Updated on 2024/12/15

写真a

 
FUJITA Kiyotaka
 
Organization
Research Field in Agriculture, Agriculture, Fisheries and Veterinary Medicine Area Faculty of Agriculture Department of Agriculture Associate Professor
Research Field in Agriculture, Agriculture, Fisheries and Veterinary Medicine Area United Graduate School of Agricultural Sciences
Title
Associate Professor
Homepage
http://hypba2.jimdo.com/
External link

Degree

  • 博士（農学） ( 2001.3   愛媛大学 )

Research Interests

  • β-アラビノオリゴ糖鎖

  • β-L-arabinofuranosidase

  • AGP

  • 食物繊維

  • 腸内細菌

  • 糖質科学

  • 糖質分解酵素

  • カラメル化糖

  • LAM

Research Areas

  • Others / Others  / 遺伝子工学

  • Others / Others  / 酵素工学

  • Life Science / Applied biochemistry  / 糖質科学

  • Life Science / Food sciences

Research History

  • Kagoshima University   Associate Professor

    2004.4

  • Kagoshima University

    2004.4

Professional Memberships

  • THE JAPANESE SOCIETY OF APPLIED GLYCOSCIENCE

  • JAPAN SOCIETY FOR BIOSCIENCE, BIOTECHNOLOGY, AND AGROCHEMISTRY

  • THE JAPANESE SOCIETY OF CARBOHYDRATE RESEARCH

  • The Society for Biotechnology, Japan

 

Papers

  • Yuki Sasaki, Ayako Matsuo, Mimika Hashiguchi, Kanoko Fujimura, Hiroyuki Koshino, Katsunori Tanaka, Yukishige Ito, Kanefumi Kitahara, Akihiro Ishiwata, Kiyotaka Fujita .  Structural analysis of gum arabic side chains from Acacia seyal released by bifidobacterial β-arabino-oligosaccharide 3-O-β-L-arabinopyranosyl-α-L-arabinofuranosidase .  Carbohydrate Polymers349   122965   2024.11Reviewed

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    Authorship：Last author,　Corresponding author   Language：Japanese   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

    DOI： 10.1016/j.carbpol.2024.122965

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  • Ting Ye, Ayako Horigome, Hiroki Kaneko, Toshitaka Odamaki, Kanefumi Kitahara, Kiyotaka Fujita .  Degradation mechanism of difructose dianhydride III in Blautia species .  Applied Microbiology and Biotechnology108 ( 1 ) 502   2024.11Reviewed

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    Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1007/s00253-024-13346-5

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  • Kiyotaka Fujita, Hanako Tsunomachi, Pan Lixia, Shun Maruyama, Masayuki Miyake, Aimi Dakeshita, Kanefumi Kitahara, Katsunori Tanaka, Yukishige Ito, Akihiro Ishiwata, Shinya Fushinobu .  Bifidobacterial GH146 β-L-arabinofuranosidase for the removal of β1,3-L-arabinofuranosides on plant glycans .  Applied Microbiology and Biotechnology108 ( 1 ) 199   2024.2Reviewed

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    Authorship：Lead author,　Corresponding author   Language：Japanese   Publishing type：Research paper (scientific journal)  

    DOI： 10.1007/s00253-024-13014-8

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  • Michiko Shimokawa, Akihiro Ishiwata, Toma Kashima, Chiho Nakashima, Jiaman Li, Riku Fukushima, Naomi Sawai, Miku Nakamori, Yuuki Tanaka, Azusa Kudo, Sae Morikami, Nao Iwanaga, Genki Akai, Nobutaka Shimizu, Takatoshi Arakawa, Chihaya Yamada, Kanefumi Kitahara, Katsunori Tanaka, Yukishige Ito, Shinya Fushinobu, Kiyotaka Fujita .  Identification and characterization of endo-α-, exo-α-, and exo-β-D-arabinofuranosidases degrading lipoarabinomannan and arabinogalactan of mycobacteria. .  Nature communications14 ( 1 ) 5803 - 5803   2023.9Reviewed International journal

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    The cell walls of pathogenic and acidophilic bacteria, such as Mycobacterium tuberculosis and Mycobacterium leprae, contain lipoarabinomannan and arabinogalactan. These components are composed of D-arabinose, the enantiomer of the typical L-arabinose found in plants. The unique glycan structures of mycobacteria contribute to their ability to evade mammalian immune responses. In this study, we identified four enzymes (two GH183 endo-D-arabinanases, GH172 exo-α-D-arabinofuranosidase, and GH116 exo-β-D-arabinofuranosidase) from Microbacterium arabinogalactanolyticum. These enzymes completely degraded the complex D-arabinan core structure of lipoarabinomannan and arabinogalactan in a concerted manner. Furthermore, through biochemical characterization using synthetic substrates and X-ray crystallography, we elucidated the mechanisms of substrate recognition and anomer-retaining hydrolysis for the α- and β-D-arabinofuranosidic bonds in both endo- and exo-mode reactions. The discovery of these D-arabinan-degrading enzymes, along with the understanding of their structural basis for substrate specificity, provides valuable resources for investigating the intricate glycan architecture of mycobacterial cell wall polysaccharides and their contribution to pathogenicity.

    DOI： 10.1038/s41467-023-41431-2

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  • Sasaki, Y., Yanagita, M., Hashiguchi, M., Horigome, A., Xiao, J-Z., Odamaki, T., Kitahara, K., and Fujita, K. .  Assimilation of arabinogalactan side chains with novel 3-O-β-L-arabinopyranosyl-α-L-arabinofuranosidase in Bifidobacterium pseudocatenulatum .  Microbiome Res. Rep.2 ( 3 ) 12 - 12   2023.4Reviewed

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    Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：OAE Publishing Inc.  

    Aim: Dietary plant fibers affect gut microbiota composition; however, the underlying microbial degradation pathways are not fully understood. We previously discovered 3-O-α-D-galactosyl-α-L-arabinofuranosidase (GAfase), a glycoside hydrolase family 39 enzyme involved in the assimilation of side chains of arabinogalactan protein (AGP), from Bifidobacterium longum subsp. longum JCM7052. Although GAfase homologs are not highly prevalent in the Bifidobacterium genus, several Bifidobacterium strains possess the homologs. To explore the differences in substrate specificity among the homologs, a homolog of B. longum GAfase in Bifidobacterium pseudocatenulatum MCC10289 (MCC10289_0425) was characterized. Methods: Gum arabic, larch, wheat AGP, and sugar beet arabinan were used to determine the substrate specificity of the MCC10289_0425 protein. An amino acid replacement was introduced into GAfase to identify a critical residue that governs the differentiation of substrate specificity. The growth of several Bifidobacterium strains on β-L-arabinopyranosyl disaccharide and larch AGP was examined. Results: MCC10289_0425 was identified to be an unprecedented 3-O-β-L-arabinopyranosyl-α-L-arabinofuranosidase (AAfase) with low GAfase activity. A single amino acid replacement (Asn119 to Tyr) at the catalytic site converted GAfase into AAfase. AAfase releases sugar source from AGP, thereby allowing B. pseudocatenulatum growth. Conclusion: Bifidobacteria have evolved several homologous enzymes with overlapping but distinct substrate specificities depending on the species. They have acquired different fitness abilities to respond to diverse plant polysaccharide structures.

    DOI： 10.20517/mrr.2023.08

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  • Akihiro Ishiwata, Hanako Tsunomachi, Kyohei Kameyama, Kaeothip Sophon, Masayuki Nakamura, Kanefumi Kitahara, Katsunori Tanaka, Yukishige Ito, Kiyotaka Fujita .  Bifidobacterial GH family 146 β‐L‐arabinofuranosidase (Bll4HypBA1) as the last enzyme for the complete removal of oligoarabinofuranosides from HRGP .  ChemBioChem24 ( 5 ) e202200637   2023.1Reviewed

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    Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

    DOI： 10.1002/cbic.202200637

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  • Toma Kashima, Kouki Okumura, Akihiro Ishiwata, Machika Kaieda, Tohru Terada, Takatoshi Arakawa, Chihaya Yamada, Kentaro Shimizu, Katsunori Tanaka, Motomitsu Kitaoka, Yukishige Ito, Kiyotaka Fujita, Shinya Fushinobu .  Identification of a difructose dianhydride I synthase/hydrolase from oral bacterium establishes a novel glycoside hydrolase family. .  The Journal of biological chemistry297 ( 5 ) 101324 - 101324   2021.10Reviewed International journal

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    Fructooligosaccharides and their anhydrides are widely utilized as health-promoting foods and prebiotics. Various enzymes acting on β-D-fructofuranosyl linkages of natural fructan polymers have been utilized to produce functional compounds. However, enzymes that hydrolyze and form α-D-fructofuranosyl linkages have been less studied. Here, we identified the BBDE_2040 gene product from Bifidobacterium dentium (αFFase1) as an enzyme with α-D-fructofuranosidase and α-D-arabinofuranosidase activities and an anomer-retaining manner. αFFase1 is not homologous with any known enzymes, suggesting that it is a member of a novel glycoside hydrolase family. When caramelized fructose sugar was incubated with αFFase1, conversions of β-D-Frup-(2→1)-α-D-Fruf to α-D-Fruf-1,2':2,1'-β-D-Frup (diheterolevulosan II), and from β-D-Fruf-(2→1)-α-D-Fruf (inulobiose) to α-D-Fruf-1,2':2,1'-β-D-Fruf (difructose dianhydride I, DFA I) were observed. The reaction equilibrium between inulobiose and DFA I was biased toward the latter (1:9) to promote the intramolecular dehydrating condensation reaction. Thus, we named this enzyme DFA I synthase/hydrolase. The crystal structures of αFFase1 in complex with β-D-Fruf and β-D-Araf were determined at resolutions of up to 1.76 Å. Modeling of a DFA I molecule in the active site and mutational analysis also identified critical residues for catalysis and substrate binding. The hexameric structure of αFFase1 revealed the connection of the catalytic pocket to a large internal cavity via a channel. Molecular dynamics analysis implied stable binding of DFA I and inulobiose to the active site with surrounding water molecules. Taken together, these results establish DFA I synthase/hydrolase as a member of a new glycoside hydrolase family (GH172).

    DOI： 10.1016/j.jbc.2021.101324

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  • Enkang Zhu, Kentaro Hiramatsu, Taiga Inoue, Kazuki Mori, Kosuke Tashiro, Kiyotaka Fujita, Takefumi Karashima, Hideharu Takashita, Kayu Okutsu, Yumiko Yoshizaki, Kazunori Takamine, Hisanori Tamaki, Taiki Futagami .  Deficiency of β-xylosidase activity in Aspergillus luchuensis mut. kawachii IFO 4308. .  Bioscience, biotechnology, and biochemistry88 ( 7 ) 816 - 823   2024.4Invited Reviewed International journal

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    In this study, we investigated a deleterious mutation in the β-xylosidase gene, xylA (AkxylA), in Aspergillus luchuensis mut. kawachii IFO 4308 by constructing an AkxylA disruptant and complementation strains of AkxylA and xylA derived from A. luchuensis RIB2604 (AlxylA), which does not harbor the mutation in xylA. Only the AlxylA complementation strain exhibited significantly higher growth and substantial β-xylosidase activity in medium containing xylan, accompanied by an increase in XylA expression. This resulted in lower xylobiose and higher xylose concentrations in the mash of barley shochu. These findings suggest that the mutation in xylA affects xylose levels during the fermentation process. Because the mutation in xylA was identified not only in the genome of strain IFO 4308 but also the genomes of other industrial strains of A. luchuensis and A. luchuensis mut. kawachii, these findings enhance our understanding of the genetic factors that affect the fermentation characteristics.

    DOI： 10.1093/bbb/zbae046

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  • Lee S., Leclercq L.D., Guerardel Y., Szymanski C.M., Hurtaux T., Doering T.L., Katayama T., Fujita K., Aoki K., Aoki-Kinoshita K.F. .  MicroGlycoDB: A database of microbial glycans using Semantic Web technologies .  BBA Advances6   2024.1Invited Reviewed

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    Language：Japanese   Publisher：BBA Advances  

    Glycoconjugates are present on microbial surfaces and play critical roles in modulating interactions with the environment and the host. Extensive research on microbial glycans, including elucidating the structural diversity of the glycan moieties of glycoconjugates and polysaccharides, has been carried out to investigate the function of glycans in modulating the interactions between the host and microbes, to explore their potential applications in the therapeutic targeting of pathogenic species, and in the use as probiotics in gut microbiomes. However, glycan-related information is dispersed across numerous databases and a vast amount of literature, which makes it laborious and time-consuming to identify and gather the relevant information about microbial glycosylation. This challenge can be addressed by a comprehensive database, which could offer insight into the fundamental processes underlying glycosylation. We have developed a MicroGlycoDB database to provide integrated glycan information on important model microorganisms. The data is described using Semantic Web Technologies, which allow microbial glycan data to be represented in a structured format accessible by machines, thus facilitating data sharing and integration with other resources that catalog features such as pathways, diseases, or interactions. This semantic data based on ontologies will contribute to the discovery of new knowledge in the field of microbiology, along with the expansion of information on the glycosylation of other microorganisms.

    DOI： 10.1016/j.bbadva.2024.100126

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  • Akihiro Ishiwata, Toma Kashima, Machika Kaieda, Katsunori Tanaka, Kiyotaka Fujita, Shinya Fushinobu, Yukishige Ito .  Synthesis and structural analysis of D-fructofuranosylated compounds for the analysis of GH172 difructose dianhydride I synthase/hydrolase .  Pure Appl. Chem.95 ( 9 ) in press - 964   2023.4Invited Reviewed

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：Walter de Gruyter GmbH  

    Abstract

    d-Arabinofuranosidases (Arafases) degrade the arabinan in the cell wall of acid-fast bacteria like Mycobacterium. Synthetic arabinan fragment probes could be used to investigate the function of d-Arafases, whose synthetic studies had been reported previously. The homologue of one of the arabinan-degrading enzymes, exo-α-d-Arafase, was identified as BBDE_2040 from Bifidobacterium dentium. BBDE_2040, which is a homologue of α-d-Arafase, was also observed to hydrolyze α-d-fructofuranosides (Fruf), whose linkage is found in food. In this paper, we present synthetic studies and structural analysis of the α-d-Araf and α-d-Fruf derivatives as substrates and products of the enzymatic reaction for a thorough examination of BBDE_2040. The results indicated that BBDE_2040 is a glycoside hydrolase (GH) family 172 difructose dianhydride I synthase/hydrolase and an anomer-retaining GH.

    DOI： 10.1515/pac-2023-0112

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    Other Link： https://www.degruyter.com/document/doi/10.1515/pac-2023-0112/pdf

  • Akihiro Ishiwata, Satoru Narita, Kenta Kimura, Katsunori Tanaka, Kiyotaka Fujita, Shinya Fushinobu, Yukishige Ito .  Mechanism-based inhibition of GH127/146 cysteine glycosidases by stereospecifically functionalized l-arabinofuranosides. .  Bioorganic & medicinal chemistry75   117054 - 117054   2022.10Reviewed International journal

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    Language：English   Publishing type：Research paper (scientific journal)  

    To understand the precise mechanism of the glycoside hydrolase (GH) family 127, a cysteine β-l-arabinofuranosidase (Arafase) - HypBA1 - has been isolated from Bifidobacterium longum in the human Gut microbiota, and the design and synthesis of the mechanism-based inhibitors such as l-Araf-haloacetamides have been carried out. The α-l-Araf-azide derivative was used as the monoglycosylamine equivalent to afford the l-Araf-chloroacetamides (α/β-1-Cl) as well as bromoacetamides (α/β-1-Br) in highly stereoselective manner through Staudinger reaction followed by amide formation with/without anomerization. Against HypBA1, the probes 1, especially in the case of α/β-1-Br inhibited the hydrolysis. Conformational implications of these observations are discussed in this manuscript. Additional examinations using l-Araf-azides (α/β-5) resulted in further mechanistic observations of the GH127/146 cysteine glycosidases, including the hydrolysis of β-5 as the substrate and oxidative inhibition by α-5 using the GH127 homologue.

    DOI： 10.1016/j.bmc.2022.117054

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  • Akihiro Ishiwata, Kiyotaka Fujita, Shinya Fushinobu, Katsunori Tanaka, Yukishige Ito .  Synthesis of naturally occurring β-L-arabinofuranosyl-L-arabinofuranoside structures towards the substrate specificity evaluation of β-L-arabinofuranosidase. .  Bioorganic & medicinal chemistry68   116849 - 116849   2022.5Reviewed International journal

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    Language：English   Publishing type：Research paper (scientific journal)  

    Methyl β-l-arabinofuranosyl-(1 → 2)-, -(1 → 3)-, and -(1 → 5)-α-l-arabinofuranosides have been stereoselectively synthesized through 2-naphthylmethyl ether-mediated intramolecular aglycon delivery (NAP-IAD), whose β-linkages were confirmed by NMR analysis on the 3JH1-H2 coupling constant and 13C chemical shift of C1. The NAP-IAD approach was simply extended for the synthesis of trisaccharide motifs possessing β-l-arabinofuranosyl-(1 → 5)-l-arabinofuranosyl non-reducing terminal structure with the branched β-l-arabinofuranosyl-(1 → 5)-[α-l-arabinofuranosyl-(1 → 3)]-α-l-arabinofuranosyl and the liner β-l-arabinofuranosyl-(1 → 5)-β-l-arabinofuranosyl-(1 → 5)-β-l-arabinofuranosyl structures in olive arabinan and dinoflagellate polyethers, respectively. The results on the substrate specificity of a bifidobacterial β-l-arabinofuranosidase HypBA1 using the regioisomers indicated that HypBA1 could hydrolyze all three linkages however behaved clearly less active to β-(1 → 5)-linked disaccharide than other two regioisomers including the proposed natural degradation product, β-(1 → 2)-linked one from plant extracellular matrix such as extensin. On the other hand, Xanthomonas XeHypBA1 was found to hydrolyze all three disaccharides as the substrate with higher specificity to β-(1 → 2)-linkage than bifidobacterial HypBA1.

    DOI： 10.1016/j.bmc.2022.116849

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  • Masahiro Komeno, Yuki Yoshihara, Junya Kawasaki, Wataru Nabeshima, Koshi Maeda, Yuki Sasaki, Kiyotaka Fujita, Hisashi Ashida .  Two α-L-arabinofuranosidases from Bifidobacterium longum subsp. longum are involved in arabinoxylan utilization. .  Applied microbiology and biotechnology106 ( 5-6 ) 1957 - 1965   2022.3Reviewed International journal

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    Arabinoxylan (AX) and arabinoxylooligosaccharides (AXOs) are carbohydrate sources utilized by Bifidobacterium longum subsp. longum. However, their degradation pathways are poorly understood. In this study, we characterized two genes, BLLJ_1850 and BLLJ_1851, in the hemicellulose-degrading gene cluster (BLLJ_1836-BLLJ_1859) of B. longum subsp. longum JCM 1217. Both recombinant enzymes expressed in Escherichia coli exhibited exo-α-L-arabinofuranosidase activity toward p-nitrophenyl-α-L-arabinofuranoside. BlArafE (encoded by BLLJ_1850) contains the glycoside hydrolase family 43 (GH43), subfamily 22 (GH43_22), and GH43_34 domains. The BlArafE GH43_22 domain was demonstrated to release α1,3-linked Araf from AX, but the function of BlArafE GH43_34 could not be clearly identified in this study. BlArafD (encoded by BLLJ_1851) contains GH43 unclassified subfamily (GH43_UC) and GH43_26 domains. The BlArafD GH43_UC domain showed specificity for α1,2-linked Araf in α1,2- and α1,3-Araf double-substituted structures in AXOs, while BlArafD GH43_26 was shown to hydrolyze α1,5-linked Araf in the arabinan backbone. Co-incubation of BlArafD and BlArafE revealed that these two enzymes sequentially removed α1,2-Araf and α1,3-Araf from double-substituted AXOs in this order. B. longum strain lacking BLLJ_1850-BLLJ_1853 did not grow in the medium containing α1,2/3-Araf double-substituted AXOs, suggesting that BlArafE and BlArafD are important for the assimilation of AX. KEY POINTS: • BlArafD GH43 unclassified subfamily domain is a novel α1,2-L-arabinofuranosidase. • BlArafE GH43 subfamily 22 domain is an α1,3-L-arabinofuranosidase. • BlArafD and BlArafE cooperatively degrade α1,2/3-Araf double-substituted arabinoxylan.

    DOI： 10.1007/s00253-022-11845-x

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  • Yuki Sasaki, Masahiro Komeno, Akihiro Ishiwata, Ayako Horigome, Toshitaka Odamaki, Jin-Zhong Xiao, Katsunori Tanaka, Yukishige Ito, Kanefumi Kitahara, Hisashi Ashida, Kiyotaka Fujita .  Mechanism of cooperative degradation of gum arabic arabinogalactan protein by Bifidobacterium longum surface enzymes. .  Applied and environmental microbiology88 ( 6 ) aem0218721   2022.2Mechanism of cooperative degradation of gum arabic arabinogalactan protein by Bifidobacterium longum surface enzymes.Reviewed International journal

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    Gum arabic is an arabinogalactan protein (AGP) that is effective as a prebiotic for the growth of bifidobacteria in the human intestine. We recently identified a key enzyme in the glycoside hydrolase (GH) family 39, 3-O-α-d-galactosyl-α-l-arabinofuranosidase (GAfase), for the assimilation of gum arabic AGP in Bifidobacterium longum subsp. longum. The enzyme released α-d-Galp-(1→3)-l-Ara and β-l-Arap-(1→3)-l-Ara from gum arabic AGP and facilitated the action of other enzymes for degrading the AGP backbone and modified sugar. In this study, we identified an α-l-arabinofuranosidase (BlArafE; encoded by BLLJ_1850), a multidomain enzyme with both GH43_22 and GH43_34 catalytic domains, as a critical enzyme for the degradation of modified α-l-arabinofuranosides in gum arabic AGP. Site-directed mutagenesis approaches revealed that the α1,3/α1,4-Araf double-substituted gum arabic AGP side chain was initially degraded by the GH43_22 domain and subsequently cleaved by the GH43_34 domain to release α1,3-Araf and α1,4-Araf residues, respectively. Furthermore, we revealed that a tetrasaccharide, α-l-Rhap-(1→4)-β-d-GlcpA-(1→6)-β-d-Galp-(1→6)-d-Gal, was a limited degradative oligosaccharide in the gum arabic AGP fermentation of Bi. longum JCM7052. The oligosaccharide was produced from gum arabic AGP by the cooperative action of the three cell surface-anchoring enzymes, GAfase, exo-β1,3-galactanase (Bl1,3Gal), and BlArafE, on Bi. longum JCM7052. Furthermore, the tetrasaccharide was utilized by the commensal bacteria. IMPORTANCE Terminal galactose residues of the side chain of gum arabic arabinogalactan protein (AGP) are mainly substituted by α1,3/α1,4-linked Araf and β1,6-linked α-l-Rhap-(1→4)-β-d-GlcpA residues. This study found a multidomain α-l-arabinofuranosidase (BlArafE) with GH43_22 and GH43_34 catalytic domains showing cooperative action for degrading α1,3/α1,4-linked Araf of the side chain of gum arabic AGP. In particular, the GH43_34 domain of BlArafE was a novel α-l-arabinofuranosidase for cleaving the α1,4-Araf linkage of terminal galactose. α-l-Rhap-(1→4)-β-d-GlcpA-(1→6)-β-d-Galp-(1→6)-d-Gal tetrasaccharide was released from gum arabic AGP by the cooperative action of GAfase, GH43_24 exo-β-1,3-galactanase (Bl1,3Gal), and BlArafE and remained after Bi. longum JCM7052 culture. Furthermore, in vitro assimilation test of the remaining oligosaccharide using Bacteroides species revealed that cross-feeding may occur from bifidobacteria to other taxonomic groups in the gut.

    DOI： 10.1128/aem.02187-21

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  • KASHIMA Toma, ISHIWATA Akihiro, FUJITA Kiyotaka, FUSHINOBU Shinya .  Identification and Structural Basis of an Enzyme Degrading Oligosaccharides in Caramel .  Seibutsu Butsuri62 ( 3 ) 184 - 186   2022Invited

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    Language：Japanese   Publisher：The Biophysical Society of Japan General Incorporated Association  

    DOI： 10.2142/biophys.62.184

  • Maruyama S, Sawano K, Amaki S, Suzuki T, Narita S, Kimura K, Arakawa T, Yamada C, Ito Y, Dohmae N, Fujita K, Ishiwata A, Fushinobu S .  Substrate complex structure, active site labeling and catalytic role of the zinc ion in cysteine glycosidase. .  Glycobiology   2021.10Substrate complex structure, active site labeling and catalytic role of the zinc ion in cysteine glycosidase.Invited Reviewed

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    DOI： 10.1093/glycob/cwab103

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  • Sasaki Yuki, Uchimura Yumi, Kitahara Kanefumi, Fujita Kiyotaka .  Characterization of a GH36 α-D-Galactosidase Associated with Assimilation of Gum Arabic in Bifidobacterium longum subsp. longum JCM7052 .  Journal of Applied Glycoscience68 ( 2 ) 47 - 52   2021.5Characterization of a GH36 α-D-Galactosidase Associated with Assimilation of Gum Arabic in Bifidobacterium longum subsp. longum JCM7052Reviewed

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    Authorship：Corresponding author   Language：English   Publisher：(一社)日本応用糖質科学会  

  • Sasaki Y, Horigome A, Odamaki T, Xiao JZ, Ishiwata A, Ito Y, Kitahara K, Fujita K .  Novel 3-O-α-D-galactosyl-α-L-arabinofuranosidase for the assimilation of gum arabic arabinogalactan protein in Bifidobacterium longum subsp. longum .  Appl. Environ. Microbiol.87 ( 10 ) e02690 - 02620   2021.4Novel 3-O-α-D-galactosyl-α-L-arabinofuranosidase for the assimilation of gum arabic arabinogalactan protein in Bifidobacterium longum subsp. longumReviewed

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    Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1128/AEM.02690-20

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  • Yamamoto I, Ueno Y, Geshi M, Inagaki Y, Odamaki T, Fujita K. .  Complete genome sequence of Bifidobacterium longum subsp. longum JCM7052 .  Microbiol. Resour. Announc.10   e01193-011   2021.4Reviewed

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    Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1128/MRA.01193-20

  • Saito K, Viborg AH, Sakamoto S, Arakawa T, Yamada C, Fujita K, Fushinobu S. .  Crystal structure of β-L-arabinobiosidase belonging to glycoside hydrolase family 121 .  PLoS ONE15 ( 6 ) e0231513   2020.6Reviewed

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    Language：English   Publishing type：Research paper (scientific journal)  

    © 2020 Saito et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Enzymes acting on α-L-arabinofuranosides have been extensively studied; however, the structures and functions of β-L-arabinofuranosidases are not fully understood. Three enzymes and an ABC transporter in a gene cluster of Bifidobacterium longum JCM 1217 constitute a degradation and import system of β-L-arabinooligosaccharides on plant hydroxyproline-rich glycoproteins. An extracellular β-L-arabinobiosidase (HypBA2) belonging to the glycoside hydrolase (GH) family 121 plays a key role in the degradation pathway by releasing β-1,2-linked arabinofuranose disaccharide (β-Ara2) for the specific sugar importer. Here, we present the crystal structure of the catalytic region of HypBA2 as the first three-dimensional structure of GH121 at 1.85 Å resolution. The HypBA2 structure consists of a central catalytic (α/α)6 barrel domain and two flanking (N- and C-terminal) β-sandwich domains. A pocket in the catalytic domain appears to be suitable for accommodating the β-Ara2 disaccharide. Three acidic residues Glu383, Asp515, and Glu713, located in this pocket, are completely conserved among all members of GH121; site-directed mutagenesis analysis showed that they are essential for catalytic activity. The active site of HypBA2 was compared with those of structural homologs in other GH families: GH63 α-glycosidase, GH94 chitobiose phosphorylase, GH142 β-L-arabinofuranosidase, GH78 α-L-rhamnosidase, and GH37 α,α-trehalase. Based on these analyses, we concluded that the three conserved residues are essential for catalysis and substrate binding. β-L-Arabinobiosidase genes in GH121 are mainly found in the genomes of bifidobacteria and Xanthomonas species, suggesting that the cleavage and specific import system for the β-Ara2 disaccharide on plant hydroxyproline-rich glycoproteins are shared in animal gut symbionts and plant pathogens.

    DOI： 10.1371/journal.pone.0231513

    Scopus

    PubMed

  • Miyake M, Terada T, Shimokawa M, Sugimoto N, Arakawa T, Shimizu K, Igarashi K, Fujita K, and Fushinobu, S. .  Structural analysis of β-L-arabinobiose-binding protein in the metabolic pathway of hydroxyproline-rich glycoproteins in Bifidobacterium longum. .  FEBS J.287 ( 23 ) 5114 - 5129   2020.4Reviewed

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    Bifidobacterium longum is a symbiotic human gut bacterium that has a degradation system for β-arabinooligosaccharides, which are present in the hydroxyproline-rich glycoproteins of edible plants. Whereas microbial degradation systems for α-linked arabinofuranosyl carbohydrates have been extensively studied, little is understood about the degradation systems targeting β-linked arabinofuranosyl carbohydrates. We functionally and structurally analyzed a substrate-binding protein (SBP) of a putative ABC transporter (BLLJ_0208) in the β-arabinooligosaccharide degradation system. Thermal shift assays and isothermal titration calorimetry revealed that the SBP specifically bound Araf-β1,2-Araf (β-Ara2 ) with a Kd of 0.150 μm, but did not bind L-arabinose or methyl-β-Ara2 . Therefore, the SBP was termed β-arabinobiose-binding protein (BABP). Crystal structures of BABP complexed with β-Ara2 were determined at resolutions of up to 1.78 Å. The findings showed that β-Ara2 was bound to BABP within a short tunnel between two lobes as an α-anomeric form at its reducing end. BABP forms extensive interactions with β-Ara2 , and its binding mode was unique among SBPs. A molecular dynamics simulation revealed that the closed conformation of substrate-bound BABP is stable, whereas substrate-free form can adopt a fully open and two distinct semi-open states. The importer system specific for β-Ara2 may contribute to microbial survival in biological niches with limited amounts of digestible carbohydrates. DATABASE: Atomic coordinates and structure factors (codes 6LCE and 6LCF) have been deposited in the Protein Data Bank (http://wwpdb.org/).

    DOI： 10.1111/febs.15315

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    PubMed

  • Kenji Katayama, Mio Nishinaka, Yoshiyuki Nakamura, Toshikazu Kuranouchi, Akiko Ohara-Takada, Kiyotaka Fujita, Kanefumi Kitahara .  New Sweetpotato Lines have High Amylose and Resistant Starch Contents .  STARCH-STARKE71 ( 3-4 )   2019.3Reviewed

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    Language：English   Publisher：WILEY-V C H VERLAG GMBH  

    The sweetpotato is an important starch crop and a health-promoting food, owing to its richness in functional components. New sweetpotato lines (HA lines) with high amylose and high resistant starch (RS) contents are developed by cross-breeding, and the authors evaluate the root and starch properties and the influence of heat-treatment on the RS contents of these HA lines. The HA lines are found to have comparable root weights; much lower starch contents; more than 28% higher (45-59%) amylose contents; much lower viscosities, gelatinization temperatures, and gelatinization enthalpy changes; a higher proportion of both amylose and short chains (DP 6-11) fractions in the unit chain distribution of the debranched starches; and higher RS contents in gelatinized starches, raw, and heat-treated roots than those of the ordinary varieties. These results present useful information for food industries and breeders of sweetpotato.

    DOI： 10.1002/star.201800180

    Web of Science

    Scopus

  • Komeno M, Hayamizu H, Fujita K, Ashida H .  Two novel α-L-arabinofuranosidases from Bifidobacterium longum subsp. longum belonging to glycoside hydrolase family 43 cooperatively degrade arabinan. .  Applied and environmental microbiology85 ( 6 )   2019.3Reviewed

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    Language：English  

    DOI： 10.1128/AEM.02582-18

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    PubMed

  • M. Komeno, H. Hayamizu, K. Fujita, H. Ashida .  Two Novel α-L-Arabinofuranosidases from Bifidobacterium longum subsp. longum Belonging to Glycoside Hydrolase Family 43 Cooperatively Degrade Arabinan. .    85   e02582-18   2019.1Two Novel α-L-Arabinofuranosidases from Bifidobacterium longum subsp. longum Belonging to Glycoside Hydrolase Family 43 Cooperatively Degrade Arabinan.Invited Reviewed

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  • Fujita K, Sakamoto A, Kaneko S, Kotake T, Tsumuraya Y, Kitahara K .  Degradative enzymes for type II arabinogalactan side chains in Bifidobacterium longum subsp. longum. .  Appl. Microbiol. Biotech.103   1299 - 1310   2019.1Degradative enzymes for type II arabinogalactan side chains in Bifidobacterium longum subsp. longum.Reviewed

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    Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1007/s00253-018-9

  • Wade Abbott, Orly Alber, Ed Bayer, Jean-Guy Berrin, Alisdair Boraston, Harry Brumer, Ryszard Brzezinski, Anthony Clarke, Beatrice Cobucci-Ponzano, Darrell Cockburn, Pedro Coutinho, Mirjam Czjzek, Bareket Dassa, Gideon John Davies, Vincent Eijsink, Jens Eklof, Alfons Felice, Elizabeth Ficko-Blean, Geoff Pincher, Thierry Fontaine, Zui Fujimoto, Kiyotaka Fujita, Shinya Fushinobu, Harry Gilbert, Tracey Gloster, Ethan Goddard-Borger, Ian Greig, Jan-Hendrik Hehemann, Glyn Hemsworth, Bernard Henrissat, Masafumi Hidaka, Ramon Hurtado-Guerrero, Kiyohiko Igarashi, Takuya Ishida, Stefan Janecek, Seino Jongkees, Nathalie Juge, Satoshi Kaneko, Takane Katayama, Motomitsu Kitaoka, Naotake Konno, Daniel Kracher, Anna Kulminskaya, Alicia Lammerts van Bueren, Sine Larsen, Junho Lee, Markus Linder, Leila LoLeggio, Roland Ludwig, Ana Luis, Mirko Maksimainen, Brian Mark, Richard McLean, Gurvan Michel, Gurvan Michel, Cedric Montanier, Marco Moracci, Haruhide Mori, Hiroyuki Nakai, Wim Nerinckx, Takayuki Ohnuma, Richard Pickersgill, Kathleen Piens, Tirso Pons, Etienne Rebuffet, Peter Reilly, Magali Remaud-Simeon, Brian Rempel, Kyle Robinson, David Rose, Juha Rouvinen, Wataru Saburi, Yuichi Sakamoto, Mats Sandgren, Fathima Shaikh, Yuval Shoham, Franz St John, Jerry Stahlberg, Michael Suits, Gerlind Sulzenbacher, Tomomi Sumida, Ryuichiro Suzuki, Birte Svensson, Toki Taira, Ed Taylor, Takashi Tonozuka, Breeanna Urbanowicz, Gustav Vaaje-Kolstad, Wim Van den Ende, Annabelle Varrot, Maxime Versluys, Florence Vincent, David Vocadlo, Warren Wakarchuk, Tom Wennekes, Rohan Williams, Spencer Williams, David Wilson, Stephen Withers, Katsuro Yaoi, Vivian Yip, Ran Zhang .  Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes .  GLYCOBIOLOGY28 ( 1 ) 3 - 8   2018.1Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymesInternational coauthorship

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    Language：English   Publisher：OXFORD UNIV PRESS INC  

    CAZypedia was initiated in 2007 to create a comprehensive, living encyclopedia of the carbohydrate active enzymes (CAZymes) and associated carbohydrate-binding modules involved in the synthesis, modification and degradation of complex carbohydrates. CAZypedia is closely connected with the actively curated CAZy database, which provides a sequence-based foundation for the biochemical, mechanistic and structural characterization of these diverse proteins. Now celebrating its 10th anniversary online, CAZypedia is a successful example of dynamic, community-driven and expert-based biocuration. CAZypedia is an open-access resource available at URL http://www.cazypedia.org.

    DOI： 10.1093/glycob/cwx089

    Web of Science

  • Sasaki, Y., Togo, N., Kitahara, K., and Fujita, K. .  Characterization of a GH36 β-L-Arabinopyranosidase in Bifidobacterium adolescentis .  J. Appl. Glycosci.65 ( 2 ) 23 - 30   2018Invited Reviewed

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    Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.5458/jag.jag.JAG-2018_001

    Web of Science

  • Nakamura, M., Yasukawa, Y., Furusawa, A., Fuchiwaki, T., Honda, T., Okamura, Y., Fujita, K., Iwai, H. .  Functional characterization of unique enzymes in Xanthomonas euvesicatoria related to degradation of arabinofurano-oligosaccharides on hydroxyproline-rich glycoproteins. .  PLoS One9   e0201982   2018Functional characterization of unique enzymes in Xanthomonas euvesicatoria related to degradation of arabinofurano-oligosaccharides on hydroxyproline-rich glycoproteins.Reviewed

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  • Nakamura M, Yasukawa Y, Furusawa A, Fuchiwaki T, Honda T, Okamura Y, Fujita K, Iwai H .  Functional characterization of unique enzymes in Xanthomonas euvesicatoria related to degradation of arabinofurano-oligosaccharides on hydroxyproline-rich glycoproteins. .  PloS one13 ( 8 ) e0201982   2018

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  • FUJITA Kiyotaka .  The Metabolic Pathways for the Sugar Chains of Glycoproteins in Bifidobacteria:Prebiotic Glycoproteins Are Growth Substrates for Bifidobacteria .  KAGAKU TO SEIBUTSU55 ( 4 ) 242 - 248   2017Invited Reviewed

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    Language：Japanese   Publisher：Japan Society for Bioscience, Biotechnology, and Agrochemistry  

    DOI： 10.1271/kagakutoseibutsu.55.242

    J-GLOBAL

  • Shimokawa, M., Kitahara, K., and Fujita, K. .  Characterization of a β-L-arabinopyranosidase from Bifidobacterium longum subsp. longum. .  J. Appl. Glycosci.62   1 - 6   2015.2Characterization of a β-L-arabinopyranosidase from Bifidobacterium longum subsp. longum.Reviewed

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    Language：Japanese   Publishing type：Research paper (scientific journal)  

  • Kitahara, K., yamasaki T., Fujita, K., and Suganuma, T. .  Physicochemical Properties of Starches from Recently Bred Sweetpotatoes in Japan. .  J. Appl. Glycosci.61   81 - 88   2014.8Physicochemical Properties of Starches from Recently Bred Sweetpotatoes in Japan.Reviewed

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  • Fujita, K., Sakaguchi, T., Sakamoto, A., Shimokawa, M., and Kitahara, K. .  Bifidobacterium longum subsp. longum exo-β-1,3-galactanase, an enzyme for the degradation of type II arabinogalactan. .  Appl. Environ. Microbiol.80 ( 15 ) 4577 - 4584   2014.8Bifidobacterium longum subsp. longum exo-β-1,3-galactanase, an enzyme for the degradation of type II arabinogalactan.Reviewed

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  • 時村金愛，下園英俊，久米隆志，西原悟，小山田耕作，福元伸一，藤田清貴，北原兼文 .  栽培条件の異なるサツマイモ新品種「こなみずき」塊根の澱粉品質 .  応用糖質科学4 ( 3 ) 234 - 240   2014.8栽培条件の異なるサツマイモ新品種「こなみずき」塊根の澱粉品質Reviewed

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  • Fujita, K., Takashi, Y., Obuchi, E., Kitahara, K., and Suganuma, T. .  Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: Functional elucidation of a DUF1680 protein family member. .  J. Biol. Chem.289   5240 - 5249   2014.2Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: Functional elucidation of a DUF1680 protein family member.Reviewed

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  • Ito, T., Saikawa, K., Kim, S., Fujita, K., Ishiwata, A., Kaeothip, S., Arakawa, T., Wakagi, T., Beckham G. T., Ito, Y., and Fushinobu, S. .  Crystal structure of glycoside hydrolase family 127 β-L-arabinofuranosidase from Bifidobacterium longum. .  Biochem. Biophys. Res. Commun.447   32 - 37   2014.1Crystal structure of glycoside hydrolase family 127 β-L-arabinofuranosidase from Bifidobacterium longum.Reviewed

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  • Kaeothip, S., Ishiwata, A., Ito, T., Fushinobu, S., Fujita, K., Ito., Y. .  Preparation of p-nitrophenyl β-L-arabinofuranoside as a substrate of β-L-arabinofuranosidase. .  Carbohydr. Res.382   95 - 100   2013Preparation of p-nitrophenyl β-L-arabinofuranoside as a substrate of β-L-arabinofuranosidase.Reviewed

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  • Kitahara, K., Takahata, Y., Otani, M., Tanaka, M., Katayama, K., Yoshinaga, M., Fujita, K., and Suganuma, T. .  Starch properties of transgenic sweetpotato plants modified by RNA interference of the starch synthase II gene. .  J. Appl. Glycosci.58 ( 3 ) 85 - 90   2011.9Starch properties of transgenic sweetpotato plants modified by RNA interference of the starch synthase II gene.Reviewed

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  • Fujita, K., Sakamoto, S., Ono, Y., Wakao, M., Suda, Y., Kitahara, K., and Suganuma, T. .  Molecular cloning and characterization of a β-L-arabinobiosidase in Bifidobacterium longum that belongs to a novel glycoside hydrolase family. .  J. Biol. Chem.286 ( 7 ) 5143 - 5150   2011.2Molecular cloning and characterization of a β-L-arabinobiosidase in Bifidobacterium longum that belongs to a novel glycoside hydrolase family.Reviewed

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    Language：Japanese   Publishing type：Research paper (scientific journal)  

  • Al-Dabbas, M. M., Al-Ismail, K., Abu-Taleb, R., Hashimoto, F., Rabah, I. O., Kitahara, K. Fujita, K., and Suganuma, T. .  Chemistry and antiproliferative activities of 3-methoxyflavones isolated from Varthemia iphionoides. .  Chem. Nat. Comp.47   17 - 21   2011Chemistry and antiproliferative activities of 3-methoxyflavones isolated from Varthemia iphionoides.Reviewed

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  • Ashida H, Ozawa H, Fujita K, Suzuki S, Yamamoto K. .  Syntheses of mucin-type O-glycopeptides and oligosaccharides using transglycosylation and reverse-hydrolysis activities of Bifidobacterium endo-α-N-acetylgalactosaminidase. .  Glycoconj. J.27   125 - 132   2010Syntheses of mucin-type O-glycopeptides and oligosaccharides using transglycosylation and reverse-hydrolysis activities of Bifidobacterium endo-α-N-acetylgalactosaminidase.Reviewed

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    Language：Japanese   Publishing type：Research paper (scientific journal)  

  • Umekawa, M., Huang, W., Li, B., Fujita, K., Ashida, H., Wang, L. X., and Yamamoto, K. .  Mutants of Mucor hiemalis endo-β-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities. .  J. Biol. Chem.283   4469 - 4479   2008.2Mutants of Mucor hiemalis endo-β-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities.Reviewed

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  • Fujita, K., Sato, R., Toma, K., Kitahara, K., Suganuma, T., Yamamoto, K., and Takegawa, K. .  Identification of the catalytic acid-base residue of Arthrobacter endo-b-N-acetylglucosaminidase by chemical rescue of an inactive mutant. .  J. Biochem.142 ( 3 ) 301 - 306   2007.9Identification of the catalytic acid-base residue of Arthrobacter endo-b-N-acetylglucosaminidase by chemical rescue of an inactive mutant. Reviewed

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  • Kitahara, K., Hamasuna, K., Nozuma, K., Otani, M., Hamada, T., Shimada, T., Fujita, K., and Suganuma, T. .  Physicochemical properties of amylose-free and high-amylose starches from transgenic sweetpotatoes modified by RNA interference. .  Carbohydrate Polymers69   233 - 240   2007.1Physicochemical properties of amylose-free and high-amylose starches from transgenic sweetpotatoes modified by RNA interference. Reviewed

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  • Fujita, K., and Yamamoto, K. .  A remodeling system for the oligosaccharide chains on glycoproteins with microbial endo-b-N-acetylglucosaminidases. .  Biochim. Biophis. Acta.・ELSEVIER1760 ( 11 ) 1631 - 1635   2006.11A remodeling system for the oligosaccharide chains on glycoproteins with microbial endo-b-N-acetylglucosaminidases.Reviewed

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  • Fujita, K., Oura, F., Nagamine, N., Katayama, T., Hiratake, J., Sakata, K., Kumagai, H., and Yamamoto, K .  Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-a-N-acetylgalactosaminidase from Bifidobacterium longum. .  J. Biol. Chem.・HighWire Press280 ( 45 ) 37415 - 37422   2005.11Identification and molecular cloning of a novel glycoside hydrolase family of core 1 type O-glycan-specific endo-a-N-acetylgalactosaminidase from Bifidobacterium longum.Reviewed

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  • Yamanoi, T., Yoshida, N., Oda, Y., Akaike, E., Tsutsumida, M., Kobayashi, N., Osumi, K., Yamamoto, K., Fujita, K., Takahashi, K., and Hattori, K. .  Synthesis of mono-glucose-branched cyclodextrins with a high inclusion ability for doxorubicin and their efficient glycosylation using Mucor hiemalis endo-β-N-acetylglucosaminidase .  Bioorg. Med. Chem. Lett.15   1009 - 1013   2005Synthesis of mono-glucose-branched cyclodextrins with a high inclusion ability for doxorubicin and their efficient glycosylation using Mucor hiemalis endo-β-N-acetylglucosaminidaseReviewed

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  • Fujita, K., Takami, H., Yamamoto, K., and Takegawa, K. .  Characterization of endo-β-N-acetylglucosaminidase from alkaliphilic Bacillus halodurans C-125 .  Biosci. Biotechnol. Biochem., ・JSBA68 ( 5 ) 41 - 49   2004.12Characterization of endo-β-N-acetylglucosaminidase from alkaliphilic Bacillus halodurans C-125Reviewed

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  • Fujita, K., Kobayashi, K., Iwamatsu, A., Takeuchi, M., Kumagai, H., and Yamamoto, K. .  Molecular cloning of Mucor hiemalis endo-b-N-acetylglucosaminidase and some properties of the recombinant enzyme. .  Arch. Biochem. Biophys., ・ELSEVIER432 ( 1 ) 1059 - 1066   2004.5Molecular cloning of Mucor hiemalis endo-b-N-acetylglucosaminidase and some properties of the recombinant enzyme.Reviewed

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  • Akaike, E., Tsutsumida, M., Osumi, K., Fujita, M., Yamanoi, T., Yamamoto, K., and Fujita, K. .  High efficiency of transferring a native sugar chain from a glycopeptide by a microbial endoglycosidase in organic solvents .  Carbohydr. Res.339   719 - 722   2004.1High efficiency of transferring a native sugar chain from a glycopeptide by a microbial endoglycosidase in organic solventsReviewed

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  • Yamanoi, T., Tsutsumida, M., Oda, Y., Akaike, E., Osumi, K., Yamamoto, K., and Fujita, K. .  Transglycosylation reaction of Mucor hiemalis endo-β-N-acetylglucosaminidase using sugar derivatives modified at C-1 or C-2 as oligosaccharide acceptors .  Carbohydr. Res.339   1403 - 1406   2004Transglycosylation reaction of Mucor hiemalis endo-β-N-acetylglucosaminidase using sugar derivatives modified at C-1 or C-2 as oligosaccharide acceptorsReviewed

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  • Mizutani, K., Okamoto, I., Fujita, K., Yamamoto, K., and Hirose, M. .  Structural and functional characterization of ovotransferrin produced by Pichia pastoris .  Biosci. Biotechnol. Biochem.68   376 - 383   2004Structural and functional characterization of ovotransferrin produced by Pichia pastorisReviewed

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  • Osumi, K., Makino, Y., Akaike, E., Yamanoi, T., Mizuno, M., Noguchi, M., Inazu, T., Yamamoto, K., and Fujita, K. .  Mucor hiemalis endo-β-N-acetylglucosaminidase can transglycosylate a bisecting hybrid-type oligosaccharide from an ovalbumin glycopeptide .  Carbohydr. Res.339   2633 - 2635   2004Mucor hiemalis endo-β-N-acetylglucosaminidase can transglycosylate a bisecting hybrid-type oligosaccharide from an ovalbumin glycopeptideReviewed

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  • Fujita, K., Tsuyoshi, M., Sano, M., Kato, I., and Takegawa, K. .  Transfer of high-mannose-type oligosaccharides to disaccharides by endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae .  J. Biosci. Bioeng.93 ( 6 ) 614 - 617   2002.6Transfer of high-mannose-type oligosaccharides to disaccharides by endo-β-N-acetylglucosaminidase from Arthrobacter protophormiaeReviewed

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  • Kato, T., Fujita, K., Takeuchi, M., Kobayashi, K., Natsuka, S., Ikura, K., Kumagai, H., and Yamamoto, K. .  Identification of an endo-β-N-acetylglucosaminidase gene in Caenorhabditis elegans and its expression in Escherichia coli .  Glycobiology12   581 - 587   2002Identification of an endo-β-N-acetylglucosaminidase gene in Caenorhabditis elegans and its expression in Escherichia coliReviewed

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  • Fujita, K., and Takegawa, K. .  Chemoenzymatic synthesis of neoglycoproteins using transglycosylation with endo-β-N-acetylglucosaminidase A .  Biochem. Biophys. Res. Commun.2825   678 - 682   2001.1Chemoenzymatic synthesis of neoglycoproteins using transglycosylation with endo-β-N-acetylglucosaminidase AReviewed

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  • Fujita, K., and Takegawa, K. .  Tryptophan-216 is essential for the transglycosylation activity of endo-β-N-acetylglucosaminidase A .  Biochem. Biophys. Res. Commun.283   680 - 686   2001Tryptophan-216 is essential for the transglycosylation activity of endo-β-N-acetylglucosaminidase AReviewed

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  • Fujita, K., Nakatake, R., Yamabe, K., Watanabe, A., Asada, Y., and Takegawa, K. .  Identification of amino acid residues essential for the substrate specificity of Flavobacterium sp. endo-β-N-acetylglucosaminidase .  Biosci. Biotechnol. Biochem.65   1542 - 1548   2001Identification of amino acid residues essential for the substrate specificity of Flavobacterium sp. endo-β-N-acetylglucosaminidaseReviewed

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  • Fujita, K., Asada, Y., Yamamoto, K., and Takegawa, K. .  Plate assay for endo-β-N-acetylglucosaminidase activity using a chromogenic substrate synthesized by transglycosylation with Arthrobacter endo-β-N-acetylglucosaminidase .  J. Biosci. Bioeng.90 ( 4 ) 462 - 464   2000.4Plate assay for endo-β-N-acetylglucosaminidase activity using a chromogenic substrate synthesized by transglycosylation with Arthrobacter endo-β-N-acetylglucosaminidaseReviewed

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  • Fujita, K., Tanaka, N., Sano, M., Kato, I., Asada, Y., and Takegawa, K. .  Synthesis of neoglycoenzymes with homogeneous N-linked oligosaccharides using immobilized endo-β-N-acetylglucosaminidase A .  Biochem. Biophys. Res. Commun.267   134 - 138   2000Synthesis of neoglycoenzymes with homogeneous N-linked oligosaccharides using immobilized endo-β-N-acetylglucosaminidase AReviewed

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  • Bhuiyan, M. S., Ito, Y., Nakamura, A., Tanaka, N., Fujita, K., Fukui, H.,and Takegawa, K. .  Nystatin effects on vacuolar function in Saccharomyces cerevisiae .  Biosci. Biotechnol. Biochem.63   1075 - 1082   1999Nystatin effects on vacuolar function in Saccharomyces cerevisiae Reviewed

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  • Tanaka, N., Awai, A., Bhuiyan, M. S., Fujita, K., Fukui, H., and Takegawa, K. .  Cell surface galactosylation is essential for nonsexual flocculation in Schizosaccharomyces pombe .  J. Bacteriol.181   1356 - 1359   1999Cell surface galactosylation is essential for nonsexual flocculation in Schizosaccharomyces pombeReviewed

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    Language：English   Publishing type：Research paper (scientific journal)  

  • Takegawa, K., Fujita, K., Fan, J. Q., Tabuchi, M., Tanaka, N., Kondo, A., Iwamoto, H., Kato, I., Lee, Y. C., and Iwahara, S. .  Enzymatic synthesis of a neoglycoconjugate by transglycosylation with Arthrobacter endo-β-N-acetylglucosaminidase: A substrate for colorimetric detection of endo-β-N-acetylglucosaminidase activity. .  Anal. Biochem.257   218 - 223   1998Enzymatic synthesis of a neoglycoconjugate by transglycosylation with Arthrobacter endo-β-N-acetylglucosaminidase: A substrate for colorimetric detection of endo-β-N-acetylglucosaminidase activity.Reviewed

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    Language：Japanese   Publishing type：Research paper (scientific journal)  

  • Takegawa, K., Yamabe, K., Fujita, K., Tabuchi, M., Mita, M., Izu, H., Watanabe, A., Asada, Y., Sano, M., Kondo, A., Kato, I., and Iwahara, S. .  Cloning, sequencing, and expression of Arthrobacter protophormiae endo-β-N-acetylglucosaminidase in Escherichia coli .  Arch. Biochem. Biophys.338   24 - 28   1997Cloning, sequencing, and expression of Arthrobacter protophormiae endo-β-N-acetylglucosaminidase in Escherichia coliReviewed

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    Language：Japanese   Publishing type：Research paper (scientific journal)  

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Books

  • 第7章 エンドAの構造から糖タンパク質合成の最適条件を探る

    竹川薫、藤田清貴（ Role： Joint author）

    「バイオ医薬品開発における糖鎖技術」早川堯夫・掛樋一晃・平林 淳監修・シーエムシー出版  2011.11 

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    Language：Japanese Book type：Scholarly book

  • 酵素的切断法・(2)O-グリコシド結合の酵素分解

    藤田清貴，山本憲二（ Role： Joint author）

    「糖質II糖タンパク質実験法」生物薬科学実験講座4卷・川嵜敏祐編・廣川書店  2011.7 

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    Language：Japanese Book type：Scholarly book

  • Remodeling of Sugar Chains by Endo-M, in: Endo, M., Hase, S., Yamamoto, K., and Takagaki, K. (Eds.),

    Fujita, K., and Yamamoto, K.（ Role： Joint author）

    Endoglycosidases: Biochemistry, Biotechnology, Application ・Kodansha  2006.1 

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    Language：English Book type：Scholarly book

MISC

  • Identification and Structural Basis of Novel Enzymes that Degrade Cell Wall Glycans of Mycobacteria Invited

    KASHIMA Toma, SHIMOKAWA Michiko, ISHIWATA Akihiro, FUJITA Kiyotaka, FUSHINOBU Shinya

    Nihon Kessho Gakkaishi   66 ( 3 )   171 - 172   2024.8

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    Language：Japanese   Publisher：The Crystallographic Society of Japan  

    DOI： 10.5940/jcrsj.66.171

  • Role of β-L-Arabinofuranosidases in Intestinal Bacteria Invited Reviewed

    Fujita Kiyotaka, Ishiwata Akihiro, Fushinobu Shinya

    Trends in Glycoscience and Glycotechnology   36 ( 210 )   E35 - E38   2024.3

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    Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)   Publisher：FCCA(Forum: Carbohydrates Coming of Age)  

    <p>β-L-Arabinofuranosidase (β-Ara<i>f</i>ase) is an enzyme belonging to the glycoside hydrolase families GH127/137/142/146 that hydrolyze β-L-arabinofuranoside (Ara<i>f</i>) from plant polysaccharides and glycoproteins. With the development of functional and structural analyses of β-Ara<i>f</i>ases from major human intestinal bacteria <i>Bifidobacterium longum</i> ssp. <i>longum</i> and <i>Bacteroides thetaiotaomicron</i>, the importance of β-Ara<i>f</i>ase to remove modified sugars has been revealed for the efficient degradation of dietary fibers by the intestinal bacteria. This minireview describes the distribution of β-Ara<i>f</i> in plant polysaccharides and glycoproteins and the findings revealed by functional and structural studies of β-Ara<i>f</i>ases from intestinal bacteria.</p>

    DOI： 10.4052/tigg.2306.1e

    Scopus

  • Role of β-L-Arabinofuranosidases in Intestinal Bacteria Invited Reviewed

    Fujita Kiyotaka, Ishiwata Akihiro, Fushinobu Shinya

    Trends in Glycoscience and Glycotechnology   36 ( 210 )   J35 - J38   2024.3

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    Authorship：Lead author,　Corresponding author   Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)   Publisher：FCCA(Forum: Carbohydrates Coming of Age)  

    <p>β-L-Arabinofuranosidase (β-Ara<i>f</i>ase) is an enzyme belonging to the glycoside hydrolase families GH127/137/142/146 that hydrolyze β-L-arabinofuranoside (Ara<i>f</i>) from plant polysaccharides and glycoproteins. With the development of functional and structural analyses of β-Ara<i>f</i>ases from major human intestinal bacteria <i>Bifidobacterium longum</i> ssp. <i>longum</i> and <i>Bacteroides thetaiotaomicron</i>, the importance of β-Ara<i>f</i>ase to remove modified sugars has been revealed for the efficient degradation of dietary fibers by the intestinal bacteria. This minireview describes the distribution of β-Ara<i>f</i> in plant polysaccharides and glycoproteins and the findings revealed by functional and structural studies of β-Ara<i>f</i>ases from intestinal bacteria.</p>

    DOI： 10.4052/tigg.2306.1j

    DOI： 10.4052/tigg.2306.1J

  • ビフィズス菌におけるアラビアガム分解代謝機構の解明

    佐々木 優紀, 北原 兼文, 藤田 清貴

    応用糖質科学   12 ( 2 )   108 - 116   2022.5

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    Language：Japanese   Publisher：(一社)日本応用糖質科学会  

    アラビアガムは、マメ科アカシア属の木から得られる滲出物であり、ヒトの腸内でビフィズス菌を増殖させるプレバイオティクスとしての機能がある。分子構造の大部分はII型アラビノガラクタン鎖で構成されており、側鎖に多様な修飾糖が付加することで複雑な構造を有している。ビフィズス菌によるカラマツ由来のII型AGの分解機構が明らかになったものの、これらの酵素群はアラビアガムには作用せず、ビフィズス菌の増殖機構は不明であった。筆者らはB.longumのアラビアガム資化性が菌株特異的であることに着目し、資化性試験と比較ゲノム解析によって、資化性菌にのみ共通して保存されている遺伝子クラスターを明らかにした。本遺伝子クラスターにコードされる3-O-α-D-ガラクトシル-α-L-アラビノフラノシダーゼ(GAfase)はアラビアガムの側鎖末端から二糖を遊離する新規の反応性を持つ鍵酵素であった。さらにGAfase作用後に、α1,4-Arafの分解を行いα-L-アラビノフラノシダーゼとエキソ-β-1,3-ガラクターゼが協調的に作用していることを見出し、B.longumにおけるアラビアガム分解代謝機構の全容を明らかにした。(著者抄録)

  • 腸内細菌によるアラビノガラクタン-プロテインの糖鎖分解に関わる酵素群の役割

    藤田清貴, 佐々木優紀, 北原兼文

    バイオサイエンスとインダストリー   80 ( 6 )   2022

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  • Identification and Structural Basis of an Enzyme Degrading Oligosaccharides in Caramel

    鹿島騰真, 石渡明弘, 藤田清貴, 伏信進矢

    生物物理(Web)   62 ( 3 )   2022

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  • ラクトフェリンのAsn-糖鎖のプレバイオティックス作用とビフィズス菌の糖取り込みと代謝

    藤田清貴

    ラクトフェリン2021   37 - 42   2021.9

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    Authorship：Lead author   Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • カラメル化糖に作用するビフィズス菌の新規exo-α-D-fructofuranosidaseの構造解析

    鹿島 騰真, 奥村 公喜, 荒川 孝俊, 山田 千早, 石渡 明弘, 伊藤 幸成, 藤田 清貴, 伏信 進矢

    応用糖質科学：日本応用糖質科学会誌   11 ( 2 )   105 - 106   2021.5

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    Language：Japanese   Publisher：一般社団法人 日本応用糖質科学会  

    DOI： 10.5458/bag.11.2_105

  • バイオミディア　食物繊維が育む"大人"のビフィズス菌

    藤田 清貴

    生物工学会誌   97 ( 12 )   736 - 736   2019.12

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    Publisher：(公社)日本生物工学会  

  • Degradation of plant arabinogalactan proteins by intestinal bacteria: characteristics and functions of the enzymes involved. Reviewed

    Fujita, K., Sasaki, Y., and Kitahara, K.

    Appl. Microbiol. Biotech.   103   7451 - 7457   2019

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    Language：English   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • ビフィズス菌が持つ糖タンパク質糖鎖の分解代謝システム：ビフィズス菌を増やすプレバイオティック糖タンパク質 Reviewed

    藤田清貴

    化学と生物   55 ( 4 )   242 - 248   2017.3

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • 糖タンパク質糖鎖の加水分解酵素に関する研究 Reviewed

    藤田清貴

    応用糖質科学   6 ( 1 )   30 - 36   2016.3

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)   Publisher：応用糖質科学  

  • Functional analysis of degradative enzymes for hydroxyproline-linked β-L-arabinofuranosides in Bifidobacterium longum. Reviewed

    Fujita, K., Kitahara, K., and Suganuma, T.

    Trends Glycosci. Glycotechnol.   24 ( 139 )   215 - 224   2012.9

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • ビフィズス菌由来β-L-アラビノビオシダーゼの機能解析 Reviewed

    藤田清貴、坂元志帆、小野祐樹、若尾雅広、隅田泰生、北原兼文、菅沼俊彦

    応用糖質科学   1 ( 2 )   153 - 158   2011.5

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • Functions of Novel Glycosidases Isolated from Bifidobacteria. Reviewed

    Katayama, T., Wada, J., Fujita, K., Kiyohara, M., Ashida, H., and Yamamoto, K.

    J. Appl. Glycosci.   55   101 - 109   2008.1

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    Language：English   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • さつまいも食物繊維の糖分析と食品素材化-南九州の未利用糖質資源の活用-

    菅沼俊彦、北原兼文、藤田清貴

    FFI Journal   213   699 - 707   2008

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • Some distinguishable properties between acid-stable and neutral types of α-amylases from acid-producing koji. Reviewed

    Suganuma, T., Fujita, K., and Kitahara, K

    J. Biosci. Bioeng.   104 ( 5 )   353 - 362   2007.10

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins.

    Katayama, T., Fujita, K., and Yamamoto, K.

    J. Biosci. Bioeng.   99   457 - 465   2005.1

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    Language：English   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • 微生物酵素を用いた糖タンパク質糖鎖の自由なモデリング

    藤田清貴，山本憲二

    化学と生物   41   244 - 249   2003

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

  • 糸状菌の糖鎖工学・糖鎖生物学

    山本憲二，青木一弘，牧村 裕，藤田清貴

    日本農芸化学会誌   77   42 - 44   2003

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    Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

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Presentations

  • 藤田清貴   結核菌細胞壁を構成するD-アラビナンの分解に関わる酵素群の機能解析   Invited

    第97回日本生化学会大会  2024.11 

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    Event date： 2024.11

    Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

  • Kiyotaka Fujita   Strategy of plant arabinogalactan-protein degradation by Bifidobacterium longum subsp. longum.   Invited International conference

    The 1st International Symposium on Bifidobacterium Research  2024.10 

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    Event date： 2024.10

    Language：English   Presentation type：Symposium, workshop panel (nominated)  

  • 藤田清貴   腸内細菌におけるカラメル化糖の資化戦略   Invited

    第13回応用糖質科学シンポジウム  2024.9 

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    Event date： 2024.9

    Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

  • 藤田清貴   成人型ビフィズス菌における植物糖タンパク質の分解戦略   Invited

    第96回日本生化学会大会  2023.11 

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    Event date： 2023.11

    Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

  • Fujita, K., Morikami, S., Fukushima, R., Kitahara, K., Tanaka, K., Ito, Y., Fushinobu, S., and Ishiwata, A.   A novel exo-β-D-arabinofuranosidase for the degradation of D-arabinan of Mycobacterial lipoarabinomannan   International conference

    26th International Symposium on Glycoconjugates (Glyco26)  2023.8 

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    Event date： 2023.8

    Language：English   Presentation type：Poster presentation  

  • 藤田清貴   ビフィズス菌における難消化性糖質の分解代謝機構の解明.   Invited

    令和4 年度日本農芸化学会西日本支部例会  2022.6 

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    Event date： 2022.6

    Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

  • Kiyotaka Fujita   D-arabinan degradative enzymes of Microbacterium arabinogalactanolyticum for the assimilation of mycobacterial lipoarabinomannan.   International conference

    Microbial Glycoconjugates and the GlySpace Alliance (MiGGA) Symposium  2022.3 

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    Event date： 2022.3

    Language：English   Presentation type：Symposium, workshop panel (nominated)  

  • 藤田清貴   結核菌細胞壁を構成するD-アラビナンの分解酵素群の発見.   Invited

    第18回糖鎖科学コンソーシアムシンポジウム  2021.12 

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    Event date： 2021.12

    Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

  • 藤田清貴   未知の糖質分解酵素探索とビフィズス菌の生存戦略の解明. 酵素が拓くSDGs への道.   Invited

    JBA“未来へのバイオ技術” 勉強会  2021.10 

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    Event date： 2021.10

    Language：Japanese   Presentation type：Symposium, workshop panel (public)  

  • 藤田清貴   成人型ビフィズス菌が持つ植物糖タンパク質糖鎖を資化するための分解酵素群.  

    ビフィズス菌研究会第１回シンポジウム  2021.3 

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    Event date： 2021.3

    Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

  • 藤田清貴   ラクトフェリンのAsn-糖鎖のプレバイオティックス作用とビフィズス菌の糖取り込みと代謝.   Invited

    日本ラクトフェリン学会第9回学術集会 

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    Event date： 2020.12

    Language：Japanese   Presentation type：Symposium, workshop panel (nominated)  

  • 佐々木 優紀、柳田真言、吉田圭祐、小田巻 俊孝、清水（肖） 金忠、北原 兼文、藤田清貴   アラビノガラクタンプロテインに対する成人型ビフィズス菌の二糖遊離酵素の機能解析.  

    日本応用糖質科学会2020年度大会 

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    Event date： 2020.9

    Language：English   Presentation type：Poster presentation  

  • 鹿島騰真、奥村公喜、荒川孝俊、山田千早、石渡明弘、伊藤幸成、藤田清貴、伏信進矢   カラメル化糖に作用するビフィズス菌の新規exo-α-D-fructofuranosidaseの構造解析   Invited

    日本応用糖質科学会2020年度大会 

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    Event date： 2020.9

    Language：Japanese   Presentation type：Poster presentation  

  • 77. 佐々木 優紀、内村 祐美、堀米 綾子、小田巻 俊孝、清水（肖） 金忠、北原 兼文、藤田清貴   アラビアガム資化性を持つビフィズス菌由来のGH36 α-D-galactosidaseの機能解析.  

    日本応用糖質科学会2019年度大会 

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    Event date： 2019.9

    Language：English   Presentation type：Oral presentation (general)  

  • 藤田清貴, 田中悠暉, 石渡明弘, 伊藤幸成, 隅田泰生, 北原兼文   Microbacterium arabinogalactanolyticum由来の組み換えendo-D-arabinaseの機能解析.  

    日本農芸化学会 2019年度大会 

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    Event date： 2019.3

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 佐々木 優紀、堀米 綾子、小田巻 俊孝、清水（肖）金忠、北原 兼文、藤田清貴   ビフィズス菌由来アラビアガム分解酵素3-O-α-D-galactosyl-α-L-arabinofuranosidaseの機能解析.  

    第25回日本生物工学会九州支部鹿児島大会 

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    Event date： 2018.12

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 藤田清貴,石渡明弘,伊藤幸成,若尾雅広,隅田泰生,北原兼文   Aureobacterium sp. M2由来の組み換えendo-D-arabinaseの機能解析.  

    第91回日本生化学会大会 

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    Event date： 2018.9

    Language：Japanese   Presentation type：Poster presentation  

  • 佐々木 優紀、堀米 綾子、小田巻 俊孝、清水（肖） 金忠、北原 兼文、藤田清貴   アラビアガム資化性ビフィズス菌由来Gal-α1,3-Ara/Arap-β1,3-Ara分解酵素の機能解析.  

    日本応用糖質科学会平成29年度大会 

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    Event date： 2018.9

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 藤田清貴   ビフィズス菌が持つ植物糖タンパク質糖鎖の分解代謝システム.   Invited

    セルラーゼ研究会　第32回大会 

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    Event date： 2018.7

    Language：Japanese   Presentation type：Oral presentation (invited, special)  

  • 佐々木 優紀、堀米 綾子、小田巻 俊孝、清水（肖） 金忠、北原 兼文、藤田清貴   Bifidobacterium longumにコードされたアラビアガム資化性の鍵を握る酵素の機能解析.  

    2018年度 乳酸菌学会 

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    Event date： 2018.7

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 佐々木 優紀、堀米 綾子、小田巻 俊孝、清水（肖） 金忠、北原 兼文、藤田清貴   ビフィズス菌のアラビアガム資化性の鍵を握る酵素endo-1,3-α-L-arabinofuranosidaseの機能解析  

    日本農芸化学会 2018年度大会 

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    Event date： 2018.3

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 藤田清貴、嵩下 愛果、東郷 奈未、福元 諒、角町 華子、佐々木 優紀、北原 兼文   Bifidobacterium adolescentisのアラビノガラクタン-プロテイン分解酵素群をコードする遺伝子クラスターの解析  

    日本農芸化学会 2018年度大会 

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    Event date： 2018.3

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 藤田清貴,石渡明弘,伊藤幸成,若尾雅広,隅田泰生,北原兼文   Lipoarabinomannanに作用する新規Ｄ－アラビナン分解酵素  

    第2回 抗酸菌研究会 

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    Event date： 2017.11

    Language：Japanese   Presentation type：Oral presentation (general)  

    Venue：国立感染症研究所戸山庁舎  

  • 藤田清貴   Bifidobacterium longum subsp. longumが持つ植物HRGP分解酵素群の役割.  

    第８回グライコバイオロジクス研究会 

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    Event date： 2017.11

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 佐々木優紀, 東郷奈未, 北原兼文, 藤田清貴   Bifidobacterium adolescentis由来の新規β-L-アラビノピラノシダーゼの機能解析  

    日本応用糖質科学会平成29年度大会 

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    Event date： 2017.9

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 澤井未視, 下川倫子, 石渡明弘, 伊藤幸成, 若尾雅広, 隅田泰生, 北原兼文, 藤田清貴   Aureobacterium sp. M2由来endo-D-arabinaseの基質特異性の解析.  

    日本応用糖質科学会平成29年度大会 

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    Event date： 2017.9

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 藤田清貴   ビフィズス菌が持つ植物糖タンパク質糖鎖分解酵素の役割   Invited

    第31回キチンキトサン学会大会 

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    Event date： 2017.8

    Language：Japanese   Presentation type：Oral presentation (invited, special)  

  • 藤田清貴、石渡明弘、伊藤幸成、北原兼文   Bifidobacterium longum subsp. longum由来のβ-L-アラビノフラノシダーゼの機能解析  

    第36回日本糖質学会年会 

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    Event date： 2017.7

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 藤田清貴、坂本 彩美、嵩下 愛果、東郷 奈未、北原兼文   Bifidobacterium longum subsp. longumのII型アラビノガラクタン分解酵素群の解析  

    日本農芸化学会 2017年度大会 

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    Event date： 2017.3

    Language：Japanese   Presentation type：Oral presentation (general)  

  • 藤田清貴、角町華子、石渡明弘、伊藤幸成、北原兼文   β-1,3-結合に作用するβ-L-アラビノフラノシダ―ゼの機能解析  

    日本応用糖質科学会平成28年度大会 

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    Event date： 2016.9

    Language：Japanese   Presentation type：Oral presentation (general)  

  • Fujita, K.   Characterization of a β-1,3 specific β-L-arabinofuranosidases from subsp.Bifidobacterium longum subsp. longum   International conference

    International Carbohydrate Symposium 2016 

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    Event date： 2016.7

    Language：English   Presentation type：Poster presentation  

  • Fujita, K., Tsunomachi, H., Ishiwata, A., Ito, I., and Kitahara, K.   Characterization of novel β-L-arabinofuranosidases acting on HRGPs.   International conference

    10th Georgia Glycoscience Symposium / Plant Polysaccharide Workshop 2016 

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    Event date： 2016.7

    Language：English   Presentation type：Poster presentation  

  • 藤田清貴、福元諒、北原兼文   Bifidobacterium adolescentis由来のGH27 β-L-アラビノピラノシダーゼ／α-D-ガラクトピラノシダーゼの機能解析.  

    日本農芸化学会 2016年度大会  日本農芸化学会

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    Event date： 2016.3

    Language：Japanese   Presentation type：Poster presentation  

    Venue：札幌  

  • Fujita, K., Tsunomachi, H., and Kitahara, K.   The mechanism by which the plant HRGPs have prebiotic effect on Bifidobacterium longum.   International conference

    Food for Health International Conference (FOHIC2016) 

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    Event date： 2016.3

    Language：English   Presentation type：Oral presentation (general)  

    Venue：Kagoshima, Japan  

  • 藤田清貴   ビフィズス菌由来の植物糖タンパク質糖鎖分解酵素群の機能解析.  

    応用糖質九州支部 第18回特別講演会  日本応用糖質科学会九州支部

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    Event date： 2016.3

    Language：English   Presentation type：Oral presentation (invited, special)  

    Venue：鹿児島  

  • 58. 澤井未視、下川倫子、石渡明弘、伊藤幸成、若尾雅広、隅田泰生、北原兼文、藤田清貴   Aureobacterium sp. M2由来のエンド-D-アラビナーゼの精製と諸性質の解析  

    第67回日本生物工学会大会 

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    Event date： 2015.10

    Language：Japanese   Presentation type：Poster presentation  

    Venue：鹿児島  

  • 藤田清貴   糖タンパク質糖鎖の加水分解酵素に関する研究  

    日本応用糖質科学会平成27年度大会  日本応用糖質科学会平成27年度大会

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    Event date： 2015.9

    Language：Japanese  

    Venue：奈良  

    国内学会

  • 藤田清貴、亀山恭平、下川倫子、伏信進矢、石渡明弘、Sophon Kaeothip、伊藤幸成、北原兼文   βーアラビノオリゴ糖鎖に作用するβ-L-アラビノフラノシダーゼの機能解析  

    第34回日本糖質学会年会  第34回日本糖質学会年会

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    Event date： 2015.8

    Language：Japanese  

    Venue：東京  

    国内学会

  • 藤田清貴、坂本彩美、下川倫子、金子 哲、北原兼文   HRGPの分解に関与するBifidobacterium longum由来α-L-アラビノフラノシダーゼの機能解析  

    日本農芸化学会 2015年度大会  日本農芸化学会 2015年度大会

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    Event date： 2015.3

    Language：Japanese  

    Venue：岡山  

    国内学会

  • 坂本彩美、下川倫子、小竹敬久、円谷陽一、北原兼文、藤田清貴   Bifidobacterium longum由来のβ-1,6-ガラクタン側鎖分解酵素群の機能解析  

    日本応用糖質科学会平成26年度大会  日本応用糖質科学会平成26年度大会

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    Event date： 2014.9

    Language：Japanese  

    Venue：新潟  

    国内学会

  • 藤田清貴、川原由義、下川倫子、伏信進矢、石渡明弘、Sophon Kaeothip、伊藤幸成、北原兼文   Bifidobacterium longumにコードされたβ-L-アラビノフラノシダーゼホモログの機能解析  

    日本応用糖質科学会平成26年度大会  日本応用糖質科学会平成26年度大会

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    Event date： 2014.9

    Language：Japanese  

    Venue：新潟  

    国内学会

  • 藤田清貴、坂本彩美、下川倫子、北原兼文   Bifidobacterium longumのⅡ型アラビノガラクタン分解代謝経路の解析  

    第３3回日本糖質学会年会  第３3回日本糖質学会年会

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    Event date： 2014.8

    Language：Japanese  

    Venue：名古屋  

    国内学会

  • 伊藤 佑、齋川 匡、Seonah Kim、藤田 清貴、石渡 明弘、Sophon Kaeothip、荒川 孝俊、若木 高善、Gregg T. Beckham、伊藤 幸成、伏信 進矢   ビフィズス菌由来GH127 β-L-アラビノフラノシダ―ゼの新規な活性中心  

    日本農芸化学会 2014年度大会  日本農芸化学会 2014年度大会

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    Event date： 2014.3

    Language：Japanese  

    Venue：東京  

    国内学会

  • 藤田清貴、吉嶺良平、下川倫子、北原兼文   Bifidobacterium longumにおけるβ-アラビノオリゴ糖鎖分解酵素群の転写解析  

    日本農芸化学会 2014年度大会  日本農芸化学会 2014年度大会

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    Event date： 2014.3

    Language：Japanese  

    Venue：東京  

    国内学会

  • 坂本彩美、坂口武則、下川倫子、藤田清貴、北原兼文、菅沼俊彦   Bifidobacterium longum由来のエンド-β-1,6-ガラクタナーゼの機能解析  

    日本応用糖質科学会平成25年度大会  日本応用糖質科学会平成25年度大会

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    Event date： 2013.9

    Language：Japanese  

    Venue：鹿児島  

    国内学会

  • 下川倫子、藤田清貴、北原兼文、菅沼俊彦   Bifidobacterium longum由来のβ-L-アラビノピラノシダーゼの機能解析  

    日本応用糖質科学会平成25年度大会  日本応用糖質科学会平成25年度大会

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    Event date： 2013.9

    Language：Japanese  

    Venue：鹿児島  

    国内学会

  • 藤田清貴、坂本彩美、坂口武則、下川倫子、北原兼文   ビフィズス菌由来のⅡ型アラビノガラクタン分解酵素群の機能解析  

    第３２回日本糖質学会年会  第３２回日本糖質学会年会

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    Event date： 2013.8

    Language：Japanese  

    Venue：大阪  

    国内学会

  • 藤田清貴、坂口武則、北原兼文、菅沼俊彦   Bifidobacterium longum由来のエキソ-β-1,3-ガラクタナーゼの機能解析  

    日本農芸化学会 2013年度大会  日本農芸化学会 2013年度大会

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    Event date： 2013.3

    Language：Japanese  

    Venue：仙台  

    国内学会

  • 藤田清貴   ビフィズス菌が生産する植物糖タンパク質糖鎖分解酵素群の解析  

    第2回新潟大学国際糖質科学シンポジウム  第2回新潟大学国際糖質科学シンポジウム

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    Event date： 2012.11

    Language：Japanese  

    Venue：新潟  

    その他

  • 藤田清貴   ビフィズス菌が持つ植物糖タンパク質糖鎖分解酵素  

    第36回 蛋白質と酵素の構造と機能に関する九州シンポジウム  第36回 蛋白質と酵素の構造と機能に関する九州シンポジウム

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    Event date： 2012.9

    Language：Japanese  

    Venue：宮崎  

    その他

  • 藤田清貴、奥山千代美、坂口武則、北原兼文、菅沼俊彦   Bifidobacterium longumのハイドロキシプロリンに富む糖タンパク質の分解メカニズムの解明  

    第16回腸内細菌腸内細菌学会  第16回腸内細菌腸内細菌学会

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    Event date： 2012.6

    Language：Japanese  

    Venue：兵庫  

    国内学会

  • 藤田清貴、奥山千代美、北原兼文、菅沼俊彦   β-アラビノオリゴ糖鎖のBifidobacterium longumに対する増殖促進効果  

    日本農芸化学会 2012年度大会  日本農芸化学会 2012年度大会

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    Event date： 2012.3

    Language：Japanese  

    Venue：京都  

    国内学会

  • 藤田清貴   ビフィズス菌が生産するβ-アラビノオリゴ糖鎖の分解酵素群の解析  

    日本農芸化学会西日本支部奨励賞講演会  日本農芸化学会西日本支部奨励賞講演会

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    Event date： 2012.1

    Language：Japanese  

    Venue：福岡  

    その他

  • 安川結野、中村正幸、藤田清貴、岩井 久   Xanthomonas campestris pv. campestris ATCC33913株由来β-L-アラビノフラノシダーゼのクローニングと機能解析  

    日本植物病理学会九州部会  日本植物病理学会九州部会

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    Event date： 2011.11

    Language：Japanese  

    Venue：大分  

    国内学会

  • 藤田清貴、五反田孝平、大渕衣里子、北原兼文、菅沼俊彦   ビフィズス菌由来β-L-アラビノフラノシダーゼのGlu366残基の役割  

    平成２３年度日本農芸化学会西日本支部・中四国支部合同大会  平成２３年度日本農芸化学会西日本支部・中四国支部合同大会

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    Event date： 2011.9

    Language：Japanese  

    Venue：宮崎  

    国内学会

  • 藤田清貴、大渕衣里子、五反田孝平、北原兼文、菅沼俊彦   ビフィズス菌によるβ-アラビノオリゴ糖鎖の資化性と関連酵素群の解析  

    日本応用糖質科学会平成23年度大会  日本応用糖質科学会平成23年度大会

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    Event date： 2011.9

    Language：Japanese  

    Venue：札幌  

    国内学会

  • Fujita, K., Sakamoto, S., Takashi, Y., Ono, Y., Obuchi, E., Kitahara, K., and Suganuma, T.   Characterization of novel glycosidases involved in the degradation of Hyp-linked oligoarabinosides.   International conference

    9th Carbohydrate Bioengineering Meeting (CBM9)  9th Carbohydrate Bioengineering Meeting (CBM9)

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    Event date： 2011.5

    Language：English  

    Venue： Portugal  

    国際学会

  • 藤田清貴   ビフィズス菌によるβ-アラビノオリゴ糖鎖の分解と代謝  

    日本農芸化学会  日本農芸化学会

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    Event date： 2011.3

    Language：Japanese  

    Venue：京都  

    国内学会

  • 藤田清貴、坂元志帆、高 由香里、小野祐樹、大渕衣里子、北原兼文、菅沼俊彦   β-アラビノオリゴ糖鎖の分解に関わる新規糖質分解酵素群の機能解析  

    日本生物工学会2010年度大会  日本生物工学会2010年度大会

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    Event date： 2010.10

    Language：Japanese  

    Venue：宮崎  

    国内学会

  • 藤田清貴、高 由香里、大渕衣里子、北原兼文、菅沼俊彦   ビフィズス菌由来新規β-L-アラビノフラノシダーゼのクローニングと機能解析  

    日本応用糖質科学会平成22年度大会  日本応用糖質科学会平成22年度大会

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    Event date： 2010.9

    Language：Japanese  

    Venue：静岡  

    国内学会

  • 藤田清貴、坂元志帆、高 由香里、小野祐樹、若尾雅広、隅田泰生、北原兼文、菅沼俊彦   ビフィズス菌由来β-L-アラビノビオシダーゼの機能解析  

    第17回糖質関連酵素化学シンポジウム  第17回糖質関連酵素化学シンポジウム

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    Event date： 2010.9

    Language：Japanese  

    Venue：静岡  

    国内学会

  • 藤田清貴、坂元志帆、高 由香里、若尾雅広、隅田泰生、北原兼文、菅沼俊彦   β-アラビノオリゴ糖鎖の分解に関わる新規β-L-アラビノビオシダーゼの機能解析  

    日本農芸化学会  日本農芸化学会

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    Event date： 2010.3

    Language：Japanese  

    Venue：東京  

    国内学会

  • 坂元志帆、藤田清貴、若尾雅広、隅田泰生、北原兼文、菅沼俊彦   β-1,2-L-アラビノビオースを遊離させる新規糖質分解酵素の機能解析  

    日本応用糖質科学会  日本応用糖質科学会

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    Event date： 2009.9

    Language：Japanese  

    Venue：青森  

    国内学会

  • 藤田清貴、坂元志帆、高 由香里、金子 哲、北原兼文、菅沼俊彦   ポテトレクチンの糖鎖部分に作用するGH43 α-L-arabinofuranosidaseの機能解析  

    日本応用糖質科学会  日本応用糖質科学会

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    Event date： 2009.9

    Language：Japanese  

    Venue：青森  

    国内学会

  • 中本 政勝,藤田清貴,北原兼文,菅沼俊彦   部位特異的変異導入による焼酎白麹菌由来中性α-amylase Leu232の機能解析  

    日本応用糖質科学会  日本応用糖質科学会

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    Event date： 2008.9

    Language：Japanese  

    Venue：沖縄  

    国内学会

  • 藤田清貴、坂元志帆、北原兼文、菅沼俊彦   Bifidobacterium longum由来の新規アラビナン分解酵素の機能解析  

    日本応用糖質科学会  日本応用糖質科学会

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    Event date： 2008.9

    Language：Japanese  

    Venue：沖縄  

    国内学会

  • 藤田清貴   ペクチンのビフィズス菌に対するプレバイオティクス効果とグリコシダーゼの関係  

    第7回KAGAWA機能糖鎖フォーラム  第7回KAGAWA機能糖鎖フォーラム

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    Event date： 2008.9

    Language：Japanese  

    Venue：香川  

    その他

  • 藤田清貴、北原兼文、菅沼俊彦、山本憲二、竹川薫   部位特異的変異導入によるendo-β-N-acetylglucosaminidase A(Endo-A)の糖転移効率の向上  

    日本糖質学会  日本糖質学会

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    Event date： 2008.8

    Language：Japanese  

    Venue：茨城  

    国内学会

  • 梅川碧里、藤田清貴、Wei Huang、Lai-Xi Wang、芦田久、山本憲二   Mucor hiemalis 由来 endo-β-N-acetylglucosaminidase (Endo-M)の糖転移機能の改変とその反応解析   International conference

    日本応用糖質科学会 2007年度大会  日本応用糖質科学会 2007年度大会

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    Event date： 2007.8

    Language：English  

    Venue：神奈川  

    国際学会

  • 梅川碧里、藤田清貴、Wei Huang、加藤紀彦、芦田久、Lai-Xi Wang、山本憲二   Mucor hiemalis 由来 endo-β-N-acetylglucosaminidase (Endo-M) が有する特異な糖転移機能の改変及び解析  

    日本農芸化学会関西支部 第449回 講演会  日本農芸化学会関西支部 第449回 講演会

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    Event date： 2007.5

    Language：Japanese  

    Venue：京都  

    国内学会

  • 梅川碧里、藤田清貴、加藤紀彦、芦田久、山本憲二   Mucor hiemallis 由来 Endo-β-N-acetylglucosaminidase (Endo-M) の糖転移機能の改変  

    日本農芸化学会 2007 年度大会  日本農芸化学会 2007 年度大会

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    Event date： 2007.3

    Language：Japanese  

    Venue：東京  

    国内学会

  • 中本 政勝、藤田 清貴、北原 兼文、菅沼 俊彦   焼酎麹由来耐酸性α-アミラーゼの酵母での発現と機能解析  

    日本生物工学会九州支部大会（第13回）  日本生物工学会九州支部大会（第13回）

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    Event date： 2006.12

    Language：Japanese  

    Venue：鹿児島  

    国内学会

  • 梅川碧里、藤田清貴、加藤紀彦、芦田久、山本憲二   Mucor hiemalis由来エンド-β-N-アセチルグルコサミニダーゼ(Endo-M)の大腸菌における発現  

    日本応用糖質科学会平成 18 年度大会  日本応用糖質科学会平成 18 年度大会

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    Event date： 2006.9

    Language：Japanese  

    Venue：大阪  

    国内学会

  • Fujita, K., Oura F., Nagamine N., Hiratake J., Ozawa H., Yamaguchi M., Katayama T., and Yamamoto K.   Identification and Molecular Cloning of a Novel Endo-α- N-acetylgalactosaminidase from Bifidobacterium longum.   International conference

    20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress.  20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress.

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    Event date： 2006.6

    Language：English  

    Venue：京都  

    国際学会

  • 藤田 清貴、瀬口 智恵、北原 兼文、菅沼 俊彦   各種変異酵素を用いた焼酎麹耐酸性α-アミラーゼの機能解析  

    日本農芸化学会  日本農芸化学会

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    Event date： 2006.3

    Language：Japanese  

    Venue：京都  

    国内学会

  • 藤田 清貴、佐藤 玲子、戸澗 一孔、片山 高嶺、竹川 薫、山本 憲二   Chemical rescueを用いたendo-b-N-acetylglucosaminidase Aの触媒残基の同定.  

    日本糖質学会年会  日本糖質学会年会

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    Event date： 2005.7

    Language：Japanese  

    Venue：大津  

    国内学会

  • 藤田 清貴、枇榔 誠、北原 兼文、菅沼 俊彦   焼酎麹α-アミラーゼのPichia pastorisでの発現と耐酸性の解析.  

    日本農芸化学会  日本農芸化学会

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    Event date： 2005.3

    Language：Japanese  

    Venue：札幌  

    国内学会

  • 久保 留理子、藤田 清貴、北原 兼文、菅沼 俊彦   組換えペクチン分解酵素系を用いたサツマイモデンプン粕の分解様式  

    日本農芸化学会 2005年度大会  日本農芸化学会 2005年度大会

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    Event date： 2005.3

    Language：Japanese  

    Venue：北海道  

    国内学会

  • 鹿島 騰真, 奥村 公喜, 荒川 孝俊, 山田 千早, 石渡 明弘, 伊藤 幸成, 藤田 清貴, 伏信 進矢   カラメル化糖に作用するビフィズス菌の新規exo-α-D-fructofuranosidaseの構造解析  

    応用糖質科学  2020.11  (一社)日本応用糖質科学会

  • 佐々木 優紀, 柳田 真言, 吉田 圭祐, 小田巻 俊孝, 清水 金忠[肖], 北原 兼文, 藤田 清貴   アラビノガラクタンプロテインに対する成人型ビフィズス菌の二糖遊離酵素の機能解析  

    応用糖質科学  2020.11  (一社)日本応用糖質科学会

  • 澤野 孝太, 丸山 瞬, 荒川 孝俊, 中村 正幸, 石渡 明弘, 伊藤 幸成, 藤田 清貴, 伏信 進矢   Xanthomonas属細菌由来β-L-アラビノフラノシダーゼの結晶構造  

    生命科学系学会合同年次大会  2017.12  生命科学系学会合同年次大会運営事務局

  • 佐々木 優紀, 堀米 綾子, 小田巻 俊孝, 清水 金忠[肖], 北原 兼文, 藤田 清貴   Bifidobacterium longumにコードされたアラビアガム資化性の鍵を握る酵素の機能解析  

    日本乳酸菌学会誌  2018.7  日本乳酸菌学会

  • 藤田 清貴, 石渡 明弘, 伊藤 幸成, 若尾 雅広, 隅田 泰生, 北原 兼文   Aureobacterium sp.M2由来の組み換えendo-D-arabinaseの機能解析  

    日本生化学会大会プログラム・講演要旨集  2018.9  (公社)日本生化学会

  • 藤田 清貴   糖鎖を介した微生物の生存戦略を探る　成人型ビフィズス菌における植物糖タンパク質の分解戦略  

    日本生化学会大会プログラム・講演要旨集  2023.10  (公社)日本生化学会

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    Language：Japanese  

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Intellectual Property

  • 糖質分解酵素、抗酸菌の検出キット及び抗酸菌の検出方法

    藤田 清貴

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    Applicant：国立大学法人 鹿児島大学

    Application no：特願2021-147456  Date applied：2021.9

    Announcement no：特開2023-040472  Date announced：2023.3

    J-GLOBAL

  • 糖質分解酵素、食品添加用細菌のスクリーニング方法、プレバイオティクスの評価方法及びプライマー対

    藤田 清貴, 石渡 明弘

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    Applicant：国立大学法人 鹿児島大学

    Application no：特願2020-055336  Date applied：2020.3

    Announcement no：特開2021-153433  Date announced：2021.10

    J-GLOBAL

  • 糖質分解酵素及びプレバイオティクスの評価方法

    藤田 清貴, 石渡 明弘

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    Applicant：国立大学法人 鹿児島大学

    Application no：特願2020-055336  Date applied：2020.3

    Announcement no：特開2021-153433  Date announced：2021.10

    Patent/Registration no：特許第7493751号  Date registered：2024.5 

    J-GLOBAL

  • 新規D−アラビナン分解酵素

    藤田 清貴, 隅田 泰生

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    Applicant：株式会社スディックスバイオテック

    Application no：特願2017-141706  Date applied：2017.7

    Announcement no：特開2019-017358  Date announced：2019.2

    Patent/Registration no：特許第7082262号  Date registered：2022.5  Date issued：2022.6

    J-GLOBAL

  • 新規アラビアガム資化性ビフィズス菌

    藤田 清貴, 小田巻 俊孝, 堀米 綾子

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    Applicant：国立大学法人 鹿児島大学, 森永乳業株式会社

    Application no：特願2017-138371  Date applied：2017.7

    Announcement no：特開2019-017292  Date announced：2019.2

    Patent/Registration no：特許第6972476号  Date registered：2021.11  Date issued：2021.11

    J-GLOBAL

Awards

  • 平成27年度日本応用糖質科学会奨励賞

    2015.9   日本応用糖質科学会   糖タンパク質糖鎖の加水分解酵素に関する研究

    藤田 清貴

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    Country：Japan

  • 2012年度食創会 第17回 安藤百福賞 発明発見奨励賞

    2013.3   安藤スポーツ・食文化振興財団   植物糖タンパク質糖鎖が有するビフィズス菌増殖促進効果の発見

    藤田 清貴

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    Country：Japan

  • 平成23年度日本農芸化学会西日本支部奨励賞（一般）

    2012.1   日本農芸化学会西日本支部   ビフィズス菌が生産するβーアラビノオリゴ糖鎖の分解酵素群の解析

    藤田 清貴

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    Country：Japan

Research Projects

  • Prebiotic effects of caramelized sugars based on the degradation mechanism of intestinal bacteria

    Grant number：24K01704  2024.4 - 2028.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

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    Grant amount：\18590000 （ Direct Cost: \14300000 、 Indirect Cost：\4290000 ）

  • Molecular analysis of mirror-arabinan present in cell wall polysaccharides of Mycobacteria and its degrading enzymes

    Grant number：19H00929  2019.4 - 2023.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (A)  Grant-in-Aid for Scientific Research (A)

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    Grant amount：\45240000 （ Direct Cost: \34800000 、 Indirect Cost：\10440000 ）

  • 新規アラビノビオース遊離酵素により解き明かすビフィズス菌のAGP分解メカニズム

    2019.4 - 2022.3

    科学研究費補助金  基盤研究(C)

  • Structure-function analysis and study on reaction mechanism of microbial cysteine glycosidases

    Grant number：15H02443  2015.4 - 2019.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (A)  Grant-in-Aid for Scientific Research (A)

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    Grant amount：\42120000 （ Direct Cost: \32400000 、 Indirect Cost：\9720000 ）

  • 植物糖タンパク質糖鎖分解酵素群の解析から明らかにするビフィズス菌間の共生関係

    2015.4 - 2018.3

    科学研究費補助金  基盤研究(C)

  • Symbiosis between bifidobacterial species by the analysis of the degradative enzymes for plant glycoprotein

    Grant number：15K07397  2015.4 - 2018.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)  Grant-in-Aid for Scientific Research (C)

    FUJITA Kiyotaka

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    Grant amount：\5070000 （ Direct Cost: \3900000 、 Indirect Cost：\1170000 ）

    L-Arabinose is a widely occurring sugar in plant cell wall polysaccharides and proteoglycans such as arabinan, arabinoxylan, arabinogalactan protein (AGP), and extensin. Bifidobacterium adolescentis encodes a gene cluster for L-arabinose degradative enzymes. In this study, we cloned and characterized GH27 β-L-arabinopyranosidase (BAD_1525), GH51 α-L-arabinofuranosidase (BAD_1524), GH43 α-L-arabinofuranosidase (BAD_1527), GH36 β-L-arabinopyranosidase (BAD_1528), and GH127β-L-arabinofuranosidase (BAD_1529) from B. adolescentis JCM1275.

  • Structural and functional analysis of glycosidases from plants that have a novel active center

    Grant number：26660083  2014.4 - 2018.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Exploratory Research  Grant-in-Aid for Challenging Exploratory Research

    Fushinobu Shinya, FUJITA Kiyotaka, ISHIWATA Akihiro, ITO Yukishige, Beckham Gregg T.

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    Grant amount：\3900000 （ Direct Cost: \3000000 、 Indirect Cost：\900000 ）

    We initially aimed to study the structure and function of uncharacterized enzyme from plants that belong to DUF1680. Although we examined heterologous expression of the genes from Arabidopsis thaliana and Oryza sativa under various conditions, they did not express or expressed as insoluble aggregates. We determined a novel crystal structure of a GH146 β-L-arabinofuranosidase from plant pathogen, Xanthomonas. The active site of the Xanthomonas enzyme was cysteine, like the case of GH127 enzyme (HypBA1), and the enzyme had a novel carbohydrate-binding module domain.

  • ビフィズス菌のL-アラビノース含有オリゴ糖の分解に関わる菌体内酵素群の解析

    2013.4 - 2017.3

    その他機関  競争的研究資金 

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    Grant type：Competitive

    ビフィズス菌のL-アラビノース含有オリゴ糖の分解に関わる菌体内酵素群の解析

  • ビフィズス菌のアラビノガラクタンープロテイン代謝機構に関わる糖質分解酵素群の解析

    2012.4 - 2015.3

    科学研究費補助金  基盤研究(C)

  • ビフィズス菌におけるL-アラビノースの輸送体と代謝酵素の同定

    2012.4 - 2014.3

    その他機関  競争的研究資金 

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    Grant type：Competitive

    ビフィズス菌におけるL-アラビノースの輸送体と代謝酵素の同定

  • 大豆食品廃棄物のビフィズス菌増殖促進効果の検証

    2011.4 - 2012.3

    その他機関  競争的研究資金 

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    Grant type：Competitive

    大豆食品廃棄物のビフィズス菌増殖促進効果の検証

  • ビフィズス菌のβーアラビノオリゴ糖鎖代謝機構に関わる糖質分解酵素群の解析

    2010.4 - 2012.3

    科学研究費補助金  若手研究(B)

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