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dc.contributor.authorPellicer, José Antonio
dc.contributor.authorNavarro, Patricia
dc.contributor.authorHernández Sánchez, Pilar
dc.contributor.authorGómez López, Vicente Manuel
dc.date.accessioned2021-03-05T14:40:23Z
dc.date.available2021-03-05T14:40:23Z
dc.date.issued2019
dc.identifier.citationJosé Antonio Pellicer, Patricia Navarro, Pilar Hernández Sánchez, Vicente M. Gómez-López, Structural changes associated with the inactivation of lipoxygenase by pulsed light, LWT, Volume 113, 2019, 108332, ISSN 0023-6438, https://doi.org/10.1016/j.lwt.2019.108332. (https://www.sciencedirect.com/science/article/pii/S0023643819306747)es
dc.identifier.issn0023-6438
dc.identifier.urihttp://hdl.handle.net/10952/4823
dc.description.abstractPulsed light (PL) is a non-thermal technology able to inactivate enzymes. Lipoxygenase (LOX) causes enzymatic rancidity in some foods. This study aimed to determine the structural changes associated with the PL inactivation of LOX and used measurements of residual activity, temperature, spectropolarimetry, fluorescence, spectrophotometry, free sulfhydryl and carbonyl contents and electrophoresis. LOX inactivation was non-log-linear, with a slight temperature rise. PL significantly increased the concentration of carbonlys and free-sulfhydryls of LOX and caused loss of ellipticity and intrinsic fluorescence, a red shift in the intrinsic fluorescence peak and an increase in 1-anilino-8-naphthalenesulfonate fluorescence. The turbidity of LOX sample increased during inactivation and electrophoretic bands faded. Phase diagram analysis showed no evidence of formation of intermediates. In summary, the inactivation of LOX by PL followed a Weibull kinetics, is exclusively photochemical and is an all-or-none process where the protein gets oxidized, decreases its α-helix content, unfolds and aggregates.es
dc.language.isoenes
dc.publisherElsevieres
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectPulsed lightes
dc.subjectLipoxygenase inactivationes
dc.subjectEnzyme structurees
dc.subjectSoybeanes
dc.titleStructural changes associated with the inactivation of lipoxygenase by pulse lightes
dc.typearticlees
dc.rights.accessRightsopenAccesses
dc.relation.projectIDThis work was supported by Universidad Católica de Murcia, grant PMAFI/29/14.es
dc.journal.titleLWT-Food Science and Technologyes
dc.volume.number113es
dc.description.disciplineCiencias de la Alimentaciónes
dc.identifier.doi10.1016/j.lwt.2019.108332es


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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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