Interesterification of fat blends rich in omega-3 polyunsaturated fatty acids catalysed by immobilized Thermomyces lanuginosa lipase under high pressure
Main Author: | |
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Publication Date: | 2008 |
Other Authors: | , , |
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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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 |
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info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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application/pdf |
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Elsevier |
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Elsevier |
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