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Applied and Environmental Microbiology, June 2005, p. 3158-3162, Vol. 71, No. 6
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.6.3158-3162.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Novel Putative Galactose Operon Involving Lacto-N-Biose Phosphorylase in Bifidobacterium longum

Motomitsu Kitaoka,* Jiesheng Tian, and Mamoru Nishimoto

National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan

Received 28 October 2004/ Accepted 18 December 2004

A lacto-N-biose phosphorylase (LNBP) was purified from the cell extract of Bifidobacterium bifidum. Its N-terminal and internal amino acid sequences were homologous with those of the hypothetical protein of Bifidobacterium longum NCC2705 encoded by the BL1641 gene. The homologous gene of the type strain B. longum JCM1217, lnpA, was expressed in Escherichia coli 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 lnpA 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-N-biose structure found in milk oligosaccharides.

* Corresponding author. Mailing address: National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. Phone: 81-298-38-8071. Fax: 81-298-38-7321. E-mail: mkitaoka{at}nfri.affrc.go.jp.

Applied and Environmental Microbiology, June 2005, p. 3158-3162, Vol. 71, No. 6
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.6.3158-3162.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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