Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions

Autores
Trubiano, G.; Borio, Daniel Oscar; Ferreira, María Luján
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The solvent-free esterification reaction of a commercial oleic acid and ethanol was selected as the test reaction for Candida rugosa lipase immobilized on polypropylene (PP) at 318 K (initial molar ratio 1:1). Adding of water from 0 to 30 wt. % (in gram per gram of fatty acid × 100) and the pretreatment of Candida rugosa lipase with polyethylenglycol (PEG), octane, and acetone increases the conversion to ethyl esters. The role of hydrophobic interactions of the lipase with PP and PEG was studied using molecular mechanics (MM2) for calculation of steric energies and the parametrized model (PM3) for calculation of enthalpy changes upon interaction. The nonpolar lateral groups of amino acids interact strongly with PP, whereas polar groups interact more strongly with PEG. Both interactions stabilize the open, active conformation of the lipase from Candida rugosa. Activities ranged from 5 × 10-5 to 2.0 × 10-4 mol ethyl oleate/h/mg enzyme, depending on reaction conditions. Steric energy changes vary between +30 and -10 kcal/mol, whereas the enthalpy changes ranged from +10 to -10 kcal/mol.
Fil: Trubiano, G.. 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: Borio, Daniel Oscar. 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
Esterification
Ethyl Oleate
Enzimes
Candida Rugosa Lipase
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:11336/97513
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic InteractionsTrubiano, G.Borio, Daniel OscarFerreira, María LujánEsterificationEthyl OleateEnzimesCandida Rugosa Lipasehttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2The solvent-free esterification reaction of a commercial oleic acid and ethanol was selected as the test reaction for Candida rugosa lipase immobilized on polypropylene (PP) at 318 K (initial molar ratio 1:1). Adding of water from 0 to 30 wt. % (in gram per gram of fatty acid × 100) and the pretreatment of Candida rugosa lipase with polyethylenglycol (PEG), octane, and acetone increases the conversion to ethyl esters. The role of hydrophobic interactions of the lipase with PP and PEG was studied using molecular mechanics (MM2) for calculation of steric energies and the parametrized model (PM3) for calculation of enthalpy changes upon interaction. The nonpolar lateral groups of amino acids interact strongly with PP, whereas polar groups interact more strongly with PEG. Both interactions stabilize the open, active conformation of the lipase from Candida rugosa. Activities ranged from 5 × 10-5 to 2.0 × 10-4 mol ethyl oleate/h/mg enzyme, depending on reaction conditions. Steric energy changes vary between +30 and -10 kcal/mol, whereas the enthalpy changes ranged from +10 to -10 kcal/mol.Fil: Trubiano, G.. 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: Borio, Daniel Oscar. 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; ArgentinaAmerican Chemical Society2004-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/97513Trubiano, G.; Borio, Daniel Oscar; Ferreira, María Luján; Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions; American Chemical Society; Biomacromolecules; 5; 5; 9-2004; 1832-18401525-7797CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1021/bm049828uinfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/bm049828uinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:43:30Zoai:ri.conicet.gov.ar:11336/97513instacron: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:34982025-09-29 10:43:31.185CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions
title Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions
spellingShingle Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions
Trubiano, G.
Esterification
Ethyl Oleate
Enzimes
Candida Rugosa Lipase
title_short Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions
title_full Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions
title_fullStr Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions
title_full_unstemmed Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions
title_sort Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions
dc.creator.none.fl_str_mv Trubiano, G.
Borio, Daniel Oscar
Ferreira, María Luján
author Trubiano, G.
author_facet Trubiano, G.
Borio, Daniel Oscar
Ferreira, María Luján
author_role author
author2 Borio, Daniel Oscar
Ferreira, María Luján
author2_role author
author
dc.subject.none.fl_str_mv Esterification
Ethyl Oleate
Enzimes
Candida Rugosa Lipase
topic Esterification
Ethyl Oleate
Enzimes
Candida Rugosa Lipase
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The solvent-free esterification reaction of a commercial oleic acid and ethanol was selected as the test reaction for Candida rugosa lipase immobilized on polypropylene (PP) at 318 K (initial molar ratio 1:1). Adding of water from 0 to 30 wt. % (in gram per gram of fatty acid × 100) and the pretreatment of Candida rugosa lipase with polyethylenglycol (PEG), octane, and acetone increases the conversion to ethyl esters. The role of hydrophobic interactions of the lipase with PP and PEG was studied using molecular mechanics (MM2) for calculation of steric energies and the parametrized model (PM3) for calculation of enthalpy changes upon interaction. The nonpolar lateral groups of amino acids interact strongly with PP, whereas polar groups interact more strongly with PEG. Both interactions stabilize the open, active conformation of the lipase from Candida rugosa. Activities ranged from 5 × 10-5 to 2.0 × 10-4 mol ethyl oleate/h/mg enzyme, depending on reaction conditions. Steric energy changes vary between +30 and -10 kcal/mol, whereas the enthalpy changes ranged from +10 to -10 kcal/mol.
Fil: Trubiano, G.. 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: Borio, Daniel Oscar. 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 The solvent-free esterification reaction of a commercial oleic acid and ethanol was selected as the test reaction for Candida rugosa lipase immobilized on polypropylene (PP) at 318 K (initial molar ratio 1:1). Adding of water from 0 to 30 wt. % (in gram per gram of fatty acid × 100) and the pretreatment of Candida rugosa lipase with polyethylenglycol (PEG), octane, and acetone increases the conversion to ethyl esters. The role of hydrophobic interactions of the lipase with PP and PEG was studied using molecular mechanics (MM2) for calculation of steric energies and the parametrized model (PM3) for calculation of enthalpy changes upon interaction. The nonpolar lateral groups of amino acids interact strongly with PP, whereas polar groups interact more strongly with PEG. Both interactions stabilize the open, active conformation of the lipase from Candida rugosa. Activities ranged from 5 × 10-5 to 2.0 × 10-4 mol ethyl oleate/h/mg enzyme, depending on reaction conditions. Steric energy changes vary between +30 and -10 kcal/mol, whereas the enthalpy changes ranged from +10 to -10 kcal/mol.
publishDate 2004
dc.date.none.fl_str_mv 2004-09
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/11336/97513
Trubiano, G.; Borio, Daniel Oscar; Ferreira, María Luján; Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions; American Chemical Society; Biomacromolecules; 5; 5; 9-2004; 1832-1840
1525-7797
CONICET Digital
CONICET
url http://hdl.handle.net/11336/97513
identifier_str_mv Trubiano, G.; Borio, Daniel Oscar; Ferreira, María Luján; Ethyl Oleate Synthesis Using Candida rugosa Lipase in a Solvent-Free System. Role of Hydrophobic Interactions; American Chemical Society; Biomacromolecules; 5; 5; 9-2004; 1832-1840
1525-7797
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/bm049828u
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/bm049828u
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
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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_ 1844614470745194496
score 13.070432

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