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

Hdl Handle:
http://hdl.handle.net/10147/126946
Title:
Myosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protection
Authors:
Rosberg-Cody, Eva; Liavonchanka, Alena; Gobel, Cornelia; Ross, R.Paul; O'Sullivan, Orla; Fitzgerald, Gerald F; Feussner, Ivo; Stanton, Catherine
Citation:
BMC Biochemistry. 2011 Feb 17;12(1):9
Issue Date:
17-Feb-2011
URI:
http://hdl.handle.net/10147/126946
Abstract:
Abstract Background The aim of this study was to determine the catalytic activity and physiological role of myosin-cross-reactive 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.
Item Type:
Journal Article

Full metadata record

DC FieldValue Language
dc.contributor.authorRosberg-Cody, Eva-
dc.contributor.authorLiavonchanka, Alena-
dc.contributor.authorGobel, 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.date.accessioned2011-04-04T09:21:24Z-
dc.date.available2011-04-04T09:21:24Z-
dc.date.issued2011-02-17-
dc.identifierhttp://dx.doi.org/10.1186/1471-2091-12-9-
dc.identifier.citationBMC Biochemistry. 2011 Feb 17;12(1):9-
dc.identifier.urihttp://hdl.handle.net/10147/126946-
dc.description.abstractAbstract Background The aim of this study was to determine the catalytic activity and physiological role of myosin-cross-reactive 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.-
dc.titleMyosin-cross-reactive antigen (MCRA) protein from Bifidobacterium breve is a FAD-dependent fatty acid hydratase which has a function in stress protection-
dc.typeJournal Article-
dc.language.rfc3066en-
dc.rights.holderRosberg-Cody et al.; licensee BioMed Central Ltd.-
dc.description.statusPeer Reviewed-
dc.date.updated2011-03-29T15:22:09Z-
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