Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents

Detalhes bibliográficos
Autor(a) principal: Rocha, J. M. S.
Data de Publicação: 1999
Outros Autores: Gil, M. H., Garcia, F. A. P.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10316/8193
https://doi.org/10.1002/(SICI)1097-4660(199907)74:7<607::AID-JCTB74>3.0.CO;2-N
Resumo: The enzymatic synthesis of n-octyl oleate by direct esterification of the oleic acid and the octanol in a solvent-free medium was previously shown to be efficiently catalysed by a lipase from Rhizomucor miehei covalently linked to a graft copolymer, the partially hydrolysed poly(ethylene)-g co-hydroxyethyl methacrylate (PE-g co-HEMA). In this work we went further towards an optimisation of the production of n-octyl oleate taking into account several parameters that affect the catalytic activity of the preparation. The physical characteristics of the support, such as the particle size and the degree of hydrolysis of the copolymer, the amount of lipase used in the method of immobilisation, the water content of the reaction mixture and the operational conditions of reaction, in particular the temperature, were evaluated in order to achieve not only high activities but also a good stability of the preparation. © 1999 Society of Chemical Industry
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spelling Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solventsThe enzymatic synthesis of n-octyl oleate by direct esterification of the oleic acid and the octanol in a solvent-free medium was previously shown to be efficiently catalysed by a lipase from Rhizomucor miehei covalently linked to a graft copolymer, the partially hydrolysed poly(ethylene)-g co-hydroxyethyl methacrylate (PE-g co-HEMA). In this work we went further towards an optimisation of the production of n-octyl oleate taking into account several parameters that affect the catalytic activity of the preparation. The physical characteristics of the support, such as the particle size and the degree of hydrolysis of the copolymer, the amount of lipase used in the method of immobilisation, the water content of the reaction mixture and the operational conditions of reaction, in particular the temperature, were evaluated in order to achieve not only high activities but also a good stability of the preparation. © 1999 Society of Chemical Industry1999info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/8193http://hdl.handle.net/10316/8193https://doi.org/10.1002/(SICI)1097-4660(199907)74:7<607::AID-JCTB74>3.0.CO;2-NengJournal of Chemical Technology & Biotechnology. 74:7 (1999) 607-612Rocha, J. M. S.Gil, M. H.Garcia, F. A. P.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2020-05-29T09:42:38Zoai:estudogeral.uc.pt:10316/8193Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:59:19.455552Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
title Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
spellingShingle Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
Rocha, J. M. S.
title_short Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
title_full Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
title_fullStr Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
title_full_unstemmed Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
title_sort Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
author Rocha, J. M. S.
author_facet Rocha, J. M. S.
Gil, M. H.
Garcia, F. A. P.
author_role author
author2 Gil, M. H.
Garcia, F. A. P.
author2_role author
author
dc.contributor.author.fl_str_mv Rocha, J. M. S.
Gil, M. H.
Garcia, F. A. P.
description The enzymatic synthesis of n-octyl oleate by direct esterification of the oleic acid and the octanol in a solvent-free medium was previously shown to be efficiently catalysed by a lipase from Rhizomucor miehei covalently linked to a graft copolymer, the partially hydrolysed poly(ethylene)-g co-hydroxyethyl methacrylate (PE-g co-HEMA). In this work we went further towards an optimisation of the production of n-octyl oleate taking into account several parameters that affect the catalytic activity of the preparation. The physical characteristics of the support, such as the particle size and the degree of hydrolysis of the copolymer, the amount of lipase used in the method of immobilisation, the water content of the reaction mixture and the operational conditions of reaction, in particular the temperature, were evaluated in order to achieve not only high activities but also a good stability of the preparation. © 1999 Society of Chemical Industry
publishDate 1999
dc.date.none.fl_str_mv 1999
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10316/8193
http://hdl.handle.net/10316/8193
https://doi.org/10.1002/(SICI)1097-4660(199907)74:7<607::AID-JCTB74>3.0.CO;2-N
url http://hdl.handle.net/10316/8193
https://doi.org/10.1002/(SICI)1097-4660(199907)74:7<607::AID-JCTB74>3.0.CO;2-N
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of Chemical Technology & Biotechnology. 74:7 (1999) 607-612
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