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Production of human milk fat substitutes enriched in omega-3 polyunsaturated fatty acids using immobilized commercial lipases and Candida parapsilosis lipase/acyltransferase

2010-08Journal article Restricted access
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datacite.subject.fosEngenharia e Tecnologia::Engenharia Química
datacite.subject.fosCiências Naturais::Ciências Biológicas
datacite.subject.sdg12:Produção e Consumo Sustentáveis
datacite.subject.sdg13:Ação Climática
datacite.subject.sdg14:Proteger a Vida Marinha
dc.contributor.authorTecelão, Carla
dc.contributor.authorSilva, Joana
dc.contributor.authorDubreucq, Eric
dc.contributor.authorRibeiro, Maria H.
dc.contributor.authorFerreira-Dias, Suzana
dc.date.accessioned2025-12-09T13:04:03Z
dc.date.available2025-12-09T13:04:03Z
dc.date.issued2010-08
dc.description.abstractIn human milk fat (HMF), palmitic acid (20-30%), the major saturated fatty acid, is mostly esterified at the sn-2 position of triacylglycerols, while unsaturated fatty acids are at the sn-1,3 positions, conversely to that occurring in vegetable oils. This study aims at the production of HMF substitutes by enzyme-catalyzed interesterification of tripalmitin with (i) oleic acid (system I) or (ii) omega-3 polyunsaturated fatty acids (omega-3 PUFA) (system II) in solvent-free media. Interesterification activity and batch operational stability of commercial immobilized lipases from Rhizomucor miehei (Lipozyme RM IM), Thermomyces lanuginosa (Lipozyme TL IM) and Candida antarctica (Novozym 435) from Novozymes, DK, and Candida parapsilosis lipase/acyltransferase immobilized on Accurel MP 1000 were evaluated. After 24-h reaction at 60 °C, molar incorporation of oleic acid was about 27% for all the commercial lipases tested and 9% with C. parapsilosis enzyme. Concerning omega-3 PUFA, the highest incorporations were observed with Novozym 435 (21.6%) and Lipozyme RM IM (20%), in contrast with C. parapsilosis enzyme (8.5%) and Lipozyme TL IM (8.2%). In system I, Lipozyme RM IM maintained its activity for 10 repeated 23-h batches while for Lipozyme TL IM, Novozym 435 and C. parapsilosis enzyme, linear (half-life time, t1/2 = 154 h), series-type (t1/2 = 253 h) and first-order (t1/2 = 34.5 h) deactivations were respectively observed. In system II, Lipozyme RM IM showed linear deactivation (t1/2 = 276 h), while Novozym 435 (t1/2 = 322 h) and C. parapsilosis enzyme (t1/2 = 127 h), presented series-type deactivation. Both activity and stability of the biocatalysts depended on the acyl donor used.eng
dc.description.sponsorshipThe authors are grateful to EPAX, AS, Norway, for the gift of the “EPAX 4510TG” and Novozymes, Denmark, for the supply of the commercial immobilized lipases, to the Fundação para a Ciência e a Tecnologia (FCT), Portugal, for a PhD fellowship for Mrs. Carla Tecelão (SFRH/BD/45773/2008) and FCT and EGIDE for the financial support of the transnational cooperation programme PESSOA/Hubert Curien (“Lipase/acyltransferase-catalyzed lipid structuration”), respectively.
dc.identifier.citationCarla Tecelão, Joana Silva, Eric Dubreucq, Maria H. Ribeiro, Suzana Ferreira-Dias, Production of human milk fat substitutes enriched in omega-3 polyunsaturated fatty acids using immobilized commercial lipases and Candida parapsilosis lipase/acyltransferase, Journal of Molecular Catalysis B: Enzymatic, Volume 65, Issues 1–4, 2010, Pages 122-127, ISSN 1381-1177, https://doi.org/10.1016/j.molcatb.2010.01.026.
dc.identifier.doi10.1016/j.molcatb.2010.01.026
dc.identifier.eissn1873-3158
dc.identifier.issn1381-1177
dc.identifier.urihttp://hdl.handle.net/10400.8/14953
dc.language.isoeng
dc.peerreviewedyes
dc.publisherElsevier
dc.relation.hasversionhttps://www.sciencedirect.com/science/article/pii/S1381117710000366?via%3Dihub
dc.relation.ispartofJournal of Molecular Catalysis B: Enzymatic
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectLipase
dc.subjectHuman milk fat substitutes
dc.subjectOmega-3 polyunsaturated fatty acids
dc.subjectOperational stability
dc.subjectStructured lipids
dc.titleProduction of human milk fat substitutes enriched in omega-3 polyunsaturated fatty acids using immobilized commercial lipases and Candida parapsilosis lipase/acyltransferaseeng
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage127
oaire.citation.issue1-4
oaire.citation.startPage122
oaire.citation.titleMolecular Catalysis
oaire.citation.volume65
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85
person.familyNameTecelão
person.givenNameCarla
person.identifier.ciencia-id9B1D-4AC0-1B03
person.identifier.orcid0000-0003-2423-0495
person.identifier.scopus-author-id7801371939
relation.isAuthorOfPublication0d890808-4e69-4e6c-a631-802f1a7dce1f
relation.isAuthorOfPublication.latestForDiscovery0d890808-4e69-4e6c-a631-802f1a7dce1f

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In human milk fat (HMF), palmitic acid (20-30%), the major saturated fatty acid, is mostly esterified at the sn-2 position of triacylglycerols, while unsaturated fatty acids are at the sn-1,3 positions, conversely to that occurring in vegetable oils. This study aims at the production of HMF substitutes by enzyme-catalyzed interesterification of tripalmitin with (i) oleic acid (system I) or (ii) omega-3 polyunsaturated fatty acids (omega-3 PUFA) (system II) in solvent-free media. Interesterification activity and batch operational stability of commercial immobilized lipases from Rhizomucor miehei (Lipozyme RM IM), Thermomyces lanuginosa (Lipozyme TL IM) and Candida antarctica (Novozym 435) from Novozymes, DK, and Candida parapsilosis lipase/acyltransferase immobilized on Accurel MP 1000 were evaluated. After 24-h reaction at 60 °C, molar incorporation of oleic acid was about 27% for all the commercial lipases tested and 9% with C. parapsilosis enzyme. Concerning omega-3 PUFA, the highest incorporations were observed with Novozym 435 (21.6%) and Lipozyme RM IM (20%), in contrast with C. parapsilosis enzyme (8.5%) and Lipozyme TL IM (8.2%). In system I, Lipozyme RM IM maintained its activity for 10 repeated 23-h batches while for Lipozyme TL IM, Novozym 435 and C. parapsilosis enzyme, linear (half-life time, t1/2 = 154 h), series-type (t1/2 = 253 h) and first-order (t1/2 = 34.5 h) deactivations were respectively observed. In system II, Lipozyme RM IM showed linear deactivation (t1/2 = 276 h), while Novozym 435 (t1/2 = 322 h) and C. parapsilosis enzyme (t1/2 = 127 h), presented series-type deactivation. Both activity and stability of the biocatalysts depended on the acyl donor used.
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