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hal.structure.identifierInstitut de Chimie Radicalaire [ICR]
dc.contributor.authorAUDRAN, Gérard
dc.contributor.authorJACOUTOT, Samuel
hal.structure.identifierCentre de résonance magnétique des systèmes biologiques [CRMSB]
dc.contributor.authorJUGNIOT, Natacha
hal.structure.identifierInstitut Lavoisier de Versailles [ILV]
dc.contributor.authorMARQUE, Sylvain
hal.structure.identifierCentre de résonance magnétique des systèmes biologiques [CRMSB]
dc.contributor.authorMELLET, Philippe
dc.date.accessioned2021-10-07T16:28:54Z
dc.date.available2021-10-07T16:28:54Z
dc.date.issued2019
dc.identifier.issn0003-2700
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/112620
dc.description.abstractEnWhile optical methods are not efficient enough for the easy, fast, and efficient detection of enzymatic activity in turbid media, the properties of the electron paramagnetic resonance (EPR) technique make it suitable for use in such media. Nitroxides which exhibit a change in their EPR hyperfine coupling constants upon enzymatic activity and are selective to lipases were developed under the name of shifting-nitroxides. Several fatty acids, exhibiting saturated and unsaturated chains of various lengths, were coupled with the shifting-nitroxide via an enol ester link and tested against several lipases. As the solubility of fatty acids is low in HEPES buffer, experiments were performed in turbid aqueous solution. Almost all labeled fatty acids were hydrolyzed by Candida rugosa lipase, and more selectivity is observed with Porcine Pancreas lipase type II. No activity was observed for lipase AK Amano 20, Candida antartica lipase B, and Mucor miehei lipase.
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.title.enShifting-Nitroxides to Investigate Enzymatic Hydrolysis of Fatty Acids by Lipases Using Electron Paramagnetic Resonance in Turbid Media
dc.typeArticle de revue
dc.identifier.doi10.1021/acs.analchem.9b00561
dc.subject.halSciences du Vivant [q-bio]
bordeaux.journalAnalytical Chemistry
bordeaux.page5504-5507
bordeaux.volume91
bordeaux.hal.laboratoriesCentre de Résonance Magnétique des Systèmes Biologiques (CRMSB) - UMR 5536*
bordeaux.issue9
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionCNRS
bordeaux.peerReviewedoui
hal.identifierhal-02472334
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02472334v1
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