Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids

Autores
Gutiérrez Ayesta, Cecilia; Carelli Albarracin, Amalia Antonia; Ferreira, María Luján
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lipases with different structures were investigated for their catalytic ability to hydrolyse sunflower oil, soybean lecithin and their mixtures in heptane at 60 °C in a biphasic mixture heptane-buffer pH 7.0. Besides, the substrate adsorption mechanism was studied theoretically with the Chem 3D 5.0 Ultra program and the MM2 (Cambridge Soft) method by using trilinolein and phosphatidylcholine as system models of triglycerides and phospholipids, respectively. Lipolase 100T, a granulated silica immobilised commercial preparation of Thermomyces (formerly Humicola) lanuginosa lipase, evidenced the highest conversion to fatty acids when sunflower oil (85.3% conversion to fatty acids) and its mixture with lecithin (100 % conversion to fatty acids) were tested. The free lipase from Rhizomucor meiheir (RML) evidenced the highest activity with lecithin as substrate (35.6% conversion to fatty acids). The lipases with their active sites on the surface presented the highest strength of substrate coordination – as a decrease of steric energy. In the case of RML and the artificial mix sunflower oil–lecithin, the product distribution between MG, DG and FA was: 29.70% MG, 32.96% DG and 37.34% of fatty acids (FA). When Lipolase 100T was used, the distribution was: 14.91% MG, 15.46% DG and 69.63% FA. Besides the FA, monoglycerides (MG) and diglycerides (DG) a new product was detected when lecithin was present (alone or in the mix) specially when RML was used as biocatalyst. No evidence of this peak was found after the reaction using Lipolase 100T. This new product can be related to the presence of phosphate charged group in lecithin and to the possibility of cracking of one of the hydrocarbon chains of the FA in TG. A possible reaction with the exposed active site of RML is discussed. The assignation of this new compound as a MG of a shorter fatty acid chain – with 9 carbon atoms – is presented and supported with further analytical analysis.
Fil: Gutiérrez Ayesta, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Carelli Albarracin, Amalia Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Materia
Lipase
Hydrolytic Activity
Gas Chromatography
Lecithin
Sunflower Oil
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:11336/81926
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/81926
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipidsGutiérrez Ayesta, CeciliaCarelli Albarracin, Amalia AntoniaFerreira, María LujánLipaseHydrolytic ActivityGas ChromatographyLecithinSunflower Oilhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Lipases with different structures were investigated for their catalytic ability to hydrolyse sunflower oil, soybean lecithin and their mixtures in heptane at 60 °C in a biphasic mixture heptane-buffer pH 7.0. Besides, the substrate adsorption mechanism was studied theoretically with the Chem 3D 5.0 Ultra program and the MM2 (Cambridge Soft) method by using trilinolein and phosphatidylcholine as system models of triglycerides and phospholipids, respectively. Lipolase 100T, a granulated silica immobilised commercial preparation of Thermomyces (formerly Humicola) lanuginosa lipase, evidenced the highest conversion to fatty acids when sunflower oil (85.3% conversion to fatty acids) and its mixture with lecithin (100 % conversion to fatty acids) were tested. The free lipase from Rhizomucor meiheir (RML) evidenced the highest activity with lecithin as substrate (35.6% conversion to fatty acids). The lipases with their active sites on the surface presented the highest strength of substrate coordination – as a decrease of steric energy. In the case of RML and the artificial mix sunflower oil–lecithin, the product distribution between MG, DG and FA was: 29.70% MG, 32.96% DG and 37.34% of fatty acids (FA). When Lipolase 100T was used, the distribution was: 14.91% MG, 15.46% DG and 69.63% FA. Besides the FA, monoglycerides (MG) and diglycerides (DG) a new product was detected when lecithin was present (alone or in the mix) specially when RML was used as biocatalyst. No evidence of this peak was found after the reaction using Lipolase 100T. This new product can be related to the presence of phosphate charged group in lecithin and to the possibility of cracking of one of the hydrocarbon chains of the FA in TG. A possible reaction with the exposed active site of RML is discussed. The assignation of this new compound as a MG of a shorter fatty acid chain – with 9 carbon atoms – is presented and supported with further analytical analysis.Fil: Gutiérrez Ayesta, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Carelli Albarracin, Amalia Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaElsevier Science Inc2007-07-02info: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/11336/81926Gutiérrez Ayesta, Cecilia; Carelli Albarracin, Amalia Antonia; Ferreira, María Luján; Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids; Elsevier Science Inc; Enzyme and Microbial Technology; 41; 1-2; 2-7-2007; 35-430141-0229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022906005849info:eu-repo/semantics/altIdentifier/doi/10.1016/j.enzmictec.2006.11.018info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-08-25T14:50:57Zoai:ri.conicet.gov.ar:11336/81926instacron: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:34982026-08-25 14:50:58.033CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids
title Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids
spellingShingle Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids
Gutiérrez Ayesta, Cecilia
Lipase
Hydrolytic Activity
Gas Chromatography
Lecithin
Sunflower Oil
title_short Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids
title_full Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids
title_fullStr Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids
title_full_unstemmed Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids
title_sort Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids
dc.creator.none.fl_str_mv Gutiérrez Ayesta, Cecilia
Carelli Albarracin, Amalia Antonia
Ferreira, María Luján
author Gutiérrez Ayesta, Cecilia
author_facet Gutiérrez Ayesta, Cecilia
Carelli Albarracin, Amalia Antonia
Ferreira, María Luján
author_role author
author2 Carelli Albarracin, Amalia Antonia
Ferreira, María Luján
author2_role author
author
dc.subject.none.fl_str_mv Lipase
Hydrolytic Activity
Gas Chromatography
Lecithin
Sunflower Oil
topic Lipase
Hydrolytic Activity
Gas Chromatography
Lecithin
Sunflower Oil
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Lipases with different structures were investigated for their catalytic ability to hydrolyse sunflower oil, soybean lecithin and their mixtures in heptane at 60 °C in a biphasic mixture heptane-buffer pH 7.0. Besides, the substrate adsorption mechanism was studied theoretically with the Chem 3D 5.0 Ultra program and the MM2 (Cambridge Soft) method by using trilinolein and phosphatidylcholine as system models of triglycerides and phospholipids, respectively. Lipolase 100T, a granulated silica immobilised commercial preparation of Thermomyces (formerly Humicola) lanuginosa lipase, evidenced the highest conversion to fatty acids when sunflower oil (85.3% conversion to fatty acids) and its mixture with lecithin (100 % conversion to fatty acids) were tested. The free lipase from Rhizomucor meiheir (RML) evidenced the highest activity with lecithin as substrate (35.6% conversion to fatty acids). The lipases with their active sites on the surface presented the highest strength of substrate coordination – as a decrease of steric energy. In the case of RML and the artificial mix sunflower oil–lecithin, the product distribution between MG, DG and FA was: 29.70% MG, 32.96% DG and 37.34% of fatty acids (FA). When Lipolase 100T was used, the distribution was: 14.91% MG, 15.46% DG and 69.63% FA. Besides the FA, monoglycerides (MG) and diglycerides (DG) a new product was detected when lecithin was present (alone or in the mix) specially when RML was used as biocatalyst. No evidence of this peak was found after the reaction using Lipolase 100T. This new product can be related to the presence of phosphate charged group in lecithin and to the possibility of cracking of one of the hydrocarbon chains of the FA in TG. A possible reaction with the exposed active site of RML is discussed. The assignation of this new compound as a MG of a shorter fatty acid chain – with 9 carbon atoms – is presented and supported with further analytical analysis.
Fil: Gutiérrez Ayesta, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Carelli Albarracin, Amalia Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
description Lipases with different structures were investigated for their catalytic ability to hydrolyse sunflower oil, soybean lecithin and their mixtures in heptane at 60 °C in a biphasic mixture heptane-buffer pH 7.0. Besides, the substrate adsorption mechanism was studied theoretically with the Chem 3D 5.0 Ultra program and the MM2 (Cambridge Soft) method by using trilinolein and phosphatidylcholine as system models of triglycerides and phospholipids, respectively. Lipolase 100T, a granulated silica immobilised commercial preparation of Thermomyces (formerly Humicola) lanuginosa lipase, evidenced the highest conversion to fatty acids when sunflower oil (85.3% conversion to fatty acids) and its mixture with lecithin (100 % conversion to fatty acids) were tested. The free lipase from Rhizomucor meiheir (RML) evidenced the highest activity with lecithin as substrate (35.6% conversion to fatty acids). The lipases with their active sites on the surface presented the highest strength of substrate coordination – as a decrease of steric energy. In the case of RML and the artificial mix sunflower oil–lecithin, the product distribution between MG, DG and FA was: 29.70% MG, 32.96% DG and 37.34% of fatty acids (FA). When Lipolase 100T was used, the distribution was: 14.91% MG, 15.46% DG and 69.63% FA. Besides the FA, monoglycerides (MG) and diglycerides (DG) a new product was detected when lecithin was present (alone or in the mix) specially when RML was used as biocatalyst. No evidence of this peak was found after the reaction using Lipolase 100T. This new product can be related to the presence of phosphate charged group in lecithin and to the possibility of cracking of one of the hydrocarbon chains of the FA in TG. A possible reaction with the exposed active site of RML is discussed. The assignation of this new compound as a MG of a shorter fatty acid chain – with 9 carbon atoms – is presented and supported with further analytical analysis.
publishDate 2007
dc.date.none.fl_str_mv 2007-07-02
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/11336/81926
Gutiérrez Ayesta, Cecilia; Carelli Albarracin, Amalia Antonia; Ferreira, María Luján; Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids; Elsevier Science Inc; Enzyme and Microbial Technology; 41; 1-2; 2-7-2007; 35-43
0141-0229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/81926
identifier_str_mv Gutiérrez Ayesta, Cecilia; Carelli Albarracin, Amalia Antonia; Ferreira, María Luján; Relation between lipase structures and their catalityc ability to hydrolyse triglycerides and phospholipids; Elsevier Science Inc; Enzyme and Microbial Technology; 41; 1-2; 2-7-2007; 35-43
0141-0229
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/pii/S0141022906005849
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.enzmictec.2006.11.018
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 Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
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 13.364332

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