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Immobilized heterologous Rhizopus oryzae lipase: A feasible biocatalyst for the production of human milk fat substitutes

datacite.subject.sdg02:Erradicar a Fome
datacite.subject.sdg08:Trabalho Digno e Crescimento Económico
datacite.subject.sdg15:Proteger a Vida Terrestre
dc.contributor.authorTecelão, Carla
dc.contributor.authorGuillén, Marina
dc.contributor.authorValero, Francisco
dc.contributor.authorFerreira-Dias, Suzana
dc.date.accessioned2025-11-26T10:45:23Z
dc.date.available2025-11-26T10:45:23Z
dc.date.issued2012-08
dc.description.abstractThis work aims at evaluating the potentialities of a heterologous Rhizopus oryzae lipase (rROL) as a feasible biocatalyst, to be used as an alternative to commercial lipases, for the synthesis of Human Milk Fat Substitutes (HMFS). This enzyme was immobilized in three different supports (Accurel® MP 1000, Eupergit® C and Lewatit® VP OC 1600) and tested as catalysts for the acidolysis between tripalmitin and oleic acid, batchwise, at 60 ◦C, in solvent-free medium. The highest molar incorporations of oleic acid in the triacylglycerols were achieved with rROL in Lewatit® VP OC 1600 and Accurel® MP 1000, although the highest immobilization yields were observed with Eupergit® C. Quasi-equilibrium was attained after 6 h or 12 h reaction, with about 30 mol.% and 22 mol.% of oleic acid incorporation, when rROL immobilized in Lewatit and Accurel were used, respectively. Also, 23 h batch operational stability tests were performed: half-life times (t1/2) of 34.5 h and 64.0 h were achieved for rROL immobilized in Accurel® MP 1000 and in Lewatit® VP OC 1600, respectively. An important increase in the operational stability was observed for rROL immobilized in Lewatit after rehydration at the end of each batch (t1/2 = 202 h). Thus, the loss of activity may be explained by a progressive dehydration occurring along the reaction.eng
dc.description.sponsorshipThe authors are grateful to the Fundação para a Ciência e a Tecnologia (FCT), Portugal, for a PhD fellowship for Mrs. Carla Tecelão (SFRH/BD/45773/2008). This study was supported by the: (i) Program CYTED, under the scope of the “Ibero-American Network for the Extraction and Enzymatic Transformation of Functional Ingredients and Nutraceuticals from Regional Plants and Agro-Residues (ENZNUT)”, (ii) by the project CTQ2010-15131 of the Spanish Ministry of Science and Innovation, (iii) by 2009-SGR-281 and Reference Network in Biotechnology (XRB) (Generalitat de Catalunya) and by (iv) the Integrated Action Portugal-Spain E-29/11.
dc.identifier.citationCarla Tecelão, Marina Guillén, Francisco Valero, Suzana Ferreira-Dias, Immobilized heterologous Rhizopus oryzae lipase: A feasible biocatalyst for the production of human milk fat substitutes, Biochemical Engineering Journal, Volume 67, 2012, Pages 104-110, ISSN 1369-703X, https://doi.org/10.1016/j.bej.2012.06.001.
dc.identifier.doi10.1016/j.bej.2012.06.001
dc.identifier.issn1369-703X
dc.identifier.urihttp://hdl.handle.net/10400.8/14729
dc.language.isoeng
dc.peerreviewedyes
dc.publisherElsevier
dc.relationSFRH/BD/45773/2008
dc.relation.hasversionhttps://www.sciencedirect.com/science/article/pii/S1369703X12001714
dc.relation.ispartofBiochemical Engineering Journal
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectAcidolysis
dc.subjectHuman milk fat substitutes
dc.subjectImmobilization
dc.subjectRecombinant lipase
dc.subjectRhizopus oryzae
dc.subjectOperational stability
dc.titleImmobilized heterologous Rhizopus oryzae lipase: A feasible biocatalyst for the production of human milk fat substituteseng
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage110
oaire.citation.startPage104
oaire.citation.titleBiochemical Engineering Journal
oaire.citation.volume67
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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