Caracterización genética y bioquímica de esterasas de compuestos fenólicos de Lactobacillus plantarum

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dc.contributor.advisor Muñoz Moreno, Rosario (dir.)
dc.contributor.advisor Rivas González del Rey, Blanca de las (dir.)
dc.contributor.author Esteban Torres, María del Mar
dc.contributor.other UAM. Departamento de Química Física Aplicada es_ES
dc.contributor.other CSIC. Instituto de Ciencia y Tecnología de Alimentos y Nutrición es_ES
dc.date.accessioned 2015-01-27T16:01:56Z
dc.date.available 2015-01-27T16:01:56Z
dc.date.issued 2014-10-22
dc.identifier.uri http://hdl.handle.net/10486/663400
dc.description Tesis doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departamento de Química Física Aplicada. Fecha de lectura: 22-10-2014 es_ES
dc.description.abstract Phenolic esters are important constituents of food products of plant origin and are directly related to sensory characteristics of foods. These compounds, particularly hydroxycinnamoyl esters, are abundant, naturally occurring molecules that contribute to the rigidity of plant cell walls. Lactobacillus plantarum is frequently found in the fermentation of plant-derived food products, where hydroxycinnamoyl esters are common. Metabolic pathways of biosynthesis or degradation of phenolic compounds in L. plantarum have been described. Among the enzymes involved in the metabolism of phenolic compounds are esterases such as arylesterases and feruloyl esterases. Arylesterases are active toward aromatic esters while feruloyl esterases preferably act against hydroxycinnamoyl esters. Precisely, feruloyl esterases are involved in the release of phenolic compounds from plant cell walls, such as ferulic, p-coumaric, caffeic and sinapic acids. Although several esterases have been characterized in L. plantarum, enzymes having arylesterases and feruloyl esterases have not been described so far. Whereas cultures from L. plantarum WCFS1 were unable to hydrolyze hydroxycinnamoyl esters, cell extracts from this strain partially hydrolyze methyl ferulate and methyl p-coumarate. Moreover, cultures of some L. plantarum strains present feruloyl esterase activity. In this study, in order to determine the esterases from L. plantarum responsible for these activities, the putative Lp_0796, Lp_0973, Lp_1002, Lp_1760, Lp_2631, Lp_2923, Lp_3505, Lp_3561 Lp_3562 and Est_1092 esterases have been recombinantly overproduced and biochemically characterized. These enzymes exhibited arylesterase activity as they hydrolyzed phenyl acetate efficiently. Remarkably, Lp_0796 and Est_1092 also hydrolyse the four model substrates archetypical for feruloyl esterases. Upon methyl ferulate exposure, the expression of est_1092 was induced, whereas lp_0796 expression was not affected. Est_1092 was present in 7 out of 29 L. plantarum strains, whose cultures exhibited feruloyl esterase activity. The presence of Est_1092 in L. plantarum WCFS1 cultures (which is unable to hydrolyze hydroxycinnamoyl esters) conferred feruloyl esterase activity to this strain. In this study, we describe for the first time the metabolism of hydroxycinnamoyl esters by L. plantarum, reporting the analyses of novel arylesterases and feruloyl esterases en_US
dc.format.extent 204 pag. es_ES
dc.format.mimetype application/pdf en
dc.language.iso spa en
dc.subject.other Lactobacilos - Tesis doctorales es_ES
dc.subject.other Fenoles - Tesis doctorales es_ES
dc.subject.other Enzimas - Tesis doctorales es_ES
dc.title Caracterización genética y bioquímica de esterasas de compuestos fenólicos de Lactobacillus plantarum es_ES
dc.type doctoralThesis en
dc.subject.eciencia Física es_ES
dc.subject.eciencia Química es_ES
dc.rights.cc Reconocimiento – NoComercial – SinObraDerivada es_ES
dc.rights.accessRights openAccess en


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