Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure

Bibliographic Details
Main Author: Osório, N.M.
Publication Date: 2008
Other Authors: Ribeiro, M.H., Fonseca, M.M.R., Ferreira-Dias, S.
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: http://hdl.handle.net/10400.5/5632
Summary: The interesterification of natural fats will improve certain physical and nutraceutical properties by modification of their acylglycerol profile. In this study, the effect of high pressure in the interesterification kinetics of fat blends, in solvent-free medium, catalysed by a commercial immobilized lipase from Thermomyces lanuginosa was evaluated. Reaction media were ternary blends of palm stearin, palm kernel oil and a concentrate of triacylglycerols (TAG) rich in -3 polyunsaturated fatty acids. Reactions were carried out at 60 ◦C, at 0.1, 50, 100 and 150MPa. The interesterification was followed (i) by the decrease in “Solid Fat Content” values of the blend at 35 ◦C (SFC35 ◦C) and (ii) by the changes in the acylglycerol profile. The biocatalyst presented interesterification activity at least up to 150MPa. Results obtained at 0.1MPa, with no agitation of the reaction medium, were found to be similar to those obtained under high-pressure conditions. The observed decrease in SFC35 ◦C values was accompanied by important changes in the acylglycerol profile. An increase in compounds of low equivalent carbon number (ECN) and in TAG of ECN 44 and 46 were observed. This increase was accompanied by a consumption of TAG of ECN 48 and 50 for all pressure values, and also of trilaurin (ECN = 36) at normal pressure. High pressures seem to affect lipase selectivity towards lauric acid. Batch operational stability tests showed a linear inactivation profile for each pressure. Half-lives of about 15, 6 and 4 h were estimated for the biocatalyst under 0.1, 50 and 150MPa, respectively
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spelling Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressurehigh pressureimmobilized lipaseinteresterificationomega-3 polyunsaturated fatty acidsoperational stabilityThe interesterification of natural fats will improve certain physical and nutraceutical properties by modification of their acylglycerol profile. In this study, the effect of high pressure in the interesterification kinetics of fat blends, in solvent-free medium, catalysed by a commercial immobilized lipase from Thermomyces lanuginosa was evaluated. Reaction media were ternary blends of palm stearin, palm kernel oil and a concentrate of triacylglycerols (TAG) rich in -3 polyunsaturated fatty acids. Reactions were carried out at 60 ◦C, at 0.1, 50, 100 and 150MPa. The interesterification was followed (i) by the decrease in “Solid Fat Content” values of the blend at 35 ◦C (SFC35 ◦C) and (ii) by the changes in the acylglycerol profile. The biocatalyst presented interesterification activity at least up to 150MPa. Results obtained at 0.1MPa, with no agitation of the reaction medium, were found to be similar to those obtained under high-pressure conditions. The observed decrease in SFC35 ◦C values was accompanied by important changes in the acylglycerol profile. An increase in compounds of low equivalent carbon number (ECN) and in TAG of ECN 44 and 46 were observed. This increase was accompanied by a consumption of TAG of ECN 48 and 50 for all pressure values, and also of trilaurin (ECN = 36) at normal pressure. High pressures seem to affect lipase selectivity towards lauric acid. Batch operational stability tests showed a linear inactivation profile for each pressure. Half-lives of about 15, 6 and 4 h were estimated for the biocatalyst under 0.1, 50 and 150MPa, respectivelyElsevierRepositório da Universidade de LisboaOsório, N.M.Ribeiro, M.H.Fonseca, M.M.R.Ferreira-Dias, S.2013-06-05T15:38:01Z20082008-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.5/5632eng"Journal of Molecular Catalysis. B: Enzymatic". ISSN 1381-1177. 52-53 (2008) 58-661381-1177info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2025-03-17T16:00:05Zoai:repositorio.ulisboa.pt:10400.5/5632Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-29T03:59:52.276761Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
title Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
spellingShingle Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
Osório, N.M.
high pressure
immobilized lipase
interesterification
omega-3 polyunsaturated fatty acids
operational stability
title_short Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
title_full Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
title_fullStr Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
title_full_unstemmed Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
title_sort Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
author Osório, N.M.
author_facet Osório, N.M.
Ribeiro, M.H.
Fonseca, M.M.R.
Ferreira-Dias, S.
author_role author
author2 Ribeiro, M.H.
Fonseca, M.M.R.
Ferreira-Dias, S.
author2_role author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Osório, N.M.
Ribeiro, M.H.
Fonseca, M.M.R.
Ferreira-Dias, S.
dc.subject.por.fl_str_mv high pressure
immobilized lipase
interesterification
omega-3 polyunsaturated fatty acids
operational stability
topic high pressure
immobilized lipase
interesterification
omega-3 polyunsaturated fatty acids
operational stability
description The interesterification of natural fats will improve certain physical and nutraceutical properties by modification of their acylglycerol profile. In this study, the effect of high pressure in the interesterification kinetics of fat blends, in solvent-free medium, catalysed by a commercial immobilized lipase from Thermomyces lanuginosa was evaluated. Reaction media were ternary blends of palm stearin, palm kernel oil and a concentrate of triacylglycerols (TAG) rich in -3 polyunsaturated fatty acids. Reactions were carried out at 60 ◦C, at 0.1, 50, 100 and 150MPa. The interesterification was followed (i) by the decrease in “Solid Fat Content” values of the blend at 35 ◦C (SFC35 ◦C) and (ii) by the changes in the acylglycerol profile. The biocatalyst presented interesterification activity at least up to 150MPa. Results obtained at 0.1MPa, with no agitation of the reaction medium, were found to be similar to those obtained under high-pressure conditions. The observed decrease in SFC35 ◦C values was accompanied by important changes in the acylglycerol profile. An increase in compounds of low equivalent carbon number (ECN) and in TAG of ECN 44 and 46 were observed. This increase was accompanied by a consumption of TAG of ECN 48 and 50 for all pressure values, and also of trilaurin (ECN = 36) at normal pressure. High pressures seem to affect lipase selectivity towards lauric acid. Batch operational stability tests showed a linear inactivation profile for each pressure. Half-lives of about 15, 6 and 4 h were estimated for the biocatalyst under 0.1, 50 and 150MPa, respectively
publishDate 2008
dc.date.none.fl_str_mv 2008
2008-01-01T00:00:00Z
2013-06-05T15:38:01Z
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/10400.5/5632
url http://hdl.handle.net/10400.5/5632
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv "Journal of Molecular Catalysis. B: Enzymatic". ISSN 1381-1177. 52-53 (2008) 58-66
1381-1177
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron:RCAAP
instname_str FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron_str RCAAP
institution RCAAP
reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
repository.mail.fl_str_mv info@rcaap.pt
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