Abstract
The 67 kDa myosin-cross-reactive antigen (MCRA) is a member of the MCRA family of proteins present in a wide range of bacteria and was predicted to have fatty acid isomerase function. We have now characterised the catalytic activity of MCRAs from four LAB stains, including Lactobacillus rhamnosus LGG, L. plantarum ST-III, L. acidophilus NCFM and Bifidobacterium animalis subsp. lactis BB-12. MCRA genes from these strains were cloned and expressed in Escherichia coli, and the recombinant protein function was analysed with lipid profiles by GC–MS. The four MCRAs catalysed the conversion of linoleic acid and oleic acid to their respective 10-hydroxy derivatives, which suggests that MCRA proteins catalyse the first step in conjugated linoleic acid production. This is the first report of MCRA from L. rhamnosus with such catalytic function.
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Acknowledgments
This study was supported by the National Science Fund for Distinguished Young Scholars (31125021), the National High Technology Research and Development Program of China (2011AA100905), the National Natural Science Foundation of China (No. 31171636, 81071685 and 20836003), the National Basic Research Program of China 973 Program (2012CB720802), the 111 project B07029, Fundamental Research Funds for the Central Universities (JUSRP 11017, JUSRP31103), and SKLF-TS-201101.
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Yang, B., Chen, H., Song, Y. et al. Myosin-cross-reactive antigens from four different lactic acid bacteria are fatty acid hydratases. Biotechnol Lett 35, 75–81 (2013). https://doi.org/10.1007/s10529-012-1044-y
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DOI: https://doi.org/10.1007/s10529-012-1044-y