Characterization of the Cytosolic β-<i>N</i>-Acetylglucosaminidase from <i>Bifidobacterium longum</i> subsp. <i>longum</i>

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  • Honda Yuji
    National Food Research Institute, National Agriculture and Food Research Organization Department of Food Science, Ishikawa Prefectural University
  • Nishimoto Mamoru
    National Food Research Institute, National Agriculture and Food Research Organization
  • Katayama Takane
    Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University
  • Kitaoka Motomitsu
    National Food Research Institute, National Agriculture and Food Research Organization

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  • Characterization of the Cytosolic β-N-Acetylglucosaminidase from Bifidobacterium longum subsp. longum

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Abstract

The BLLJ_1391 protein from Bifidobacterium longum subsp. longum JCM1217, a cytosolic β-N-acetylglucosaminidase belonging to glycoside hydrolase family (GH) 20, hydrolyzed lacto-N-triose II (LNTri) as well as chitin oligosaccharides. Its reaction was found to follow a substrate-assisted mechanism with anomeric retention, which is common for GH 20 enzymes. Homologous enzymes are found in genomic sequences of B. longum subsp. infantis, Bifidobacterium bifidum, and Bifidobacteium breve, all of which are infant gut-associated species of Bifidobacterium. The distribution resembles that of 1,3-β-galactosyl-N-acetylhexosamine phosphorylase, suggesting that the enzyme plays a role in metabolism of human milk oligosaccharides by hydrolyzing LNTri generated via the cytosolic hydrolysis of lacto-N-tetraose (LNT) by LNT 1,3-β-galactosidase.

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