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

Show simple item record

dc.contributor.author Rosberg-Cody, Eva
dc.contributor.author Liavonchanka, Alena
dc.contributor.author Göbel, Cornelia
dc.contributor.author Ross, R. Paul
dc.contributor.author O'Sullivan, Orla
dc.contributor.author Fitzgerald, Gerald F.
dc.contributor.author Feussner, Ivo
dc.contributor.author Stanton, Catherine
dc.date.accessioned 2012-12-12T12:05:57Z
dc.date.available 2012-12-12T12:05:57Z
dc.date.copyright 2011
dc.date.issued 2011-02-17
dc.identifier.citation Rosberg-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: 10.1186/1471-2091-12-9 en
dc.identifier.volume 12 en
dc.identifier.startpage 9 en
dc.identifier.issn 1471-2091
dc.identifier.uri http://hdl.handle.net/10468/851
dc.identifier.doi 10.1186/1471-2091-12-9
dc.description.abstract Background: 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.sponsorship Science 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.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher BioMed Central en
dc.relation.uri http://www.biomedcentral.com/1471-2091/12/9
dc.rights © 2011 Rosberg-Cody et al; licensee BioMed Central Ltd. en
dc.rights.uri http://www.biomedcentral.com/about/license en
dc.subject Myosin-cross-reactive antigen (MCRA) en
dc.subject Bifidobacterium breve en
dc.subject Fatty acid hydratase en
dc.subject Stress protection en
dc.subject Lactococcus en
dc.subject Corynebacterium en
dc.title Myosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protection en
dc.type Article (peer-reviewed) en
dc.internal.authorurl http://research.ucc.ie/profiles/D010/gfitzgerald en
dc.internal.authorcontactother Gerald F. Fitzgerald, Microbiology Department, University College Cork, Cork, Ireland. Email: g.fitzgerald@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.internal.rssid 90194391
dc.contributor.funder Science Foundation Ireland en
dc.contributor.funder Irish Government en
dc.contributor.funder European Commission en
dc.contributor.funder Carl von Ossietzky Universität Oldenburg, Germany de
dc.description.status Peer reviewed en
dc.identifier.journaltitle BMC Biochemistry en
dc.internal.copyrightchecked This is a Sherpa Romeo Green Journa. Policy: You are free: to Share — to copy, distribute and transmit the work to Remix — to adapt the work to make commercial use of the work Under the following conditions: Attribution — You must attribute the work in the manner specified by the author or licensor (but not in any way that suggests that they endorse you or your use of the work). With the understanding that: Waiver— Any of the above conditions can be waived if you get permission from the copyright holder. Public Domain— Where the work or any of its elements is in the public domain under applicable law, that status is in no way affected by the license. Other Rights— In no way are any of the following rights affected by the license: • Your fair dealing or fair use rights, or other applicable copyright exceptions and limitations; • The author's moral rights; • Rights other persons may have either in the work itself or in how the work is used, such as publicity or privacy rights. Notice— For any reuse or distribution, you must make clear to others the license terms of this work. The best way to do this is with a link to this web page. A new version of this license is available. You should use it for new works, and you may want to relicense existing works under it. No works are automatically put under the new license, however. en
dc.internal.IRISemailaddress g.fitzgerald@ucc.ie en


Files in this item

This item appears in the following Collection(s)

Show simple item record

This website uses cookies. By using this website, you consent to the use of cookies in accordance with the UCC Privacy and Cookies Statement. For more information about cookies and how you can disable them, visit our Privacy and Cookies statement