Novel Putative Galactose Operon Involving Lacto-<i>N</i>-Biose Phosphorylase in<i>Bifidobacterium longum</i>

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  • Motomitsu Kitaoka
    National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan
  • Jiesheng Tian
    National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan
  • Mamoru Nishimoto
    National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan

抄録

<jats:title>ABSTRACT</jats:title><jats:p>A lacto-<jats:italic>N</jats:italic>-biose phosphorylase (LNBP) was purified from the cell extract of<jats:italic>Bifidobacterium bifidum</jats:italic>. Its N-terminal and internal amino acid sequences were homologous with those of the hypothetical protein of<jats:italic>Bifidobacterium longum</jats:italic>NCC2705 encoded by the BL1641 gene. The homologous gene of the type strain<jats:italic>B. longum</jats:italic>JCM1217,<jats:italic>lnpA</jats:italic>, was expressed in<jats:italic>Escherichia coli</jats:italic>to confirm that it encoded LNBP. No significant identity was found with any proteins with known function, indicating that LNBP should be classified in a new family. The<jats:italic>lnpA</jats:italic>gene is located in a novel putative operon for galactose metabolism that does not contain a galactokinase gene. The operon seems to be involved in intestinal colonization by bifidobacteria mediated by metabolism of mucin sugars. In addition, it may also resolve the question of the nature of the bifidus factor in human milk as the lacto-<jats:italic>N</jats:italic>-biose structure found in milk oligosaccharides.</jats:p>

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