Myosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protection

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dc.contributor.authorRosberg-Cody, Eva
dc.contributor.authorLiavonchanka, Alena
dc.contributor.authorGöbel, Cornelia
dc.contributor.authorRoss, R. Paul
dc.contributor.authorO'Sullivan, Orla
dc.contributor.authorFitzgerald, Gerald F.
dc.contributor.authorFeussner, Ivo
dc.contributor.authorStanton, Catherine
dc.contributor.funderScience Foundation Irelanden
dc.contributor.funderIrish Governmenten
dc.contributor.funderEuropean Commissionen
dc.contributor.funderCarl von Ossietzky Universität Oldenburg, Germanyde
dc.date.accessioned2012-12-12T12:05:57Z
dc.date.available2012-12-12T12:05:57Z
dc.date.copyright2011
dc.date.issued2011-02-17
dc.description.abstractBackground: The aim of this study was to determine the catalytic activity and physiological role of myosin-crossreactive antigen (MCRA) from Bifidobacterium breve NCIMB 702258. MCRA from B. breve NCIMB 702258 was cloned, sequenced and expressed in heterologous hosts (Lactococcus and Corynebacterium) and the recombinant proteins assessed for enzymatic activity against fatty acid substrates. Results: MCRA catalysed the conversion of palmitoleic, oleic and linoleic acids to the corresponding 10-hydroxy fatty acids, but shorter chain fatty acids were not used as substrates, while the presence of trans-double bonds and double bonds beyond the position C12 abolished hydratase activity. The hydroxy fatty acids produced were not metabolised further. We also found that heterologous Lactococcus and Corynebacterium expressing MCRA accumulated increasing amounts of 10-HOA and 10-HOE in the culture medium. Furthermore, the heterologous cultures exhibited less sensitivity to heat and solvent stresses compared to corresponding controls. Conclusions: MCRA protein in B. breve can be classified as a FAD-containing double bond hydratase, within the carbon-oxygen lyase family, which may be catalysing the first step in conjugated linoleic acid (CLA) production, and this protein has an additional function in bacterial stress protection.en
dc.description.sponsorshipScience Foundation Ireland (SFI-CSET); Science Foundation Ireland (02/CE/B 124); Science Foundation Ireland (07/CE/B1368); Irish Government (National Development Plan); European Commission (QLK1-2002-02362); Carl von Ossietzky Universität Oldenburg, Germany (Georg-Christoph-Lichtenberg Scholarship for PhD Program 'Molecular Biology')en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationRosberg-Cody, E., Liavonchanka, A., Göbel, C., Ross, R.P., O'Sullivan, O., Fitzgerald, G.F., Feussner, I., Stanton, C., 2011. Myosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protection. BMC Biochemistry 12(9). doi: 10.1186/1471-2091-12-9en
dc.identifier.doi10.1186/1471-2091-12-9
dc.identifier.issn1471-2091
dc.identifier.journaltitleBMC Biochemistryen
dc.identifier.startpage9en
dc.identifier.urihttps://hdl.handle.net/10468/851
dc.identifier.volume12en
dc.language.isoenen
dc.publisherBioMed Centralen
dc.relation.urihttp://www.biomedcentral.com/1471-2091/12/9
dc.rights© 2011 Rosberg-Cody et al; licensee BioMed Central Ltd.en
dc.rights.urihttp://www.biomedcentral.com/about/licenseen
dc.subjectMyosin-cross-reactive antigen (MCRA)en
dc.subjectBifidobacterium breveen
dc.subjectFatty acid hydrataseen
dc.subjectStress protectionen
dc.subjectLactococcusen
dc.subjectCorynebacteriumen
dc.titleMyosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protectionen
dc.typeArticle (peer-reviewed)en
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