Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase

This study aims to produce human milk fat substitutes (HMFS) rich in polyunsaturated fatty acids (PUFA), mainly the essential omega-3 linolenic acid, by acidolysis reaction between tripalmitin (PPP) and free fatty acids (FFA) from camelina oil, in stirred batch reactor and solvent-free media. The no...

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Autores: Faustino, Ana Rita, Osório, Natália M., Tecelão, Carla, Canet, Albert|||0009-0000-8487-8176, Valero, Francisco|||0000-0003-0429-9620, Ferreira-Dias, Suzana
Tipo de recurso: artículo
Fecha de publicación:2016
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:322366
Acceso en línea:https://ddd.uab.cat/record/322366
https://dx.doi.org/urn:doi:10.1002/ejlt.201500003
Access Level:acceso abierto
Palabra clave:Acidolysis
Camelina oil
Human milk fat substitutes
Polyunsaturated fatty acids
Rhizopus oryzae lipase
Structured lipids
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spelling Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipaseFaustino, Ana RitaOsório, Natália M.Tecelão, CarlaCanet, Albert|||0009-0000-8487-8176Valero, Francisco|||0000-0003-0429-9620Ferreira-Dias, SuzanaAcidolysisCamelina oilHuman milk fat substitutesPolyunsaturated fatty acidsRhizopus oryzae lipaseStructured lipidsThis study aims to produce human milk fat substitutes (HMFS) rich in polyunsaturated fatty acids (PUFA), mainly the essential omega-3 linolenic acid, by acidolysis reaction between tripalmitin (PPP) and free fatty acids (FFA) from camelina oil, in stirred batch reactor and solvent-free media. The non-commercial heterologous Rhizopus oryzae lipase (rROL), immobilized on Lewatit VP OC 1600 or on Relizyme OD403/S, and the immobilized commercial lipase from Rhizomucor miehei (Lipozyme RM IM) were tested as biocatalysts. Both lipases are sn-1,3 selective. After 24 h reaction at 60°C, using biocatalyst loads of 5 wt% (in relation to tripalmitin), 48.9, 43.6, and 18.3 mol% of fatty acid incorporation in triacylglycerols (TAG) were obtained with Lipozyme RM IM and rROL immobilized on Lewatit or on Relizyme, respectively. rROL immobilized on Lewatit was selected as biocatalyst for the acidolysis, as alternative to the commercial immobilized lipases. With this biocatalyst, the molar incorporation increased with its initial water activity (0.55-0.95). Modeling acidolysis catalyzed by rROL immobilized on Lewatit was performed by response surface methodology, as a function of temperature (58-72°C) and molar ratio FFA:PPP (1.2:1-6.8:1). The highest PPP consumption was achieved at 60°C with a molar ratio of 2:1. The yield of HMFS (new TAG) increased from 42.6 wt% (5% biocatalyst load) to 52% with 8% load, after 24 h acidolysis. Practical applications: Camelina oil showed to be a good source of PUFA, mainly essential fatty acids, to incorporate in HMFS. After 24 h acidolysis under optimized conditions, catalyzed by the non-commercial sn-1,3 regioselective rROL immobilized on Lewatit VP OC 1600, the TAG fraction contains 67.7 mol% of palmitic acid at position 2. These structured lipids rich in PUFA can be used in blends with 1,3-dioleoyl-2-palmitoyl-glycerol (OPO) in order to mimic the human milk fat. The performance of this biocatalyst was comparable to that observed with Lipozyme RM IM. The replacement of high-cost commercial immobilized lipases by rROL immobilized on Lewatit may reduce the biocatalyst cost. In addition, since the best molar ratio FFA:PPP for rROL is 2:1, i.e., the stoichiometric value for the acidolysis catalyzed by sn-1,3 regioselective lipases, the use of this biocatalyst will reduce downstream costs related with unconverted FFA recovery. 22016-01-0120162016-01-01Articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/322366https://dx.doi.org/urn:doi:10.1002/ejlt.201500003reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengMinisterio de Economía y Competitividad https://doi.org/10.13039/501100003329 CTQ2013-42391-RAgència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2014/SGR-452open accesshttp://purl.org/coar/access_right/c_abf2Aquest material està protegit per drets d'autor i/o drets afins. Podeu utilitzar aquest material en funció del que permet la legislació de drets d'autor i drets afins d'aplicació al vostre cas. Per a d'altres usos heu d'obtenir permís del(s) titular(s) de drets.https://rightsstatements.org/vocab/InC/1.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:3223662026-06-06T12:50:31Z
dc.title.none.fl_str_mv Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase
title Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase
spellingShingle Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase
Faustino, Ana Rita
Acidolysis
Camelina oil
Human milk fat substitutes
Polyunsaturated fatty acids
Rhizopus oryzae lipase
Structured lipids
title_short Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase
title_full Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase
title_fullStr Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase
title_full_unstemmed Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase
title_sort Camelina oil as a source of polyunsaturated fatty acids for the production of human milk fat substitutes catalyzed by a heterologous Rhizopus oryzae lipase
dc.creator.none.fl_str_mv Faustino, Ana Rita
Osório, Natália M.
Tecelão, Carla
Canet, Albert|||0009-0000-8487-8176
Valero, Francisco|||0000-0003-0429-9620
Ferreira-Dias, Suzana
author Faustino, Ana Rita
author_facet Faustino, Ana Rita
Osório, Natália M.
Tecelão, Carla
Canet, Albert|||0009-0000-8487-8176
Valero, Francisco|||0000-0003-0429-9620
Ferreira-Dias, Suzana
author_role author
author2 Osório, Natália M.
Tecelão, Carla
Canet, Albert|||0009-0000-8487-8176
Valero, Francisco|||0000-0003-0429-9620
Ferreira-Dias, Suzana
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Acidolysis
Camelina oil
Human milk fat substitutes
Polyunsaturated fatty acids
Rhizopus oryzae lipase
Structured lipids
topic Acidolysis
Camelina oil
Human milk fat substitutes
Polyunsaturated fatty acids
Rhizopus oryzae lipase
Structured lipids
description This study aims to produce human milk fat substitutes (HMFS) rich in polyunsaturated fatty acids (PUFA), mainly the essential omega-3 linolenic acid, by acidolysis reaction between tripalmitin (PPP) and free fatty acids (FFA) from camelina oil, in stirred batch reactor and solvent-free media. The non-commercial heterologous Rhizopus oryzae lipase (rROL), immobilized on Lewatit VP OC 1600 or on Relizyme OD403/S, and the immobilized commercial lipase from Rhizomucor miehei (Lipozyme RM IM) were tested as biocatalysts. Both lipases are sn-1,3 selective. After 24 h reaction at 60°C, using biocatalyst loads of 5 wt% (in relation to tripalmitin), 48.9, 43.6, and 18.3 mol% of fatty acid incorporation in triacylglycerols (TAG) were obtained with Lipozyme RM IM and rROL immobilized on Lewatit or on Relizyme, respectively. rROL immobilized on Lewatit was selected as biocatalyst for the acidolysis, as alternative to the commercial immobilized lipases. With this biocatalyst, the molar incorporation increased with its initial water activity (0.55-0.95). Modeling acidolysis catalyzed by rROL immobilized on Lewatit was performed by response surface methodology, as a function of temperature (58-72°C) and molar ratio FFA:PPP (1.2:1-6.8:1). The highest PPP consumption was achieved at 60°C with a molar ratio of 2:1. The yield of HMFS (new TAG) increased from 42.6 wt% (5% biocatalyst load) to 52% with 8% load, after 24 h acidolysis. Practical applications: Camelina oil showed to be a good source of PUFA, mainly essential fatty acids, to incorporate in HMFS. After 24 h acidolysis under optimized conditions, catalyzed by the non-commercial sn-1,3 regioselective rROL immobilized on Lewatit VP OC 1600, the TAG fraction contains 67.7 mol% of palmitic acid at position 2. These structured lipids rich in PUFA can be used in blends with 1,3-dioleoyl-2-palmitoyl-glycerol (OPO) in order to mimic the human milk fat. The performance of this biocatalyst was comparable to that observed with Lipozyme RM IM. The replacement of high-cost commercial immobilized lipases by rROL immobilized on Lewatit may reduce the biocatalyst cost. In addition, since the best molar ratio FFA:PPP for rROL is 2:1, i.e., the stoichiometric value for the acidolysis catalyzed by sn-1,3 regioselective lipases, the use of this biocatalyst will reduce downstream costs related with unconverted FFA recovery.
publishDate 2016
dc.date.none.fl_str_mv 2
2016-01-01
2016
2016-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
AM
http://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/322366
https://dx.doi.org/urn:doi:10.1002/ejlt.201500003
url https://ddd.uab.cat/record/322366
https://dx.doi.org/urn:doi:10.1002/ejlt.201500003
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 CTQ2013-42391-R
Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2014/SGR-452
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://rightsstatements.org/vocab/InC/1.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://rightsstatements.org/vocab/InC/1.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
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