Optimisation of the enzymatic synthesis of n-octyl oleate with immobilised lipase in the absence of solvents
Autor(a) principal: | |
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Data de Publicação: | 1999 |
Outros Autores: | , |
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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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 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799133884180332544 |