros y Nanotecnologia; Argentina
Fil: Morcelle del Valle, Susana Raquel. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Materia
Araujia Sericifera Lipase
Esterification Activity
Hydrolytic Activity
Storage Stability
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:11336/6553
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/6553
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latexDi Santo Metzler, PaulaFait, María ElisaForesti, María LauraMorcelle del Valle, Susana RaquelAraujia Sericifera LipaseEsterification ActivityHydrolytic ActivityStorage Stabilityhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Lipase activity found in the insoluble fraction of Araujia sericifera Brot.(Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and synthetic substrates and towards fatty acid esterifications, was assayed at different temperatures, pH, and biocatalyst load. In the case of natural substrates (cottonseed oil), highest lipase activity was found at pH 8.5 and 60 ºC. In the hydrolysis of synthetic substrates (p-nitrophenyl esters) the lipase showed preference for the lowest molecular-weight p-nitrophenyl ester assayed (butyrate). Results of the direct esterification of fatty acids of different chain length in organic media showed that esterification levels of up to 45% could be obtained in one hour of reaction. Activity results were compared with the activity shown by the commercial immobilized lipase Novozym 435 under definite reaction conditions. The high activity exhibited by ASL in the hydrolysis of natural substrates and particularly in the direct esterification of different fatty acids in organic medium, together with its high storage stability, suggest this plant lipase as a promising biocatalyst for various biotechnological applications.Fil: Di Santo Metzler, Paula. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Fait, María Elisa. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Foresti, María Laura. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Tecnologia En Polimeros y Nanotecnologia; ArgentinaFil: Morcelle del Valle, Susana Raquel. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaRoyal Society of Chemistry2014-02info: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/11336/6553Di Santo Metzler, Paula; Fait, María Elisa; Foresti, María Laura; Morcelle del Valle, Susana Raquel; Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex; Royal Society of Chemistry; Catalysis Science & Technology; 4; 5; 2-2014; 1386-13942044-4753enginfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2014/CY/c3cy00782kinfo:eu-repo/semantics/altIdentifier/doi/10.1039/C3CY00782Kinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:05:38Zoai:ri.conicet.gov.ar:11336/6553instacron: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:34982025-10-15 15:05:38.748CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex
title Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex
spellingShingle Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex
Di Santo Metzler, Paula
Araujia Sericifera Lipase
Esterification Activity
Hydrolytic Activity
Storage Stability
title_short Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex
title_full Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex
title_fullStr Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex
title_full_unstemmed Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex
title_sort Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex
dc.creator.none.fl_str_mv Di Santo Metzler, Paula
Fait, María Elisa
Foresti, María Laura
Morcelle del Valle, Susana Raquel
author Di Santo Metzler, Paula
author_facet Di Santo Metzler, Paula
Fait, María Elisa
Foresti, María Laura
Morcelle del Valle, Susana Raquel
author_role author
author2 Fait, María Elisa
Foresti, María Laura
Morcelle del Valle, Susana Raquel
author2_role author
author
author
dc.subject.none.fl_str_mv Araujia Sericifera Lipase
Esterification Activity
Hydrolytic Activity
Storage Stability
topic Araujia Sericifera Lipase
Esterification Activity
Hydrolytic Activity
Storage Stability
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Lipase activity found in the insoluble fraction of Araujia sericifera Brot.(Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and synthetic substrates and towards fatty acid esterifications, was assayed at different temperatures, pH, and biocatalyst load. In the case of natural substrates (cottonseed oil), highest lipase activity was found at pH 8.5 and 60 ºC. In the hydrolysis of synthetic substrates (p-nitrophenyl esters) the lipase showed preference for the lowest molecular-weight p-nitrophenyl ester assayed (butyrate). Results of the direct esterification of fatty acids of different chain length in organic media showed that esterification levels of up to 45% could be obtained in one hour of reaction. Activity results were compared with the activity shown by the commercial immobilized lipase Novozym 435 under definite reaction conditions. The high activity exhibited by ASL in the hydrolysis of natural substrates and particularly in the direct esterification of different fatty acids in organic medium, together with its high storage stability, suggest this plant lipase as a promising biocatalyst for various biotechnological applications.
Fil: Di Santo Metzler, Paula. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Fait, María Elisa. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Tecnologia En Polimeros y Nanotecnologia; Argentina
Fil: Morcelle del Valle, Susana Raquel. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
description Lipase activity found in the insoluble fraction of Araujia sericifera Brot.(Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and synthetic substrates and towards fatty acid esterifications, was assayed at different temperatures, pH, and biocatalyst load. In the case of natural substrates (cottonseed oil), highest lipase activity was found at pH 8.5 and 60 ºC. In the hydrolysis of synthetic substrates (p-nitrophenyl esters) the lipase showed preference for the lowest molecular-weight p-nitrophenyl ester assayed (butyrate). Results of the direct esterification of fatty acids of different chain length in organic media showed that esterification levels of up to 45% could be obtained in one hour of reaction. Activity results were compared with the activity shown by the commercial immobilized lipase Novozym 435 under definite reaction conditions. The high activity exhibited by ASL in the hydrolysis of natural substrates and particularly in the direct esterification of different fatty acids in organic medium, together with its high storage stability, suggest this plant lipase as a promising biocatalyst for various biotechnological applications.
publishDate 2014
dc.date.none.fl_str_mv 2014-02
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/11336/6553
Di Santo Metzler, Paula; Fait, María Elisa; Foresti, María Laura; Morcelle del Valle, Susana Raquel; Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex; Royal Society of Chemistry; Catalysis Science & Technology; 4; 5; 2-2014; 1386-1394
2044-4753
url http://hdl.handle.net/11336/6553
identifier_str_mv Di Santo Metzler, Paula; Fait, María Elisa; Foresti, María Laura; Morcelle del Valle, Susana Raquel; Biocatalytic characterization of a naturally immobilized lipase found in Aaujia Sericifera Brot. (Apocynaceae) latex; Royal Society of Chemistry; Catalysis Science & Technology; 4; 5; 2-2014; 1386-1394
2044-4753
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2014/CY/c3cy00782k
info:eu-repo/semantics/altIdentifier/doi/10.1039/C3CY00782K
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
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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 13.216834

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