Lipase-catalyzed modification of butterfat via acidolysis with oleic acid
Autor(a) principal: | |
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Data de Publicação: | 1997 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.14/6612 |
Resumo: | During the last decade increased interest in reactions catalyzed by lipases from various microbial sources has prompted attempts to rationally design lipases and lipase-catalyzed processes aiming at modification of functional properties of oils and fats. The present communication reports experimental work on the chemical modification of anhydrous butterfat via interesterification reactions with oleic acid catalyzed by a commercial lipase immobilized by plain physical adsorption on a bundle of hydrophobic hollow fibers. The main goal of this research effort was to engineer butterfat so as to increase its level of unsaturated fatty acid residues (viz. oleic acid) and concomitantly decrease its level of medium-to-long chain saturated fatty acid residues (viz. myristic and palmitic acids). All reactions were carried out at 40 °C in the absence of any solvent but under controlled water activity, and their extent was monitored via Chromatographic assays for free fatty acids. Although a certain degree of net hydrolysis of butterfat was observed, the enzymatic process studied was technically feasible and able to reach the predefined goals. |
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Lipase-catalyzed modification of butterfat via acidolysis with oleic acidButterfatFatty acidLipaseMucor javanicusHollow fiber reactorInteresterificationImmobilizationDuring the last decade increased interest in reactions catalyzed by lipases from various microbial sources has prompted attempts to rationally design lipases and lipase-catalyzed processes aiming at modification of functional properties of oils and fats. The present communication reports experimental work on the chemical modification of anhydrous butterfat via interesterification reactions with oleic acid catalyzed by a commercial lipase immobilized by plain physical adsorption on a bundle of hydrophobic hollow fibers. The main goal of this research effort was to engineer butterfat so as to increase its level of unsaturated fatty acid residues (viz. oleic acid) and concomitantly decrease its level of medium-to-long chain saturated fatty acid residues (viz. myristic and palmitic acids). All reactions were carried out at 40 °C in the absence of any solvent but under controlled water activity, and their extent was monitored via Chromatographic assays for free fatty acids. Although a certain degree of net hydrolysis of butterfat was observed, the enzymatic process studied was technically feasible and able to reach the predefined goals.ElsevierVeritati - Repositório Institucional da Universidade Católica PortuguesaBalcão, Victor M.Malcata, F. Xavier2011-10-21T09:46:02Z19971997-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/6612engBALCÃO, Victor M. ; MALCATA, F. Xavier - Lipase-catalyzed modification of butterfat via acidolysis with oleic acid. Journal of Molecular Catalysis B: Enzymatic. ISSN 1381-1177. 3:1-4 (1997) 161-169info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-12T17:10:53Zoai:repositorio.ucp.pt:10400.14/6612Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:06:02.971591Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Lipase-catalyzed modification of butterfat via acidolysis with oleic acid |
title |
Lipase-catalyzed modification of butterfat via acidolysis with oleic acid |
spellingShingle |
Lipase-catalyzed modification of butterfat via acidolysis with oleic acid Balcão, Victor M. Butterfat Fatty acid Lipase Mucor javanicus Hollow fiber reactor Interesterification Immobilization |
title_short |
Lipase-catalyzed modification of butterfat via acidolysis with oleic acid |
title_full |
Lipase-catalyzed modification of butterfat via acidolysis with oleic acid |
title_fullStr |
Lipase-catalyzed modification of butterfat via acidolysis with oleic acid |
title_full_unstemmed |
Lipase-catalyzed modification of butterfat via acidolysis with oleic acid |
title_sort |
Lipase-catalyzed modification of butterfat via acidolysis with oleic acid |
author |
Balcão, Victor M. |
author_facet |
Balcão, Victor M. Malcata, F. Xavier |
author_role |
author |
author2 |
Malcata, F. Xavier |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Veritati - Repositório Institucional da Universidade Católica Portuguesa |
dc.contributor.author.fl_str_mv |
Balcão, Victor M. Malcata, F. Xavier |
dc.subject.por.fl_str_mv |
Butterfat Fatty acid Lipase Mucor javanicus Hollow fiber reactor Interesterification Immobilization |
topic |
Butterfat Fatty acid Lipase Mucor javanicus Hollow fiber reactor Interesterification Immobilization |
description |
During the last decade increased interest in reactions catalyzed by lipases from various microbial sources has prompted attempts to rationally design lipases and lipase-catalyzed processes aiming at modification of functional properties of oils and fats. The present communication reports experimental work on the chemical modification of anhydrous butterfat via interesterification reactions with oleic acid catalyzed by a commercial lipase immobilized by plain physical adsorption on a bundle of hydrophobic hollow fibers. The main goal of this research effort was to engineer butterfat so as to increase its level of unsaturated fatty acid residues (viz. oleic acid) and concomitantly decrease its level of medium-to-long chain saturated fatty acid residues (viz. myristic and palmitic acids). All reactions were carried out at 40 °C in the absence of any solvent but under controlled water activity, and their extent was monitored via Chromatographic assays for free fatty acids. Although a certain degree of net hydrolysis of butterfat was observed, the enzymatic process studied was technically feasible and able to reach the predefined goals. |
publishDate |
1997 |
dc.date.none.fl_str_mv |
1997 1997-01-01T00:00:00Z 2011-10-21T09:46:02Z |
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/10400.14/6612 |
url |
http://hdl.handle.net/10400.14/6612 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
BALCÃO, Victor M. ; MALCATA, F. Xavier - Lipase-catalyzed modification of butterfat via acidolysis with oleic acid. Journal of Molecular Catalysis B: Enzymatic. ISSN 1381-1177. 3:1-4 (1997) 161-169 |
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:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799131726408056832 |