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dc.creatorPérez Gómez, Dolores
dc.creatorMartín Rengel, Sara
dc.creatorFernández-Lorente, Gloria
dc.creatorFilice, Marco
dc.creatorGuisán, José Manuel
dc.creatorVentosa Ucero, Antonio
dc.creatorGarcía Gutiérrez, María Teresa
dc.creatorMellado Durán, María Encarnación
dc.date.accessioned2015-01-19T13:28:46Z
dc.date.available2015-01-19T13:28:46Z
dc.date.issued2011
dc.identifier.citationPérez Gómez, D., Martín Rengel, S., Fernández-Lorente, G., Filice, M., Guisán, J.M., Ventosa Ucero, A.,...,Mellado Durán, M.E. (2011). A Novel Halophilic Lipase, LipBL, Showing High Efficiency in the Production of Eicosapentaenoic Acid (EPA). PLoS One, 6 (8), e23325-1-e23325-11.
dc.identifier.issn1932-6203es
dc.identifier.urihttp://hdl.handle.net/11441/17823
dc.description.abstractBackground: Among extremophiles, halophiles are defined as microorganisms adapted to live and thrive in diverse extreme saline environments. These extremophilic microorganisms constitute the source of a number of hydrolases with great biotechnological applications. The interest to use extremozymes from halophiles in industrial applications is their resistance to organic solvents and extreme temperatures. Marinobacter lipolyticus SM19 is a moderately halophilic bacterium, isolated previously from a saline habitat in South Spain, showing lipolytic activity. Methods and Findings: A lipolytic enzyme from the halophilic bacterium Marinobacter lipolyticus SM19 was isolated. This enzyme, designated LipBL, was expressed in Escherichia coli. LipBL is a protein of 404 amino acids with a molecular mass of 45.3 kDa and high identity to class C b-lactamases. LipBL was purified and biochemically characterized. The temperature for its maximal activity was 80uC and the pH optimum determined at 25uC was 7.0, showing optimal activity without sodium chloride, while maintaining 20% activity in a wide range of NaCl concentrations. This enzyme exhibited high activity against short-medium length acyl chain substrates, although it also hydrolyzes olive oil and fish oil. The fish oil hydrolysis using LipBL results in an enrichment of free eicosapentaenoic acid (EPA), but not docosahexaenoic acid (DHA), relative to its levels present in fish oil. For improving the stability and to be used in industrial processes LipBL was immobilized in different supports. The immobilized derivatives CNBr-activated Sepharose were highly selective towards the release of EPA versus DHA. The enzyme is also active towards different chiral and prochiral esters. Exposure of LipBL to buffer-solvent mixtures showed that the enzyme had remarkable activity and stability in all organic solvents tested. Conclusions: In this study we isolated, purified, biochemically characterized and immobilized a lipolytic enzyme from a halophilic bacterium M. lipolyticus, which constitutes an enzyme with excellent properties to be used in the food industry, in the enrichment in omega-3 PUFAs.es
dc.language.isoenges
dc.publisherPublic Library of Science
dc.relation.ispartofPLoS One, 6 (8), e23325-1-e23325-11.
dc.rightsAtribución-NoComercial-SinDerivadas 4.0 España*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleA Novel Halophilic Lipase, LipBL, Showing High Efficiency in the Production of Eicosapentaenoic Acid (EPA)es
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Microbiología y Parasitologíaes
dc.relation.publisherversionhttps://doi.org/10.1371/journal.pone.0023325
dc.identifier.doi10.1371/journal.pone.0023325
dc.journaltitlePLoS Onees
dc.publication.volumen6es
dc.publication.issue8es
dc.publication.initialPagee23325-1es
dc.publication.endPagee23325-11es
dc.identifier.idushttps://idus.us.es/xmlui/handle/11441/17823

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