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Volumn 3, Issue 3, 2012, Pages

Bifidobacterial enzymes involved in the metabolism of human milk oligosaccharides

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BETA 1,3 GALACTOSYL N ACETYLHEXOSAMINE PHOSPHORYLASE; BETA-1,3-GALACTOSYL-N-ACETYLHEXOSAMINE PHOSPHORYLASE; DRUG DERIVATIVE; GALACTO N BIOSE LACTO N BIOSE I PHOSPHORYLASE, BIFIDOBACTERIUM LONGUM; GALACTO-N-BIOSE-LACTO-N-BIOSE I PHOSPHORYLASE, BIFIDOBACTERIUM LONGUM; GALACTOSYL 1,3 N ACETYLGLUCOSAMINE; GALACTOSYL-1,3-N-ACETYLGLUCOSAMINE; GALACTOSYLTRANSFERASE; HEXOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE; PHOSPHORYLASE;

EID: 84866789452     PISSN: 21618313     EISSN: 21565376     Source Type: Journal    
DOI: 10.3945/an.111.001420     Document Type: Article
Times cited : (88)

References (72)
  • 1
    • 0003358703 scopus 로고
    • Ecology of bifidobacteria
    • Bezkorovainy A, Miller-Catchpole R, editors. Cleveland:CRC Press
    • Bezkorovainy A. Ecology of bifidobacteria. In:Bezkorovainy A, Miller-Catchpole R, editors. Biochemistry and physiology of bifidobacteria. Cleveland:CRC Press; 1989. p. 29-72.
    • (1989) Biochemistry and physiology of bifidobacteria , pp. 29-72
    • Bezkorovainy, A.1
  • 3
    • 20444399968 scopus 로고
    • Enzymatic inactivation of bifidus factor and blood group substances
    • Gyorgy P, Rose CS, Springer GF. Enzymatic inactivation of bifidus factor and blood group substances. J Lab Clin Med. 1954;43:543-52.
    • (1954) J Lab Clin Med. , vol.43 , pp. 543-552
    • Gyorgy, P.1    Rose, C.S.2    Springer, G.F.3
  • 4
    • 0014444718 scopus 로고
    • Uptake and metabolism of determinatives of 2-deoxy-2-amino-D-glucose in Bifidobacterium bifidum var
    • Veerkamp JH. Uptake and metabolism of determinatives of 2-deoxy-2-amino-D-glucose in Bifidobacterium bifidum var. pennsylvanicus. Arch Biochem Biophys. 1969;129:248-56.
    • (1969) pennsylvanicus. Arch Biochem Biophys. , vol.129 , pp. 248-256
    • Veerkamp, J.H.1
  • 5
    • 0001690120 scopus 로고
    • Carbohydrate in milks:analysis, quantities, and significance
    • Jensen RG, editor. San Diego:Academic Press
    • Newburg DS, Neubauer SH. Carbohydrate in milks:analysis, quantities, and significance. In:Jensen RG, editor. Handbook of Milk Composition. San Diego:Academic Press; 1995. p. 273-349.
    • (1995) Handbook of Milk Composition , pp. 273-349
    • Newburg, D.S.1    Neubauer, S.H.2
  • 6
    • 0033826695 scopus 로고    scopus 로고
    • Oligosaccharides in human milk:structural, functional, and metabolic aspects
    • McCormick DB, Bier DM, Cousins RJ, editors. Palo Alto: Annual Reviews
    • Kunz C, Rudloff S, Baier W, Klein N, Strobel S. Oligosaccharides in human milk:structural, functional, and metabolic aspects. In:McCormick DB, Bier DM, Cousins RJ, editors. Annual Review of Nutrition. Palo Alto: Annual Reviews; 2000. p. 699-722.
    • (2000) Annual Review of Nutrition , pp. 699-722
    • Kunz, C.1    Rudloff, S.2    Baier, W.3    Klein, N.4    Strobel, S.5
  • 7
    • 33746756673 scopus 로고    scopus 로고
    • Present status and future prospects of functional oligosaccharide development in Japan
    • Nakakuki T. Present status and future prospects of functional oligosaccharide development in Japan. Trends Glycosci Glycotechnol. 2005;52: 267-71.
    • (2005) Trends Glycosci Glycotechnol. , vol.52 , pp. 267-271
    • Nakakuki, T.1
  • 8
    • 0021228694 scopus 로고
    • The intestinal microflora of infants: composition of fecal flora in breast-fed and bottle-fed infants
    • Benno Y, Sawada K, Mitsuoka T. The intestinal microflora of infants: composition of fecal flora in breast-fed and bottle-fed infants. Microbiol Immunol. 1984;28:975-86.
    • (1984) Microbiol Immunol. , vol.28 , pp. 975-986
    • Benno, Y.1    Sawada, K.2    Mitsuoka, T.3
  • 9
    • 77957868691 scopus 로고    scopus 로고
    • Structures and application of oligosaccharides in human milk
    • Kobata A. Structures and application of oligosaccharides in human milk. Proc Jpn Acad, Ser B, Phys Biol Sci. 2010;86:731-47.
    • (2010) Proc Jpn Acad, Ser B, Phys Biol Sci. , vol.86 , pp. 731-747
    • Kobata, A.1
  • 13
    • 70349245210 scopus 로고    scopus 로고
    • Expression of four betagalactosidases from Bifidobacterium bifidum NCIMB41171 and their contribution on the hydrolysis and synthesis of galactooligosaccharides
    • Goulas T, Goulas A, Tzortzis G, Gibson GR. Expression of four betagalactosidases from Bifidobacterium bifidum NCIMB41171 and their contribution on the hydrolysis and synthesis of galactooligosaccharides. Appl Microbiol Biotechnol. 2009;84:899-907.
    • (2009) Appl Microbiol Biotechnol. , vol.84 , pp. 899-907
    • Goulas, T.1    Goulas, A.2    Tzortzis, G.3    Gibson, G.R.4
  • 14
    • 63949087761 scopus 로고    scopus 로고
    • Comparative analysis of four β-galactosidases from Bifidobacterium bifidum NCIMB41171:purification and biochemical characterisation
    • Goulas T, Goulas A, Tzortzis G, Gibson GR. Comparative analysis of four β-galactosidases from Bifidobacterium bifidum NCIMB41171:purification and biochemical characterisation. Appl Microbiol Biotechnol. 2009;82:1079-88.
    • (2009) Appl Microbiol Biotechnol. , vol.82 , pp. 1079-1088
    • Goulas, T.1    Goulas, A.2    Tzortzis, G.3    Gibson, G.R.4
  • 15
    • 34648824669 scopus 로고    scopus 로고
    • Molecular cloning and comparative analysis of four β-galactosidase genes from Bifidobacterium bifidum NCIMB41171
    • Goulas TK, Goulas AK, Tzortzis G, Gibson GR. Molecular cloning and comparative analysis of four β-galactosidase genes from Bifidobacterium bifidum NCIMB41171. Appl Microbiol Biotechnol. 2007;76: 1365-72.
    • (2007) Appl Microbiol Biotechnol. , vol.76 , pp. 1365-1372
    • Goulas, T.K.1    Goulas, A.K.2    Tzortzis, G.3    Gibson, G.R.4
  • 18
    • 36649024574 scopus 로고    scopus 로고
    • In vitro fermentability of human milk oligosaccharides by several strains of bifidobacteria
    • Ward RE, Ninonuevo M, Mills DA, Lebrilla CB, German JB. In vitro fermentability of human milk oligosaccharides by several strains of bifidobacteria. Mol Nutr Food Res. 2007;51:1398-405.
    • (2007) Mol Nutr Food Res. , vol.51 , pp. 1398-1405
    • Ward, R.E.1    Ninonuevo, M.2    Mills, D.A.3    Lebrilla, C.B.4    German, J.B.5
  • 19
    • 0033040820 scopus 로고    scopus 로고
    • β-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082:characterization, partial purification and relation to mucin degradation
    • Derensy-Dron D, Krzewinski F, Brassart C, Bouquelet S. β-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082:characterization, partial purification and relation to mucin degradation. Biotechnol Appl Biochem. 1999;29:3-10.
    • (1999) Biotechnol Appl Biochem. , vol.29 , pp. 3-10
    • Derensy-Dron, D.1    Krzewinski, F.2    Brassart, C.3    Bouquelet, S.4
  • 20
    • 35448959649 scopus 로고    scopus 로고
    • Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum
    • Nishimoto M, Kitaoka M. Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum. Appl Environ Microbiol. 2007; 73:6444-9.
    • (2007) Appl Environ Microbiol. , vol.73 , pp. 6444-6449
    • Nishimoto, M.1    Kitaoka, M.2
  • 21
    • 78650650902 scopus 로고    scopus 로고
    • Unique sugar metabolic pathways of bifidobacteria
    • Fushinobu S. Unique sugar metabolic pathways of bifidobacteria. Biosci Biotechnol Biochem. 2010;74:2374-84.
    • (2010) Biosci Biotechnol Biochem. , vol.74 , pp. 2374-2384
    • Fushinobu, S.1
  • 22
    • 45149087204 scopus 로고    scopus 로고
    • Structural and thermodynamic analyses of solute-binding Protein from Bifidobacterium longum specific for core 1 disaccharide and lacto-Nbiose I
    • Suzuki R, Wada J, Katayama T, Fushinobu S, Wakagi T, Shoun H, Sugimoto H, Tanaka A, Kumagai H, Ashida H, et al. Structural and thermodynamic analyses of solute-binding Protein from Bifidobacterium longum specific for core 1 disaccharide and lacto-Nbiose I. J Biol Chem. 2008;283:13165-73.
    • (2008) J Biol Chem. , vol.283 , pp. 13165-13173
    • Suzuki, R.1    Wada, J.2    Katayama, T.3    Fushinobu, S.4    Wakagi, T.5    Shoun, H.6    Sugimoto, H.7    Tanaka, A.8    Kumagai, H.9    Ashida, H.10
  • 24
    • 39149117699 scopus 로고    scopus 로고
    • Identification of galacto-N-biose phosphorylase from Clostridium perfringens ATCC13124
    • Nakajima M, Nihira T, Nishimoto M, Kitaoka M. Identification of galacto-N-biose phosphorylase from Clostridium perfringens ATCC13124. Appl Microbiol Biotechnol. 2008;78:465-71.
    • (2008) Appl Microbiol Biotechnol. , vol.78 , pp. 465-471
    • Nakajima, M.1    Nihira, T.2    Nishimoto, M.3    Kitaoka, M.4
  • 25
    • 67349154409 scopus 로고    scopus 로고
    • Characterization of β-1, 3-galactosyl-N-acetylhexosamine phosphorylase from Propionibacterium acnes
    • Nakajima M, Nishimoto M, Kitaoka M. Characterization of β-1, 3-galactosyl-N-acetylhexosamine phosphorylase from Propionibacterium acnes. Appl Microbiol Biotechnol. 2009;83:109-15.
    • (2009) Appl Microbiol Biotechnol. , vol.83 , pp. 109-115
    • Nakajima, M.1    Nishimoto, M.2    Kitaoka, M.3
  • 26
    • 79957554773 scopus 로고    scopus 로고
    • Characterization of β-galactoside phosphorylases with diverging acceptor specificities
    • Chao C, Wim S, Tom D. Characterization of β-galactoside phosphorylases with diverging acceptor specificities. Enzyme Microb Technol. 2011;49:59-65.
    • (2011) Enzyme Microb Technol. , vol.49 , pp. 59-65
    • Chao, C.1    Wim, S.2    Tom, D.3
  • 27
    • 54949156444 scopus 로고    scopus 로고
    • Identification of lacto-N-Biose I phosphorylase from Vibrio vulnificus CMCP6
    • Nakajima M, Kitaoka M. Identification of lacto-N-Biose I phosphorylase from Vibrio vulnificus CMCP6. Appl Environ Microbiol. 2008;74: 6333-7.
    • (2008) Appl Environ Microbiol. , vol.74 , pp. 6333-6337
    • Nakajima, M.1    Kitaoka, M.2
  • 28
    • 20444393045 scopus 로고    scopus 로고
    • Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum
    • Kitaoka M, Tian J, Nishimoto M. Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum. Appl Environ Microbiol. 2005;71:3158-62.
    • (2005) Appl Environ Microbiol. , vol.71 , pp. 3158-3162
    • Kitaoka, M.1    Tian, J.2    Nishimoto, M.3
  • 29
    • 67749097994 scopus 로고    scopus 로고
    • Characterization of three β-galactoside phosphorylases from Clostridium phytofermentans:discovery of D-galactosyl-beta1→4-L-rhamnose phosphorylase
    • Nakajima M, Nishimoto M, Kitaoka M. Characterization of three β-galactoside phosphorylases from Clostridium phytofermentans:discovery of D-galactosyl-beta1→4-L-rhamnose phosphorylase. J Biol Chem. 2009;284:19220-7.
    • (2009) J Biol Chem. , vol.284 , pp. 19220-19227
    • Nakajima, M.1    Nishimoto, M.2    Kitaoka, M.3
  • 30
    • 34347335742 scopus 로고    scopus 로고
    • Identification of the putative proton donor residue of lacto-N-biose phosphorylase (EC 2.4.1.211)
    • Nishimoto M, Kitaoka M. Identification of the putative proton donor residue of lacto-N-biose phosphorylase (EC 2.4.1.211). Biosci Biotechnol Biochem. 2007;71:1587-91.
    • (2007) Biosci Biotechnol Biochem. , vol.71 , pp. 1587-1591
    • Nishimoto, M.1    Kitaoka, M.2
  • 33
    • 65449168413 scopus 로고    scopus 로고
    • The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold
    • Hidaka M, Nishimoto M, Kitaoka M,Wakagi T, Shoun H, Fushinobu S. The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold. J Biol Chem. 2009;284: 7273-83.
    • (2009) J Biol Chem. , vol.284 , pp. 7273-7283
    • Hidaka, M.1    Nishimoto, M.2    Kitaoka, M.3    Wakagi, T.4    Shoun, H.5    Fushinobu, S.6
  • 34
    • 74149092036 scopus 로고    scopus 로고
    • Characterization of D-galactosylβ1→ 4-L-rhamnose phosphorylase from Opitutus terrae
    • Nakajima M, Nishimoto M, Kitaoka M. Characterization of D-galactosylβ1→ 4-L-rhamnose phosphorylase from Opitutus terrae. Enzyme Microb Technol. 2010;46:315-9.
    • (2010) Enzyme Microb Technol. , vol.46 , pp. 315-319
    • Nakajima, M.1    Nishimoto, M.2    Kitaoka, M.3
  • 35
    • 0036968554 scopus 로고    scopus 로고
    • Trimeric crystal structure of the glycoside hydrolase family 42 β-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose
    • Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, Wakagi T. Trimeric crystal structure of the glycoside hydrolase family 42 β-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose. J Mol Biol. 2002;322:79-91.
    • (2002) J Mol Biol. , vol.322 , pp. 79-91
    • Hidaka, M.1    Fushinobu, S.2    Ohtsu, N.3    Motoshima, H.4    Matsuzawa, H.5    Shoun, H.6    Wakagi, T.7
  • 36
    • 80054960221 scopus 로고    scopus 로고
    • Identification of amino acid residues determining substrate preference of 1, 3-b-galactosyl-N-acetylhexosamine phosphorylase
    • Nishimoto M, Hidaka M, Nakajima M, Fushinobu S, Kitaoka M. Identification of amino acid residues determining substrate preference of 1, 3-b-galactosyl-N-acetylhexosamine phosphorylase. J Mol Catal, B Enzym. 2012;74:97-102.
    • (2012) J Mol Catal, B Enzym. , vol.74 , pp. 97-102
    • Nishimoto, M.1    Hidaka, M.2    Nakajima, M.3    Fushinobu, S.4    Kitaoka, M.5
  • 38
    • 67449104612 scopus 로고    scopus 로고
    • A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues: substrate specificity investigations of N-acetylhexosamine 1-kinase
    • Cai L, Guan W, Kitaoka M, Shen J, Xia C, Chen W, Wang PG. A chemoenzymatic route to N-acetylglucosamine-1-phosphate analogues: substrate specificity investigations of N-acetylhexosamine 1-kinase. Chem Commun (Camb). 2009;2944-6.
    • (2009) Chem Commun (Camb) , pp. 2944-2946
    • Cai, L.1    Guan, W.2    Kitaoka, M.3    Shen, J.4    Xia, C.5    Chen, W.6    Wang, P.G.7
  • 40
    • 0242498430 scopus 로고    scopus 로고
    • Structure and function of enzymes of the Leloir pathway for galactose metabolism
    • Holden HM, Rayment I, Thoden JB. Structure and function of enzymes of the Leloir pathway for galactose metabolism. J Biol Chem. 2003;278: 43885-8.
    • (2003) J Biol Chem. , vol.278 , pp. 43885-43888
    • Holden, H.M.1    Rayment, I.2    Thoden, J.B.3
  • 41
    • 76149098836 scopus 로고    scopus 로고
    • Distribution of in vitro fermentation ability of lacto-Nbiose I, a major building block of human milk oligosaccharides, in bifidobacterial strains
    • Xiao JZ, Takahashi S, Nishimoto M, Odamaki T, Yaeshima T, Iwatsuki K, Kitaoka M. Distribution of in vitro fermentation ability of lacto-Nbiose I, a major building block of human milk oligosaccharides, in bifidobacterial strains. Appl Environ Microbiol. 2010;76:54-9.
    • (2010) Appl Environ Microbiol. , vol.76 , pp. 54-59
    • Xiao, J.Z.1    Takahashi, S.2    Nishimoto, M.3    Odamaki, T.4    Yaeshima, T.5    Iwatsuki, K.6    Kitaoka, M.7
  • 42
    • 27844482528 scopus 로고    scopus 로고
    • Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum
    • Fujita K, Oura F, Nagamine N, Katayama T, Hiratake J, Sakata K, Kumagai H, Yamamoto K. Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J Biol Chem. 2005;280:37415-22.
    • (2005) J Biol Chem. , vol.280 , pp. 37415-37422
    • Fujita, K.1    Oura, F.2    Nagamine, N.3    Katayama, T.4    Hiratake, J.5    Sakata, K.6    Kumagai, H.7    Yamamoto, K.8
  • 43
    • 70350455882 scopus 로고    scopus 로고
    • Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum
    • Suzuki R, Katayama T, Kitaoka M, Kumagai H, Wakagi T, Shoun H, Ashida H, Yamamoto K, Fushinobu S. Crystallographic and mutational analyses of substrate recognition of endo-α-N-acetylgalactosaminidase from Bifidobacterium longum. J Biochem. 2009;146:389-98.
    • (2009) J Biochem. , vol.146 , pp. 389-398
    • Suzuki, R.1    Katayama, T.2    Kitaoka, M.3    Kumagai, H.4    Wakagi, T.5    Shoun, H.6    Ashida, H.7    Yamamoto, K.8    Fushinobu, S.9
  • 44
    • 3242780110 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Bifidobacterium bifidum 1,2-α-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside hydrolase family 95)
    • Katayama T, Sakuma A, Kimura T, Makimura Y, Hiratake J, Sakata K, Yamanoi T, Kumagai H, Yamamoto K. Molecular cloning and characterization of Bifidobacterium bifidum 1,2-α-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside hydrolase family 95). J Bacteriol. 2004;186:4885-93.
    • (2004) J Bacteriol. , vol.186 , pp. 4885-4893
    • Katayama, T.1    Sakuma, A.2    Kimura, T.3    Makimura, Y.4    Hiratake, J.5    Sakata, K.6    Yamanoi, T.7    Kumagai, H.8    Yamamoto, K.9
  • 45
    • 34547137182 scopus 로고    scopus 로고
    • Structural basis of the catalytic reaction mechanism of novel 1,2-α-Lfucosidase from Bifidobacterium bifidum
    • Nagae M, Tsuchiya A, Katayama T, Yamamoto K, Wakatsuki S, Kato R. Structural basis of the catalytic reaction mechanism of novel 1,2-α-Lfucosidase from Bifidobacterium bifidum. J Biol Chem. 2007;282: 18497-509.
    • (2007) J Biol Chem. , vol.282 , pp. 18497-18509
    • Nagae, M.1    Tsuchiya, A.2    Katayama, T.3    Yamamoto, K.4    Wakatsuki, S.5    Kato, R.6
  • 47
    • 68749094075 scopus 로고    scopus 로고
    • Two distinct α-L-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates
    • Ashida H, Miyake A, Kiyohara M, Wada J, Yoshida E, Kumagai H, Katayama T, Yamamoto K. Two distinct α-L-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates. Glycobiology. 2009;19:1010-7.
    • (2009) Glycobiology. , vol.19 , pp. 1010-1017
    • Ashida, H.1    Miyake, A.2    Kiyohara, M.3    Wada, J.4    Yoshida, E.5    Kumagai, H.6    Katayama, T.7    Yamamoto, K.8
  • 48
    • 79952552818 scopus 로고    scopus 로고
    • An exo-α-sialidase from bifidobacteria involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates
    • Kiyohara M, Tanigawa K, Chaiwangsri T, Katayama T, Ashida H, Yamamoto K. An exo-α-sialidase from bifidobacteria involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates. Glycobiology. 2011;21:437-47.
    • (2011) Glycobiology. , vol.21 , pp. 437-447
    • Kiyohara, M.1    Tanigawa, K.2    Chaiwangsri, T.3    Katayama, T.4    Ashida, H.5    Yamamoto, K.6
  • 49
    • 21044451636 scopus 로고    scopus 로고
    • Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins
    • Katayama T, Fujita K, Yamamoto K. Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins. J Biosci Bioeng. 2005; 99:457-65.
    • (2005) J Biosci Bioeng. , vol.99 , pp. 457-465
    • Katayama, T.1    Fujita, K.2    Yamamoto, K.3
  • 51
    • 0027164497 scopus 로고
    • Purification and characterization of an enzyme releasing lacto-N-biose fromoligosaccharides with type 1 chain
    • Sano M, Hayakawa K, Kato I. Purification and characterization of an enzyme releasing lacto-N-biose fromoligosaccharides with type 1 chain. J Biol Chem. 1993;268:18560-6.
    • (1993) J Biol Chem. , vol.268 , pp. 18560-18566
    • Sano, M.1    Hayakawa, K.2    Kato, I.3
  • 52
    • 0026657767 scopus 로고
    • An enzyme releasing lacto-N-biose from oligosaccharides
    • Sano M, Hayakawa K, Kato I. An enzyme releasing lacto-N-biose from oligosaccharides. Proc Natl Acad Sci U S A. 1992;89:8512-6.
    • (1992) Proc Natl Acad Sci U S A. , vol.89 , pp. 8512-8516
    • Sano, M.1    Hayakawa, K.2    Kato, I.3
  • 53
    • 77957825024 scopus 로고    scopus 로고
    • Cooperation of β-galactosidase and β-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure
    • Miwa M, Horimoto T, Kiyohara M, Katayama T, Kitaoka M, Ashida H, Yamamoto K. Cooperation of β-galactosidase and β-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure. Glycobiology. 2010;20:1402-9.
    • (2010) Glycobiology. , vol.20 , pp. 1402-1409
    • Miwa, M.1    Horimoto, T.2    Kiyohara, M.3    Katayama, T.4    Kitaoka, M.5    Ashida, H.6    Yamamoto, K.7
  • 61
    • 35548975958 scopus 로고    scopus 로고
    • Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk
    • Nishimoto M, Kitaoka M. Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk. Biosci Biotechnol Biochem. 2007;71:2101-4.
    • (2007) Biosci Biotechnol Biochem. , vol.71 , pp. 2101-2104
    • Nishimoto, M.1    Kitaoka, M.2
  • 62
    • 71549147182 scopus 로고    scopus 로고
    • One-pot enzymatic production of β-Dgalactopyranosyl-( 1→3)-2-acetamido-2-deoxy-D-galactose (galacto-N-biose) from sucrose and 2-acetamido-2-deoxy-D-galactose (N-acetylgalactosamine)
    • Nishimoto M, Kitaoka M. One-pot enzymatic production of β-Dgalactopyranosyl-( 1→3)-2-acetamido-2-deoxy-D-galactose (galacto-N-biose) from sucrose and 2-acetamido-2-deoxy-D-galactose (N-acetylgalactosamine). Carbohydr Res. 2009;344:2573-6.
    • (2009) Carbohydr Res. , vol.344 , pp. 2573-2576
    • Nishimoto, M.1    Kitaoka, M.2
  • 63
    • 80053940417 scopus 로고    scopus 로고
    • One-pot enzymatic production of 2-acetamido-2-deoxy-D-galactose (GalNAc) from 2-acetamido-2-deoxy-D-glucose (GlcNAc)
    • Inoue K, Nishimoto M, Kitaoka M. One-pot enzymatic production of 2-acetamido-2-deoxy-D-galactose (GalNAc) from 2-acetamido-2-deoxy-D-glucose (GlcNAc). Carbohydr Res. 2011;346:2432-6.
    • (2011) Carbohydr Res. , vol.346 , pp. 2432-2436
    • Inoue, K.1    Nishimoto, M.2    Kitaoka, M.3
  • 69
    • 78649698242 scopus 로고    scopus 로고
    • Broad Conservation of Milk Utilization Genes in Bifidobacterium longum subsp infantis as revealed by comparative genomic hybridization
    • LoCascio RG, Desai P, Sela DA, Weimer B, Mills DA. Broad Conservation of Milk Utilization Genes in Bifidobacterium longum subsp infantis as revealed by comparative genomic hybridization. Appl Environ Microbiol. 2010;76:7373-81.
    • (2010) Appl Environ Microbiol. , vol.76 , pp. 7373-7381
    • LoCascio, R.G.1    Desai, P.2    Sela, D.A.3    Weimer, B.4    Mills, D.A.5
  • 71
    • 0032878580 scopus 로고    scopus 로고
    • Distribution of bifidobacterial species in human intestinal microflora examined with 16S rRNA-gene-targeted species-specific primers
    • Matsuki T, Watanabe K, Tanaka R, Fukuda M, Oyaizu H. Distribution of bifidobacterial species in human intestinal microflora examined with 16S rRNA-gene-targeted species-specific primers. Appl Environ Microbiol. 1999;65:4506-12.
    • (1999) Appl Environ Microbiol. , vol.65 , pp. 4506-4512
    • Matsuki, T.1    Watanabe, K.2    Tanaka, R.3    Fukuda, M.4    Oyaizu, H.5
  • 72
    • 77954142215 scopus 로고    scopus 로고
    • Nursing our microbiota:molecular linkages between bifidobacteria and milk oligosaccharides
    • Sela DA, Mills DA. Nursing our microbiota:molecular linkages between bifidobacteria and milk oligosaccharides. Trends Microbiol. 2010;18: 298-307.
    • (2010) Trends Microbiol. , vol.18 , pp. 298-307
    • Sela, D.A.1    Mills, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.