Updated on 2026/03/15

写真a

 
NAKAI Hiroyuki
 
Organization
Academic Assembly Institute of Science and Technology NOUGAKU KEIRETSU Associate Professor
Faculty of Agriculture Department of Agriculture Associate Professor
Title
Associate Professor
External link

Degree

  • 博士（農学） ( 2005.3   北海道大学 )

Research Interests

  • 物質生産

  • 酵素化学

  • 糖質科学

Research Areas

  • Life Science / Applied biochemistry

  • Life Science / Food sciences

Research History (researchmap)

  • Niigata University   Faculty of Agriculture Department of Applied Biological Chemistry   Associate Professor

    2015.4

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  • Niigata University   Graduate School of Science and Technology   Assistant Professor

    2010.12 - 2015.3

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  • National Agriculture and Food Research Organization, National Food Research Institute

    2010.10 - 2010.11

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  • デンマーク工科大学   助教

    2008.9 - 2010.9

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  • デンマーク工科大学   博士研究員

    2007.9 - 2008.8

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  • Hokkaido University

    2005.4 - 2007.9

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Research History

  • Niigata University   Faculty of Agriculture Department of Agriculture   Associate Professor

    2017.4

  • Niigata University   Graduate School of Science and Technology Life and Food Sciences Applied Life and Food Sciences   Associate Professor

    2015.4 - 2017.3

  • Niigata University   Faculty of Agriculture Department of Applied Biological Chemistry   Associate Professor

    2015.4 - 2017.3

  • Niigata University   Headquarters for Strategy and Planning Office for Promoting the Cultivation of Young Researchers   Assistant Professor

    2010.12 - 2015.3

Education

  • Hokkaido University   Graduate School, Division of Agriculture   応用生命科学専攻

    - 2005.3

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    Country： Japan

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  • Hokkaido University   Faculty of Agriculture   応用生命科学科

    - 2000.3

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    Country： Japan

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Professional Memberships

  • THE JAPANESE SOCIETY OF CARBOHYDRATE RESEARCH

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  • THE JAPANESE SOCIETY OF APPLIED GLYCOSCIENCE

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  • JAPAN SOCIETY FOR BIOSCIENCE, BIOTECHNOLOGY, AND AGROCHEMISTRY

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Papers

  • Discovery of Anomer-inverting Transglycosylation from the Diversified Reaction Mechanisms of GH186

    Motouchi Sei, Komba Shiro, Kobayashi Kaito, Nakai Hiroyuki, Nakajima Masahiro

    Bulletin of Applied Glycoscience   15 ( 2 )   70 - 78   2025.5

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    Language：Japanese   Publisher：The Japanese Society of Applied Glycoscience  

    DOI： 10.5458/bag.15.2_70

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    Other Link： https://ndlsearch.ndl.go.jp/books/R000000004-I034213233

  • Discovery of Anomer-Inverting Transglycosylase: Cyclic Glucohexadecaose-Producing Enzyme from Xanthomonas, a Phytopathogen. Reviewed International journal

    Sei Motouchi, Shiro Komba, Hiroyuki Nakai, Masahiro Nakajima

    Journal of the American Chemical Society   146 ( 26 )   17738 - 17746   2024.7

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

    Various Xanthomonas species cause well-known plant diseases. Among various pathogenic factors, the role of α-1,6-cyclized β-1,2-glucohexadecaose (CβG16α) produced by Xanthomonas campestris pv. campestris was previously shown to be vital for infecting model organisms, Arabidopsis thaliana and Nicotiana benthamiana. However, enzymes responsible for biosynthesizing CβG16α are essentially unknown, which limits the generation of agrichemicals that inhibit CβG16α synthesis. In this study, we discovered that OpgD from X. campestris pv. campestris converts linear β-1,2-glucan to CβG16α. Structural and functional analyses revealed OpgD from X. campestris pv. campestris possesses an anomer-inverting transglycosylation mechanism, which is unprecedented among glycoside hydrolase family enzymes.

    DOI： 10.1021/jacs.4c02579

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  • Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans Reviewed

    Meng-Shu Hao, Scott Mazurkewich, He Li, Alma Kvammen, Srijani Saha, Salla Koskela, Annie R. Inman, Masahiro Nakajima, Nobukiyo Tanaka, Hiroyuki Nakai, Gisela Brändén, Vincent Bulone, Johan Larsbrink, Lauren S. McKee

    Nature Communications   15 ( 1 )   2024.4

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    Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    Abstract

    Carbohydrate-binding modules (CBMs) are non-catalytic proteins found appended to carbohydrate-active enzymes. Soil and marine bacteria secrete such enzymes to scavenge nutrition, and they often use CBMs to improve reaction rates and retention of released sugars. Here we present a structural and functional analysis of the recently established CBM family 92. All proteins analysed bind preferentially to β−1,6-glucans. This contrasts with the diversity of predicted substrates among the enzymes attached to CBM92 domains. We present crystal structures for two proteins, and confirm by mutagenesis that tryptophan residues permit ligand binding at three distinct functional binding sites on each protein. Multivalent CBM families are uncommon, so the establishment and structural characterisation of CBM92 enriches the classification database and will facilitate functional prediction in future projects. We propose that CBM92 proteins may cross-link polysaccharides in nature, and might have use in novel strategies for enzyme immobilisation.

    DOI： 10.1038/s41467-024-47584-y

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    Other Link： https://www.nature.com/articles/s41467-024-47584-y

  • Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase Reviewed

    Nobukiyo Tanaka, Ryotaro Saito, Kaito Kobayashi, Hiroyuki Nakai, Shogo Kamo, Kouji Kuramochi, Hayao Taguchi, Masahiro Nakajima, Tomoko Masaike

    Applied Microbiology and Biotechnology   108 ( 1 )   2024.2

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    Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    Abstract

    Cyclic β-1,2-glucan synthase (CGS) is a key enzyme in production of cyclic β-1,2-glucans (CβGs) which are involved in bacterial infection or symbiosis to host organisms. Nevertheless, a mechanism of cyclization, the final step in the CGS reaction, has not been fully understood. Here we performed functional and structural analyses of the cyclization domain of CGS alone from Thermoanaerobacter italicus (TiCGS<sub>Cy</sub>). We first found that β-glucosidase-resistant compounds are produced by TiCGS<sub>Cy</sub> with linear β-1,2-glucans as substrates. The <sup>1</sup>H-NMR analysis revealed that these products are CβGs. Next, action pattern analyses using β-1,2-glucooligosaccharides revealed a unique reaction pattern: exclusive transglycosylation without hydrolysis and a hexasaccharide being the minimum length of the substrate. These analyses also showed that longer substrate β-1,2-glucooligosaccharides are preferred, being consistent with the fact that CGSs generally produce CβGs with degrees of polymerization of around 20. Finally, the overall structure of the cyclization domain of TiCGS<sub>Cy</sub> was found to be similar to those of β-1,2-glucanases in phylogenetically different groups. Meanwhile, the identified catalytic residues indicated clear differences in the reaction pathways between these enzymes. Overall, we propose a novel reaction mechanism of TiCGS<sub>Cy</sub>. Thus, the present group of CGSs defines a new glycoside hydrolase family, GH189.

    Key points

    • It was clearly evidenced that cyclization domain alone produces cyclic β-1,2-glucans.

    • The domain exclusively catalyzes transglycosylation without hydrolysis.

    • The present catalytic domain defines as a new glycoside hydrolase family 189.

    Graphical Abstract

    DOI： 10.1007/s00253-024-13013-9

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    Other Link： https://link.springer.com/article/10.1007/s00253-024-13013-9/fulltext.html

  • Efficient Synthesis of β-Glucose 1-Phosphate through Enzymatic Phosphorolysis and Baker's Yeast Fermentation.

    Sofia Koltovskaia, Akane Ohtao, Motomitsu Kitaoka, Hiroyuki Nakai, Takanori Nihira

    Journal of applied glycoscience   71 ( 4 )   123 - 125   2024

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

    β-Glucose 1-phosphate (βGlc1P) is a donor substrate in the synthesis of various α-glucosides by glycoside phosphorylases belonging to the glycoside hydrolase family 65. This study presents an efficient synthesis of βGlc1P combining enzymatic phosphorolysis of inexpensive maltose and baker's yeast fermentation to bias the equilibrium toward maltose phosphorolysis by removing released glucose. Mass production of βGlc1P was obtained in a 2 L reaction mixture initially containing 500 mM maltose and inorganic phosphate, with a yield of 76 %. βGlc1P was isolated from the reaction mixture by crystallization after electrodialysis to obtain 181 g of βGlc1P as a bis(cyclohexylammonium) salt.

    DOI： 10.5458/jag.jag.JAG-2024_0008

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  • Identification of enzymatic functions of osmo-regulated periplasmic glucan biosynthesis proteins from Escherichia coli reveals a novel glycoside hydrolase family Reviewed

    Sei Motouchi, Kaito Kobayashi, Hiroyuki Nakai, Masahiro Nakajima

    Communications Biology   6 ( 1 )   2023.9

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    Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    Abstract

    Most Gram-negative bacteria synthesize osmo-regulated periplasmic glucans (OPG) in the periplasm or extracellular space. Pathogenicity of many pathogens is lost by knocking out opgG, an OPG-related gene indispensable for OPG synthesis. However, the biochemical functions of OpgG and OpgD, a paralog of OpgG, have not been elucidated. In this study, structural and functional analyses of OpgG and OpgD from Escherichia coli revealed that these proteins are β-1,2-glucanases with remarkably different activity from each other, establishing a new glycoside hydrolase family, GH186. Furthermore, a reaction mechanism with an unprecedentedly long proton transfer pathway among glycoside hydrolase families is proposed for OpgD. The conformation of the region that forms the reaction pathway differs noticeably between OpgG and OpgD, which explains the observed low activity of OpgG. The findings enhance our understanding of OPG biosynthesis and provide insights into functional diversity for this novel enzyme family.

    DOI： 10.1038/s42003-023-05336-6

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    Other Link： https://www.nature.com/articles/s42003-023-05336-6

  • Cleavage of α-1,4-glycosidic linkages by the glycosylphosphatidylinositol-anchored α-amylase AgtA decreases the molecular weight of cell wall α-1,3-glucan in Aspergillus oryzae Reviewed

    Ami Koizumi, Ken Miyazawa, Makoto Ogata, Yuzuru Takahashi, Shigekazu Yano, Akira Yoshimi, Motoaki Sano, Masafumi Hidaka, Takanori Nihira, Hiroyuki Nakai, Satoshi Kimura, Tadahisa Iwata, Keietsu Abe

    Frontiers in Fungal Biology   3   Article 1061841   2023.1

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    Aspergillus fungi contain α-1,3-glucan with a low proportion of α-1,4-glucan as a major cell wall polysaccharide. Glycosylphosphatidylinositol (GPI)-anchored α-amylases are conserved in Aspergillus fungi. The GPI-anchored α-amylase AmyD in Aspergillus nidulans has been reported to directly suppress the biosynthesis of cell wall α-1,3-glucan but not to degrade it in vivo. However, the detailed mechanism of cell wall α-1,3-glucan biosynthesis regulation by AmyD remains unclear. Here we focused on AoAgtA, which is encoded by the Aspergillus oryzae agtA gene, an ortholog of the A. nidulans amyD gene. Similar to findings in A. nidulans, agtA overexpression in A. oryzae grown in submerged culture decreased the amount of cell wall α-1,3-glucan and led to the formation of smaller hyphal pellets in comparison with the wild-type strain. We analyzed the enzymatic properties of recombinant (r)AoAgtA produced in Pichia pastoris and found that it degraded soluble starch, but not linear bacterial α-1,3-glucan. Furthermore, rAoAgtA cleaved 3-α-maltotetraosylglucose with a structure similar to the predicted boundary structure between the α-1,3-glucan main chain and a short spacer composed of α-1,4-linked glucose residues in cell wall α-1,3-glucan. Interestingly, rAoAgtA randomly cleaved only the α-1,4-glycosidic bonds of 3-α-maltotetraosylglucose, indicating that AoAgtA may cleave the spacer in cell wall α-1,3-glucan. Consistent with this hypothesis, heterologous overexpression of agtA in A. nidulans decreased the molecular weight of cell wall α-1,3-glucan. These in vitro and in vivo properties of AoAgtA suggest that GPI-anchored α-amylases can degrade the spacer α-1,4-glycosidic linkages in cell wall α-1,3-glucan before its insolubilization, and this spacer cleavage decreases the molecular weight of cell wall α-1,3-glucan in vivo.

    DOI： 10.3389/ffunb.2022.1061841

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  • Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages Reviewed

    Kaito Kobayashi, Hisaka Shimizu, Nobukiyo Tanaka, Kouji Kuramochi, Hiroyuki Nakai, Masahiro Nakajima, Hayao Taguchi

    Journal of Biological Chemistry   298 ( 3 )   101606 - 101606   2022.3

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    Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

    DOI： 10.1016/j.jbc.2022.101606

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  • Discovery of solabiose phosphorylase and its application for enzymatic synthesis of solabiose from sucrose and lactose Reviewed

    Wataru Saburi, Takanori Nihira, Hiroyuki Nakai, Motomitsu Kitaoka, Haruhide Mori

    Scientific Reports   12 ( 1 )   259   2022.1

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    Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

    <title>Abstract</title>Glycoside phosphorylases (GPs), which catalyze the reversible phosphorolysis of glycosides, are promising enzymes for the efficient production of glycosides. Various GPs with new catalytic activities are discovered from uncharacterized proteins phylogenetically distant from known enzymes in the past decade. In this study, we characterized <italic>Paenibacillus borealis</italic> PBOR_28850 protein, belonging to glycoside hydrolase family 94. Screening of acceptor substrates for reverse phosphorolysis, in which α-<sc>d</sc>-glucose 1-phosphate was used as the donor substrate, revealed that the recombinant PBOR_28850 produced in <italic>Escherichia coli</italic> specifically utilized <sc>d</sc>-galactose as an acceptor and produced solabiose (β-<sc>d</sc>-Glc<italic>p</italic>-(1 → 3)-<sc>d</sc>-Gal). This indicates that PBOR_28850 is a new GP, solabiose phosphorylase. PBOR_28850 catalyzed the phosphorolysis and synthesis of solabiose through a sequential bi-bi mechanism involving the formation of a ternary complex. The production of solabiose from lactose and sucrose has been established. Lactose was hydrolyzed to <sc>d</sc>-galactose and <sc>d</sc>-glucose by β-galactosidase. Phosphorolysis of sucrose and synthesis of solabiose were then coupled by adding sucrose, sucrose phosphorylase, and PBOR_28850 to the reaction mixture. Using 210 mmol lactose and 280 mmol sucrose, 207 mmol of solabiose was produced. Yeast treatment degraded the remaining monosaccharides and sucrose without reducing solabiose. Solabiose with a purity of 93.7% was obtained without any chromatographic procedures.

    DOI： 10.1038/s41598-021-04421-2

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    Other Link： https://www.nature.com/articles/s41598-021-04421-2

  • Enzymatic control and evaluation of degrees of polymerization of β-(1→2)-glucans Reviewed

    Masahiro Nakajima, Nobukiyo Tanaka, Kaito Kobayashi, Hiroyuki Nakai, Satoshi Kimura, Tadahisa Iwata, Hayao Taguchi

    Analytical Biochemistry   632   114366 - 114366   2021.11

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    Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

    DOI： 10.1016/j.ab.2021.114366

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  • Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases. Reviewed International journal

    Shuntaro Nakamura, Takanori Nihira, Rikuya Kurata, Hiroyuki Nakai, Kazumi Funane, Enoch Y Park, Takatsugu Miyazaki

    The Journal of biological chemistry   297 ( 6 )   101366 - 101366   2021.10

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    Glycoside hydrolase family 65 (GH65) comprises glycoside hydrolases (GHs) and glycoside phosphorylases (GPs) that act on α-glucosidic linkages in oligosaccharides. All previously reported bacterial GH65 enzymes are GPs, whereas all eukaryotic GH65 enzymes known are GHs. In addition, to date, no crystal structure of a GH65 GH has yet been reported. In this study, we use biochemical experiments and X-ray crystallography to examine the function and structure of a GH65 enzyme from Flavobacterium johnsoniae (FjGH65A) that shows low amino acid sequence homology to reported GH65 enzymes. We found that FjGH65A does not exhibit phosphorolytic activity, but it does hydrolyze kojibiose (α-1,2-glucobiose) and oligosaccharides containing a kojibiosyl moiety without requiring inorganic phosphate. In addition, stereochemical analysis demonstrated that FjGH65A catalyzes this hydrolytic reaction via an anomer-inverting mechanism. The three-dimensional structures of FjGH65A in native form and in complex with glucose were determined at resolutions of 1.54 and 1.40 Å resolutions, respectively. The overall structure of FjGH65A resembled those of other GH65 GPs, and the general acid catalyst Glu472 was conserved. However, the amino acid sequence forming the phosphate-binding site typical of GH65 GPs was not conserved in FjGH65A. Moreover, FjGH65A had the general base catalyst Glu616 instead, which is required to activate a nucleophilic water molecule. These results indicate that FjGH65A is an α-1,2-glucosidase and is the first bacterial GH found in the GH65 family.

    DOI： 10.1016/j.jbc.2021.101366

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  • Next-generation prebiotic promotes selective growth of bifidobacteria, suppressing Clostridioides difficile Reviewed International journal

    Rika Hirano, Mikiyasu Sakanaka, Kazuto Yoshimi, Naohisa Sugimoto, Syogo Eguchi, Yuko Yamauchi, Misaki Nara, Shingo Maeda, Yuta Ami, Aina Gotoh, Takane Katayama, Noriho Iida, Tamotsu Kato, Hiroshi Ohno, Satoru Fukiya, Atsushi Yokota, Mamoru Nishimoto, Motomitsu Kitaoka, Hiroyuki Nakai, Shin Kurihara

    Gut Microbes   13 ( 1 )   1973835 - 1973835   2021.1

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    Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Informa UK Limited  

    Certain existing prebiotics meant to facilitate the growth of beneficial bacteria in the intestine also promote the growth of other prominent bacteria. Therefore, the growth-promoting effects of β-galactosides on intestinal bacteria were analyzed. Galactosyl-β1,4-l-rhamnose (Gal-β1,4-Rha) selectively promoted the growth of Bifidobacterium. Bifidobacterium longum subsp. longum 105-A (JCM 31944) has multiple solute-binding proteins belonging to ATP-binding cassette transporters for sugars. Each strain in the library of 11 B. longum subsp. longum mutants, in which each gene of the solute-binding protein was disrupted, was cultured in a medium containing Gal-β1,4-Rha as the sole carbon source, and only the BL105A_0502 gene-disruption mutant showed delayed and reduced growth compared to the wild-type strain. BL105A_0502 homolog is highly conserved in bifidobacteria. In a Gal-β1,4-Rha-containing medium, Bifidobacterium longum subsp. infantis JCM 1222T, which possesses BLIJ_2090, a homologous protein to BL105A_0502, suppressed the growth of enteric pathogen Clostridioides difficile, whereas the BLIJ_2090 gene-disrupted mutant did not. In vivo, administration of B. infantis and Gal-β1,4-Rha alleviated C. difficile infection-related weight loss in mice. We have successfully screened Gal-β1,4-Rha as a next-generation prebiotic candidate that specifically promotes the growth of beneficial bacteria without promoting the growth of prominent bacteria and pathogens.

    DOI： 10.1080/19490976.2021.1973835

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  • Alkoxycarbonyl elimination of 3-O-substituted glucose and fructose by heat treatment under neutral pH Reviewed

    Kazuhiro Chiku, Riku Tsukasaki, Yu Teshima, Mitsuru Yoshida, Hiroki Aramasa, Takanori Nihira, Hiroyuki Nakai, Hiroshi Ono, Motomitsu Kitaoka

    Carbohydrate Research   108129 - 108129   2020.8

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    Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

    DOI： 10.1016/j.carres.2020.108129

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  • Large-scale preparation of β-1,2-glucan using quite a small amount of sophorose Reviewed

    Kobayashi K., Nakajima M., Aramasa H., Kimura S., Iwata T., Nakai H., Taguchi H.

    Bioscience, Biotechnology, and Biochemistry   83 ( 10 )   1867 - 1874   2019.10

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

    DOI： 10.1080/09168451.2019.1630257

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  • Identification, characterization, and structural analyses of a fungal endo-beta-1,2-glucanase reveal a new glycoside hydrolase family Reviewed

    Nobukiyo Tanaka, Masahiro Nakajima, Megumi Narukawa-Nara, Hiroki Matsunaga, Shinji Kamisuki, Hiroki Aramasa, Yuta Takahashi, Naohisa Sugimoto, Koichi Abe, Tohru Terada, Akimasa Miyanaga, Tetsuro Yamashita, Fumio Sugawara, Takashi Kamakura, Shiro Komba, Hiroyuki Nakai, Hayao Taguchi

    JOURNAL OF BIOLOGICAL CHEMISTRY   294 ( 19 )   7942 - 7965   2019.5

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    DOI： 10.1074/jbc.RA118.007087

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  • Colorimetric determination of β-1,2-glucooligosaccharides for an enzymatic assay using 3-methyl-2-benzothiazolinonehydrazone. Reviewed

    Kobayashi K, Aramasa H, Nakai H, Nakajima M, Taguchi H

    Analytical biochemistry   560   1 - 6   2018.11

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  • Synthesis of three deoxy-sophorose derivatives for evaluating the requirement of hydroxy groups at position 3 and/or 3 ' of sophorose by 1,2-beta-oligoglucan phosphorylases Reviewed

    Nobukiyo Tanaka, Masahiro Nakajima, Hiroki Aramasa, Hiroyuki Nakai, Hayao Taguchi, Wakako Tsuzuki, Shiro Komba

    CARBOHYDRATE RESEARCH   468   13 - 22   2018.10

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  • Characterization and Structural Analysis of a Novel exo-Type Enzyme Acting on β-1,2-Glucooligosaccharides from Parabacteroides distasonis. Reviewed

    Shimizu H, Nakajima M, Miyanaga A, Takahashi Y, Tanaka N, Kobayashi K, Sugimoto N, Nakai H, Taguchi H

    Biochemistry   57 ( 26 )   3849 - 3860   2018.7

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  • A heterozygous mutation in the SAM domain of p63 underlies a mild form of ectodermal dysplasia. Reviewed International journal

    Toru Kawai, Ryota Hayashi, Hiroyuki Nakai, Yutaka Shimomura, Mazen Kurban, Lamiaa Hamie, Hiroki Fujikawa, Atsushi Fujimoto, Riichiro Abe

    Journal of dermatological science   90 ( 3 )   360 - 363   2018.6

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  • Structural and thermodynamic insights into -1,2-glucooligosaccharide capture by a solute-binding protein in Listeria innocua Reviewed

    Koichi Abe, Naoki Sunagawa, Tohru Terada, Yuta Takahashi, Takatoshi Arakawa, Kiyohiko Igarashi, Masahiro Samejima, Hiroyuki Nakai, Hayao Taguchi, Masahiro Nakajima, Shinya Fushinobu

    Journal of Biological Chemistry   293 ( 23 )   8812 - 8828   2018

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：American Society for Biochemistry and Molecular Biology Inc.  

    DOI： 10.1074/jbc.RA117.001536

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  • Function and structure relationships of a β-1,2-glucooligosaccharide-degrading β-glucosidase Reviewed

    Rikuto Ishiguro, Nobukiyo Tanaka, Koichi Abe, Masahiro Nakajima, Takuma Maeda, Akimasa Miyanaga, Yuta Takahashi, Naohisa Sugimoto, Hiroyuki Nakai, Hayao Taguchi

    FEBS Letters   591 ( 23 )   3926 - 3936   2017.12

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    Language：English   Publisher：Wiley Blackwell  

    DOI： 10.1002/1873-3468.12911

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  • Biochemical and structural analyses of a bacterial endo-beta-1,2-glucanase reveal a new glycoside hydrolase family Reviewed

    Koichi Abe, Masahiro Nakajima, Tetsuro Yamashita, Hiroki Matsunaga, Shinji Kamisuki, Takanori Nihira, Yuta Takahashi, Naohisa Sugimoto, Akimasa Miyanaga, Hiroyuki Nakai, Takatoshi Arakawa, Shinya Fushinobu, Hayao Taguchi

    JOURNAL OF BIOLOGICAL CHEMISTRY   292 ( 18 )   7487 - 7506   2017.5

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    DOI： 10.1074/jbc.M116.762724

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  • Mechanistic insight into the substrate specificity of 1,2-beta-oligoglucan phosphorylase from Lachnoclostridium phytofermentans Reviewed

    Masahiro Nakajima, Nobukiyo Tanaka, Nayuta Furukawa, Takanori Nihira, Yuki Kodutsumi, Yuta Takahashi, Naohisa Sugimoto, Akimasa Miyanaga, Shinya Fushinobu, Hayao Taguchi, Hiroyuki Nakai

    SCIENTIFIC REPORTS   7   42671   2017.2

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

    DOI： 10.1038/srep42671

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  • Mutations in SDR9C7 gene encoding an enzyme for vitamin A metabolism underlie autosomal recessive congenital ichthyosis Reviewed

    Yohya Shigehara, Shujiro Okuda, Georges Nemer, Adele Chedraoui, Ryota Hayashi, Fadi Bitar, Hiroyuki Nakai, Ossama Abbas, Laetitia Daou, Riichiro Abe, Maria Bou Sleiman, Abdul Ghani Kibbi, Mazen Kurban, Yutaka Shimomura

    HUMAN MOLECULAR GENETICS   25 ( 20 )   4484 - 4493   2016.10

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    DOI： 10.1093/hmg/ddw277

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  • Using Carbohydrate Interaction Assays to Reveal Novel Binding Sites in Carbohydrate Active Enzymes Reviewed

    Darrell Cockburn, Casper Wilkens, Adiphol Dilokpimol, Hiroyuki Nakai, Anna Lewinska, Maher Abou Hachem, Birte Svensson

    PLOS ONE   11 ( 8 )   e0160112   2016.8

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    DOI： 10.1371/journal.pone.0160112

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  • An efficient arabinoxylan-debranching alpha-L-arabinofuranosidase of family GH62 from Aspergillus nidulans contains a secondary carbohydrate binding site Reviewed

    Casper Wilkens, Susan Andersen, Bent O. Petersen, An Li, Marta Busse-Wicher, Johnny Birch, Darrell Cockburn, Hiroyuki Nakai, Hans E. M. Christensen, Birthe B. Kragelund, Paul Dupree, Barry McCleary, Ole Hindsgaul, Maher Abou Hachem, Birte Svensson

    APPLIED MICROBIOLOGY AND BIOTECHNOLOGY   100 ( 14 )   6265 - 6277   2016.7

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

    DOI： 10.1007/s00253-016-7417-8

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  • A Solanum torvum GH3 beta-glucosidase expressed in Pichia pastoris catalyzes the hydrolysis of furostanol glycoside Reviewed

    Rungarun Suthangkornkul, Pornpisut Sriworanun, Hiroyuki Nakai, Masayuki Okuyama, Jisnuson Svasti, Atsuo Kimura, Saengchan Senapin, Dumrongkiet Arthan

    PHYTOCHEMISTRY   127   4 - 11   2016.7

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

    DOI： 10.1016/j.phytochem.2016.03.015

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  • Purification and characterization of a chloride ion-dependent alpha-glucosidase from the midgut gland of Japanese scallop (Patinopecten yessoensis) Reviewed

    Yasushi Masuda, Masayuki Okuyama, Takahisa Iizuka, Hiroyuki Nakai, Wataru Saburi, Taro Fukukawa, Janjira Maneesan, Takayoshi Tagami, Tetsushi Naraoka, Haruhide Mori, Atsuo Kimura

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   80 ( 3 )   479 - 485   2016.3

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  • Functional and Structural Analysis of a beta-Glucosidase Involved in beta-1,2-Glucan Metabolism in Listeria innocua Reviewed

    Masahiro Nakajima, Ryuta Yoshida, Akimasa Miyanaga, Koichi Abe, Yuta Takahashi, Naohisa Sugimoto, Hiroyuki Toyoizumi, Hiroyuki Nakai, Motomitsu Kitaoka, Hayao Taguchi

    PLOS ONE   11 ( 2 )   e0148870   2016.2

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  • A tale of two sisters: identical IL36RN mutations and discordant phenotypes Reviewed

    N. Rajan, N. Sinclair, H. Nakai, Y. Shimomura, S. . Natarajan

    BRITISH JOURNAL OF DERMATOLOGY   174 ( 2 )   417 - 420   2016.2

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  • Novel splice site mutation in the fumarate hydratase (FH) gene is associated with multiple cutaneous leiomyomas in a Japanese patient Reviewed

    Yukina Yoshinaga, Hiroyuki Nakai, Ryota Hayashi, Akiko Ito, Naoyuki Kariya, Masaaki Ito, Yutaka Shimomura

    JOURNAL OF DERMATOLOGY   43 ( 1 )   85 - 91   2016.1

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  • Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua Reviewed

    Tomohiro Tsuda, Takanori Nihira, Kazuhiro Chiku, Erika Suzuki, Takatoshi Arakawa, Mamoru Nishimoto, Motomitsu Kitaoka, Hiroyuki Nakai, Shinya Fushinobu

    FEBS LETTERS   589 ( 24 )   3816 - 3821   2015.12

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  • An inverting beta-1,2-mannosidase belonging to glycoside hydrolase family 130 from Dyadobacter fermentans Reviewed

    Takanori Nihira, Kazuhiro Chiku, Erika Suzuki, Mamoru Nishimoto, Shinya Fushinobu, Motomitsu Kitaoka, Ken'ichi Ohtsubo, Hiroyuki Nakai

    FEBS LETTERS   589 ( 23 )   3604 - 3610   2015.11

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  • Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 Reviewed

    Wilkens C, Cockburn D, Andersen S, Petersen BO, Ruzanski C, Field RA, Hindsgaul O, Nakai H, McCleary B, Smith AM, Abou Hachem M, Svensson B

    62 ( 3 )   87 - 93   2015.8

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  • Crystal Structure and Substrate Recognition of Cellobionic Acid Phosphorylase, Which Plays a Key Role in Oxidative Cellulose Degradation by Microbes Reviewed

    Young-Woo Nam, Takanori Nihira, Takatoshi Arakawa, Yuka Saito, Motomitsu Kitaoka, Hiroyuki Nakai, Shinya Fushinobu

    JOURNAL OF BIOLOGICAL CHEMISTRY   290 ( 30 )   18281 - 18292   2015.7

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  • Large-scale Preparation of 1,2-β-Glucan Using 1,2-β-Oligoglucan Phosphorylase Reviewed

    Abe Koichi, Nakajima Masahiro, Kitaoka Motomitsu, Toyoizumi Hiroyuki, Takahashi Yuta, Sugimoto Naohisa, Nakai Hiroyuki, Taguchi Hayao

    Journal of Applied Glycoscience   62 ( 2 )   47 - 52   2015.5

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    1,2-β-Glucan was produced enzymatically from 1.0 M sucrose and 0.5 M glucose by the combination of sucrose phosphorylase and 1,2-β-oligoglucan phosphorylase in the presence of 100 mM inorganic phosphate. Accumulation of 1,2-β-glucan in 2 L of the reaction mixture reached over 800 mM (glucose equivalent). Sucrose, glucose and fructose were removed after the reaction by yeast treatment. 1,2-β-Glucan was precipitated with ethanol to obtain 167 g of 1,2-β-glucan from 1 L of the reaction mixture.

    DOI： 10.5458/jag.jag.JAG-2014_011

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  • Discovery of Two beta-1,2-Mannoside Phosphorylases Showing Different Chain-Length Specificities from Thermoanaerobacter sp X-514 Reviewed

    Kazuhiro Chiku, Takanori Nihira, Erika Suzuki, Mamoru Nishimoto, Motomitsu Kitaoka, Ken'ichi Ohtsubo, Hiroyuki Nakai

    PLOS ONE   9 ( 12 )   e114882   2014.12

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  • One pot enzymatic production of nigerose from common sugar resources employing nigerose phosphorylase Reviewed

    Nihira T, Miyajima F, Nishimoto M, Kitaoka M, Ohtsubo K, Nakai H

    Journal of Applied Glycoscience   61 ( 3 )   75 - 80   2014.8

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    DOI： 10.5458/jag.jag.JAG-2013_012

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  • Structural Basis for Reversible Phosphorolysis and Hydrolysis Reactions of 2-O-alpha-Glucosylglycerol Phosphorylase Reviewed

    Kouki K. Touhara, Takanori Nihira, Motomitsu Kitaoka, Hiroyuki Nakai, Shinya Fushinobu

    JOURNAL OF BIOLOGICAL CHEMISTRY   289 ( 26 )   18067 - 18075   2014.6

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  • Characterization of two α-1,3-glucoside phosphorylases from Clostridium phytofermentans Reviewed

    Nihira T, Nishimoto M, Nakai H, Ohtsubo K, Kitaoka M

    Journal of Applied Glycoscience   61 ( 2 )   59 - 66   2014.5

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  • 1,2-beta-Oligoglucan Phosphorylase from Listeria innocua Reviewed

    Masahiro Nakajima, Hiroyuki Toyoizumi, Koichi Abe, Hiroyuki Nakai, Hayao Taguchi, Motomitsu Kitaoka

    PLOS ONE   9 ( 3 )   e92353   2014.3

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  • 2-O-alpha-D-Glucosylglycerol Phosphorylase from Bacillus selenitireducens MLS10 Possessing Hydrolytic Activity on beta-D-Glucose 1-Phosphate Reviewed

    Takanori Nihira, Yuka Saito, Ken'ichi Ohtsubo, Hiroyuki Nakai, Motomitsu Kitaoka

    PLOS ONE   9 ( 1 )   e86548   2014.1

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  • Discovery of cellobionic acid phosphorylase in cellulolytic bacteria and fungi Reviewed

    Takanori Nihira, Yuka Saito, Mamoru Nishimoto, Motomitsu Kitaoka, Kiyohiko Igarashi, Ken'Ichi Ohtsubo, Hiroyuki Nakai

    FEBS Letters   587 ( 21 )   3556 - 3561   2013.11

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    DOI： 10.1016/j.febslet.2013.09.014

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  • Potassium ion-dependent trehalose phosphorylase from halophilic Bacillus selenitireducens MLS10 Reviewed

    Takanori Nihira, Yuka Saito, Kazuhiro Chiku, Motomitsu Kitaoka, Ken'ichi Ohtsubo, Hiroyuki Nakai

    FEBS LETTERS   587 ( 21 )   3382 - 3386   2013.11

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    DOI： 10.1016/j.febslet.2013.08.038

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  • Characterization of a novel missense mutation in the prodomain of GDF5, which underlies brachydactyly type C and mild Grebe type chondrodysplasia in a large Pakistani family Reviewed

    Muhammad Farooq, Hiroyuki Nakai, Atsushi Fujimoto, Hiroki Fujikawa, Klaus Wilbrandt Kjaer, Shahid Mahmood Baig, Yutaka Shimomura

    HUMAN GENETICS   132 ( 11 )   1253 - 1264   2013.11

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    DOI： 10.1007/s00439-013-1330-3

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  • Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans Reviewed

    Takanori Nihira, Erika Suzuki, Motomitsu Kitaoka, Mamoru Nishimoto, Ken'ichi Ohtsubo, Hiroyuki Nakai

    Journal of Biological Chemistry   288 ( 38 )   27366 - 27374   2013.9

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    DOI： 10.1074/jbc.M113.469080

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  • A Snapshot into the Metabolism of Isomalto-oligosaccharides in Probiotic Bacteria Reviewed

    HACHEM Maher Abou, MOLLER Marie S., ANDERSEN Joakim M., FREDSLUND Folmer, MAJUMDER Avishek, NAKAI Hiroyuki, LEGGIO Leila Lo, GOH Yong-Jun, BARRANGOU Rodolphe, KLAENHAMMER Todd R., SVENSSON Birte

    Journal of Applied Glycoscience   60 ( 2 )   95 - 100   2013.7

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    <i>In vitro</i> and <i>in vivo</i> studies have demonstrated the prebiotic potential of isomalto-oligosaccharides (IMO), comprising α-(1,6)-gluco-oligosaccharides and panose, which selectively stimulate the growth of probiotic bifidobacteria and lactobacilli. The protein machinery conferring the utilization of IMO by probiotics, however, remains vaguely described. We have used genomic, transcriptomic, enzymatic, and biophysical analyses to explore IMO utilization routes in probiotic lactobacilli and bifidobacteria as re­presented by <i>Lactobacillus acidophilus</i> NCFM and <i>Bifidobacterium animalis</i> subsp. <i>lactis</i> Bl-04, respectively. Utilization of IMO and malto-oligosaccharide (α-(1,4)-glucosides) appears to be linked both at the genetic and transcriptomic level in the acidophilus group lactobacilli as suggested by reverse transcriptase PCR (RT-PCR) and gene landscape analysis. Canonical intracellular GH13_31 glucan 1,6-α-glucosidases active on IMO longer than isomaltose occur widely in acidophilus group lactobacilli. Interestingly, however, isomaltose, isomaltulose and panose seem to be internalized through a phosphoenoyl pyruvate transferase system (PTS) and subsequently hydrolyzed by a GH4 6-phosphate-α-glucosidases based on whole genome microarray analysis. This sub-specificity within GH4 seems to be unique for lactobacilli mainly from the gut niche, as the sequences from this group segregate from characterized GH4 maltose-6-phosphate-α-glucosidases in other organisms. By comparison, IMO utilization in bifidobacteria is linked to soybean oligosaccharide utilization loci harboring GH36 α-galactosidases, GH13_31 oligo 1,6-α-glucosidases and a dual specificity ATP-binding cassette (ABC) transport system active in the uptake of both classes of α-(1,6)-glycosides. These data bring novel insight to advance our understanding of the basis of selectivity of IMO metabolism by important gut microbiome members.

    DOI： 10.5458/jag.jag.JAG-2012_022

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  • Colorimetric Quantification of α-D-Mannose 1-Phosphate Reviewed

    NIHIRA Takanori, SUZUKI Erika, KITAOKA Motomitsu, NISHIMOTO Mamoru, OHTSUBO Ken'ichi, NAKAI Hiroyuki

    Journal of Applied Glycoscience   60 ( 2 )   137 - 139   2013.7

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    We developed an enzymatic colorimetric method for the quantification of <i>α</i>-D-mannose 1-phosphate by adding phosphomannomutase, mannose 6-phosphate isomerase and glucose 6-phosphate isomerase to a conventional glucose 6-phosphate assay using glucose 6-phosphate dehydrogenase. In this method, <i>α</i>-D-mannose 1-phosphate is converted into D-glucose 6-phosphate <i>via </i>D-mannose 6-phosphate and D-fructose 6-phosphate and the resultant D-glucose 6-phosphate is ultimately converted into 6-phosphogluconolactone under concomitant reduction of thio-NAD<sup>+</sup> to thio-NADH, which can be quantified by its wavelength of 400 nm. This method is not altered by the presence of D-mannose, D-mannosamine, <i>N</i>-acetyl-D-mannosamine, L-mannose, <i>β</i>-1,4-mannobiose, <i>α</i>-1,2-mannobiose, methyl <i>α</i>-D-mannoside or dimethyl sulfoxide and it would be useful in studies involving enzymes such as phosphorylases belonging to glycoside hydrolase family 130, which release <i>α</i>-D-mannose 1-phosphate as the reaction product.

    DOI： 10.5458/jag.jag.JAG-2012_019

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  • In vitro growth of four individual human gut bacteria on oligosaccharides produced by chemoenzymatic synthesis Reviewed

    Louise K. Vigsnaes, Hiroyuki Nakai, Lene Hemmingsen, Joakim M. Andersen, Sampo J. Lahtinen, Louise E. Rasmussen, Maher Abou Hachem, Bent O. Petersen, Jens Ø. Duus, Anne S. Meyer, Tine R. Licht, Birte Svensson

    Food and Function   4 ( 5 )   784 - 793   2013.5

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    DOI： 10.1039/c3fo30357h

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  • Recent development of phosphorylases possessing large potential for oligosaccharide synthesis Reviewed

    Hiroyuki Nakai, Motomitsu Kitaoka, Birte Svensson, Ken'ichi Ohtsubo

    CURRENT OPINION IN CHEMICAL BIOLOGY   17 ( 2 )   301 - 309   2013.4

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    DOI： 10.1016/j.cbpa.2013.01.006

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  • Key aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 alpha-glucosidase contribute to recognition of long-chain substrates Reviewed

    Takayoshi Tagami, Masayuki Okuyama, Hiroyuki Nakai, Young-Min Kim, Haruhide Mori, Kazunori Taguchi, Birte Svensson, Atsuo Kimura

    BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS   1834 ( 1 )   329 - 335   2013.1

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  • Mutation Analysis of the IL36RN Gene in 14 Japanese Patients with Generalized Pustular Psoriasis Reviewed

    Muhammad Farooq, Hiroyuki Nakai, Atsushi Fujimoto, Hiroki Fujikawa, Asako Matsuyama, Naoyuki Kariya, Atsuko Aizawa, Hiroshi Fujiwara, Masaaki Ito, Yutaka Shimomura

    HUMAN MUTATION   34 ( 1 )   176 - 183   2013.1

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  • Key aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 α-glucosidase contribute to recognition of long-chain substrates. Reviewed

    Tagami T, Okuyama M, Nakai H, Kim YM, Mori H, Taguchi K, Svensson B, Kimura A

    Biochimica et biophysica acta   1834 ( 1 )   329 - 335   2013.1

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  • Characterization of a laminaribiose phosphorylase from Acholeplasma laidlawii PG-8A and production of 1,3-beta-D-glucosyl disaccharides Reviewed

    Takanori Nihira, Yuka Saito, Motomitsu Kitaoka, Mamoru Nishimoto, Ken'ichi Otsubo, Hiroyuki Nakai

    CARBOHYDRATE RESEARCH   361   49 - 54   2012.11

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    DOI： 10.1016/j.carres.2012.08.006

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  • Identification of Bacillus selenitireducens MLS10 maltose phosphorylase possessing synthetic ability for branched alpha-D-glucosyl trisaccharides Reviewed

    Takanori Nihira, Yuka Saito, Motomitsu Kitaoka, Ken'ichi Otsubo, Hiroyuki Nakai

    CARBOHYDRATE RESEARCH   360   25 - 30   2012.10

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    DOI： 10.1016/j.carres.2012.07.014

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  • Amino Acids in Conserved Region II Are Crucial to Substrate Specificity, Reaction Velocity, and Regioselectivity in the Transglucosylation of Honeybee GH-13 alpha-Glucosidases Reviewed

    Lukana Ngiwsara, Gaku Iwai, Takayoshi Tagami, Natsuko Sato, Hiroyuki Nakai, Masayuki Okuyama, Haruhide Mori, Atsuo Kimura

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   76 ( 10 )   1967 - 1974   2012.10

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  • Bacteroides thetaiotaomicron VPI-5482 glycoside hydrolase family 66 homolog catalyzes dextranolytic and cyclization reactions Reviewed

    Young-Min Kim, Eiji Yamamoto, Min-Sun Kang, Hiroyuki Nakai, Wataru Saburi, Masayuki Okuyama, Haruhide Mori, Kazumi Funane, Mitsuru Momma, Zui Fujimoto, Mikihiko Kobayashi, Doman Kim, Atsuo Kimura

    FEBS JOURNAL   279 ( 17 )   3185 - 3191   2012.9

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    DOI： 10.1111/j.1742-4658.2012.08698.x

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  • Enzymology and Structure of the GH13_31 Glucan 1,6-alpha-Glucosidase That Confers Isomaltooligosaccharide Utilization in the Probiotic Lactobacillus acidophilus NCFM Reviewed

    Marie S. Moller, Folmer Fredslund, Avishek Majumder, Hiroyuki Nakai, Jens-Christian N. Poulsen, Leila Lo Leggio, Birte Svensson, Maher Abou Hachem

    JOURNAL OF BACTERIOLOGY   194 ( 16 )   4249 - 4259   2012.8

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  • Novel Dextranase Catalyzing Cycloisomaltooligosaccharide Formation and Identification of Catalytic Amino Acids and Their Functions Using Chemical Rescue Approach Reviewed

    Young-Min Kim, Yoshiaki Kiso, Tomoe Muraki, Min-Sun Kang, Hiroyuki Nakai, Wataru Saburi, Weeranuch Lang, Hee-Kwon Kang, Masayuki Okuyama, Haruhide Mori, Ryuichiro Suzuki, Kazumi Funane, Nobuhiro Suzuki, Mitsuru Momma, Zui Fujimoto, Tetsuya Oguma, Mikihiko Kobayashi, Doman Kim, Atsuo Kimura

    JOURNAL OF BIOLOGICAL CHEMISTRY   287 ( 24 )   19927 - 19935   2012.6

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  • A Novel Metabolic Pathway for Glucose Production Mediated by alpha-Glucosidase-catalyzed Conversion of 1,5-Anhydrofructose Reviewed

    Young-Min Kim, Wataru Saburi, Shukun Yu, Hiroyuki Nakai, Janjira Maneesan, Min-Sun Kang, Seiya Chiba, Doman Kim, Masayuki Okuyama, Haruhide Mori, Atsuo Kimura

    JOURNAL OF BIOLOGICAL CHEMISTRY   287 ( 27 )   22441 - 22444   2012.6

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  • 3-O-alpha-D-Glucopyranosyl-L-rhamnose phosphorylase from Clostridium phytofermentans Reviewed

    Takanori Nihira, Hiroyuki Nakai, Motomitsu Kitaoka

    CARBOHYDRATE RESEARCH   350   94 - 97   2012.3

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  • Discovery of nigerose phosphorylase from Clostridium phytofermentans Reviewed

    Takanori Nihira, Hiroyuki Nakai, Kazuhiro Chiku, Motomitsu Kitaoka

    APPLIED MICROBIOLOGY AND BIOTECHNOLOGY   93 ( 4 )   1513 - 1522   2012.2

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  • Recombinant production and characterisation of two related GH5 endo-beta-1,4-mannanases from Aspergillus nidulans FGSC A4 showing distinctly different transglycosylation capacity Reviewed

    Adiphol Dilokpimol, Hiroyuki Nakai, Charlotte H. Gotfredsen, Martin J. Baumann, Natsuko Nakai, Maher Abou Hachem, Birte Svensson

    BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS   1814 ( 12 )   1720 - 1729   2011.12

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  • Recombinant production and characterisation of two related GH5 endo-β-1,4-mannanases from Aspergillus nidulans FGSC A4 showing distinctly different transglycosylation capacity. Reviewed

    Dilokpimol A, Nakai H, Gotfredsen CH, Baumann MJ, Nakai N, Abou Hachem M, Svensson B

    Biochimica et biophysica acta   1814 ( 12 )   1720 - 1729   2011.12

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  • An Enzymatic Colorimetric Quantification of Orthophosphate Reviewed

    LI Bingxue, NIHIRA Takanori, NAKAI Hiroyuki, NISHIMOTO Mamoru, KITAOKA Motomitsu

    Journal of Applied Glycoscience   58 ( 3 )   125 - 127   2011.9

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    Quantification of orthophosphate (Pi) in the presence of labile phosphate esters is required for biochemical assays. We developed a method for the enzymatic colorimetric quantification of Pi using pyruvate oxidase and peroxidase. The calibration curve was not affected by the presence of labile phosphate esters. Furthermore, this method allows continuous monitoring of the reaction of Pi-releasing enzymes.

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  • Truncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity Reviewed

    Young-Min Kim, Ryoko Shimizu, Hiroyuki Nakai, Haruhide Mori, Masayuki Okuyama, Min-Sun Kang, Zui Fujimoto, Kazumi Funane, Doman Kim, Atsuo Kimura

    APPLIED MICROBIOLOGY AND BIOTECHNOLOGY   91 ( 2 )   329 - 339   2011.7

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  • Starch-binding domains in the CBM45 family - low-affinity domains from glucan, water dikinase and alpha-amylase involved in plastidial starch metabolism Reviewed

    Mikkel A. Glaring, Martin J. Baumann, Maher Abou Hachem, Hiroyuki Nakai, Natsuko Nakai, Diana Santelia, Bent W. Sigurskjold, Samuel C. Zeeman, Andreas Blennow, Birte Svensson

    FEBS JOURNAL   278 ( 7 )   1175 - 1185   2011.4

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  • Enzymatic synthesis of beta-xylosyl-oligosaccharides by transxylosylation using two beta-xylosidases of glycoside hydrolase family 3 from Aspergillus nidulans FGSC A4 Reviewed

    Adiphol Dilokpimol, Hiroyuki Nakai, Charlotte H. Gotfredsen, Maaike Appeldoorn, Martin J. Baumann, Natsuko Nakai, Henk A. Schols, Maher Abou Hachem, Birte Svensson

    CARBOHYDRATE RESEARCH   346 ( 3 )   421 - 429   2011.2

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  • Efficient chemoenzymatic oligosaccharide synthesis by reverse phosphorolysis using cellobiose phosphorylase and cellodextrin phosphorylase from Clostridium thermocellum Reviewed

    Hiroyuki Nakai, Maher Abou Hachem, Bent O. Petersen, Yvonne Westphal, Karin Mannerstedt, Martin J. Baumann, Adiphol Dilokpimol, Henk A. Schols, Jens O. Duus, Birte Svensson

    BIOCHIMIE   92 ( 12 )   1818 - 1826   2010.12

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  • Suicide Substrate-based Inactivation of Endodextranase by ω-Epoxyalkyl α-D-Glucopyranosides Reviewed

    KANG Hee-Kwon, KIM Young-Min, NAKAI Hiroyuki, KANG Min-Sun, HAKAMADA Wataru, OKUYAMA Masayuki, MORI Haruhide, NISHIO Toshiyuki, KIMURA Atsuo

    Journal of Applied Glycoscience   57 ( 4 )   269 - 272   2010.11

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    Three kinds of ω-epoxyalkyl α-glucopyranosides (3′,4′-epoxybutyl α-<small>D</small>-glucopyranoside (E4G), 4′,5′-epoxypentyl α-<small>D</small>-glucopyranoside (E5G) and 5′,6′-epoxyhexyl α-<small>D</small>-glucopyranoside (E6G)), having alkyl chains of different lengths at their aglycone moieties, inactivated the endodextranase from <i>Streptococcus mutans</i> ATCC 25175 (SmDex) irreversibly with the pseudo-first order kinetics. Alkyl chain length-dependent inactivation was observed and the degree of activity loss was E5G, E6G and E4G, in that order, implying that the distance between epoxide group and glucosyl residue of ω-epoxyalkyl α-glucopyranoside was important in the modification of endodextranase. Inactivation by E5G followed the model of reversible intermediate-complex formation mechanism (suicide inhibitor-based mechanism). The rate constant of irreversible inactivation (<i>k</i>) and the dissociation constant of intermediate-complex (<i>K</i><small>R</small>) of SmDex and E5G were 0.44 min<sup>-1</sup> and 1.45 m<small>M</small>, respectively. Hydrolytic reaction product (isomaltose) protected SmDex from E5G-inactivation, suggesting that E5G bound to the catalytic site of SmDex. This is the first report that ω-epoxyalkyl α-glucopyranoside becomes a suicide substrate for endodextranase.

    DOI： 10.5458/jag.57.269

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  • Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase Reviewed

    Hiroyuki Nakai, Bent O. Petersen, Yvonne Westphal, Adiphol Dilokpimol, Maher Abou Hachem, Jens O. Duus, Henk A. Schols, Birte Svensson

    PROTEIN ENGINEERING DESIGN & SELECTION   23 ( 10 )   781 - 787   2010.10

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    DOI： 10.1093/protein/gzq055

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  • Aspergillus nidulans alpha-galactosidase of glycoside hydrolase family 36 catalyses the formation of alpha-galacto-oligosaccharides by transglycosylation Reviewed

    Hiroyuki Nakai, Martin J. Baumann, Bent O. Petersen, Yvonne Westphal, Maher Abou Hachem, Adiphol Dilokpimol, Jens O. Duus, Henk A. Schols, Birte Svensson

    FEBS JOURNAL   277 ( 17 )   3538 - 3551   2010.9

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    DOI： 10.1111/j.1742-4658.2010.07763.x

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  • Efficient one-pot enzymatic synthesis of alpha-(1,4)-glucosidic disaccharides through a coupled reaction catalysed by Lactobacillus acidophilus NCFM maltose phosphorylase Reviewed

    Hiroyuki Nakai, Adiphol Dilokpimol, Maher Abou Hachem, Birte Svensson

    CARBOHYDRATE RESEARCH   345 ( 8 )   1061 - 1064   2010.5

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    DOI： 10.1016/j.carres.2010.03.021

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  • The maltodextrin transport system and metabolism in Lactobacillus acidophilus NCFM and production of novel alpha-glucosides through reverse phosphorolysis by maltose phosphorylase Reviewed

    Hiroyuki Nakai, Martin J. Baumann, Bent O. Petersen, Yvonne Westphal, Henk Schols, Adiphol Dilokpimol, Maher A. Hachem, Sampo J. Lahtinen, Jens O. Duus, Birte Svensson

    FEBS JOURNAL   276 ( 24 )   7353 - 7365   2009.12

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    DOI： 10.1111/j.1742-4658.2009.07445.x

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  • Molecular Mechanism of α-glucosidase Reviewed

    Masayuki Okuyama, Haruhide Mori, Hironori Hondoh, Hiroyuki Nakai, Wataru Saburi, Min Sung Kang, Young Min Kim, Mamoru Nishimoto, Jintanart Wongchawalit, Takeshi Yamamoto, Mee Son, Jin Ha Lee, San San Mar, Kenji Fukuda, Seiya Chiba, Atsuo Kimura

    Carbohydrate-Active Enzymes: Structure, Function and Applications   64 - 76   2008.9

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    DOI： 10.1533/9781845695750.1.64

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  • Rice alpha-glucosidase isozymes and isoforms showing different starch granules-binding and -degrading ability Reviewed

    Hiroyuki Nakai, Shigeki Tanizawa, Tatsuya Ito, Koutaro Kamiya, Young-Min Kim, Takeshi Yamamoto, Kazuki Matsubara, Makoto Sakai, Hiroyuki Sato, T. Okio Imbe, Masayuki Okuyama, Haruhide Mori, Seiya Chiba, Yoshio Sano, Atsuo Kimura

    BIOCATALYSIS AND BIOTRANSFORMATION   26 ( 1-2 )   104 - 110   2008

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    DOI： 10.1080/10242420701788736

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  • Function-unknown glycoside hydrolase family 31 proteins, mRNAs of which were expressed in rice ripening and germinating stages, are alpha-glucosidase and alpha-xylosidase Reviewed

    Hiroyuki Nakai, Shigeki Tanizawa, Tatsuya Ito, Koutarou Kamiya, Young-Min Kim, Takeshi Yamamoto, Kazuki Matsubara, Makoto Sakai, Hiroyuki Sato, Tokio Imbe, Masayuki Okuyama, Haruhide Mori, Yoshio Sano, Seiya Chiba, Atsuo Kimura

    JOURNAL OF BIOCHEMISTRY   142 ( 4 )   491 - 500   2007.10

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    DOI： 10.1093/jb/mvm174

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  • Multiple forms of alpha-glucosidase in rice seeds (Oryza sativa L., var Nipponbare) Reviewed

    Hiroyuki Nakai, Tatsuya Ito, Masatoshi Hayashi, Koutarou Kamiya, Takeshi Yamamoto, Kazuki Matsubara, Young-Min Kim, Wongchawalit Jintanart, Masayuki Okuyama, Haruhide Mori, Seiya Chiba, Yoshio Sano, Atsuo Kimura

    BIOCHIMIE   89 ( 1 )   49 - 62   2007.1

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    DOI： 10.1016/j.biochi.2006.09.014

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  • Purification and characterization of alpha-glucosidase I from Japanese honeybee (Apis cerana japonica) and molecular cloning of its cDNA Reviewed

    Jintanart Wongchawalit, Takeshi Yamamoto, Hiroyuki Nakai, Young-Min Kim, Natsuko Sato, Mamoru Nishimoto, Masayuki Okuyama, Haruhide Mori, Osamu Saji, Chanpen Chanchao, Siriwat Wongsiri, Rudee Surarit, Jisnuson Svasti, Seiya Chiba, Atsuo Kimura

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   70 ( 12 )   2889 - 2898   2006.12

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    DOI： 10.1271/bbb.60302

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  • Plant α-Glucosidase : Molecular Analysis of Rice α-Glucosidase and Degradation Mechanism of Starch Granules in Germination Stage Reviewed

    NAKAI Hiroyuki, ITO Tatsuya, TANIZAWA Shigeki, MATSUBARA Kazuki, YAMAMOTO Takeshi, OKUYAMA Masayuki, MORI Haruhide, CHIBA Seiya, SANO Yoshio, KIMURA Atsuo

    Journal of Applied Glycoscience   53 ( 2 )   137 - 142   2006.7

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    In germination of plant seeds, storage starch is principally degraded by the combination of amylolytic enzymes. As starch is an insoluble granule, a conventional view of the degradation pathway is that the initial attack is performed by α-amylase having the starch granule-binding ability. Plant α-glucosidase was also capable of adsorbing and hydrolyzing starch granules directly, indicating a possible second pathway: the direct liberation of glucose from starch granules by plant α-glucosidase rather than the α-amylase-mediated system. We found that the starch-binding site of plant α-glucosidase was situated in its C-terminal region, of which function was independent of the catalytic domain. Site-directed mutagenesis analysis on the aromatic amino acid residues conserved in this region revealed that Trp803 and Phe895 of rice α-glucosidase were responsible for binding to starch granules. Mold α-glucosidases were devoid of the ability to attack starch granules. In plant seeds, multiple α-glucosidases have been observed. Two types of α-glucosidases, insoluble and soluble enzymes, were found in the germinating stage of rice. Expression patterns of their activities classified 14 rice varieties into two groups (Groups 1 and 2). In Group 1 varieties, insoluble enzyme decreased immediately after germination. The soluble enzyme increased by <i>de novo</i> synthesis. Group 2 maintained a constant activity level of insoluble and soluble α-glucosidases in germination. From Groups 1 and 2, we selected varieties of Akamai and Nipponbare, respectively, of which analysis elucidated interesting molecular mechanisms of insoluble and soluble enzymes: i) isoform and isozyme formations by post-translational proteolysis as well as by chromosomal gene expression; ii) characterization of purified enzymes exhibiting different activities to starch granules.

    DOI： 10.5458/jag.53.137

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  • Glucoamylase originating from Schwanniomyces occidentalis is a typical alpha-glucosidase Reviewed

    F Sato, M Okuyama, H Nakai, H Mori, A Kimura, S Chiba

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   69 ( 10 )   1905 - 1913   2005.10

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    DOI： 10.1271/bbb.69.1905

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  • Enzymatic synthesis of alkyl alpha-2-deoxyglucosides by alkyl alcohol resistant alpha-glucosidase from Aspergillus niger Reviewed

    YM Kim, M Okuyama, H Mori, H Nakai, W Saburi, S Chiba, A Kimura

    TETRAHEDRON-ASYMMETRY   16 ( 2 )   403 - 409   2005.1

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    DOI： 10.1016/j.tetasy.2004.11.046

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  • Molecular analysis of alpha-glucosidase belonging to GH-family 31 Reviewed

    H Nakai, M Okuyama, YM Kim, W Saburi, J Wongchawalit, H Mori, S Chiba, A Kimura

    BIOLOGIA   60   131 - 135   2005

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MISC

  • 直鎖β-1,2-グルカンから環状16+2(18)糖を特異的に合成する光合成細菌由来GH186ホモログの機能構造相関の解明

    丹生拳志郎, 元内省, 今場司朗, キム インヒョク, 鹿島騰真, 北野義直, 中井博之, 中島将博

    日本応用糖質科学会大会・応用糖質科学シンポジウム講演要旨集   74th-14th   2025

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  • Structural and functional analysis of novel α-1,6-cyclized β-1,2-glucan synthase from Ralstonia solanacearum and Methylomagnum ishizawai

    KIM Inhyuk, 元内省, 今場司朗, 鹿島騰真, 北野義直, 中井博之, 中島将博

    日本農芸化学会大会講演要旨集(Web)   2025   2025

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  • 新規α-1,6-環状化-β-1,2-グルコ21糖・29糖合成酵素の発見と機能構造解析

    石黒亜衣, 元内省, キム インヒョク, 今場司朗, 鹿島騰真, 北野義直, 中井博之, 中島将博

    日本応用糖質科学会大会・応用糖質科学シンポジウム講演要旨集   74th-14th   2025

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  • The novel transglycosylase from Cereibacter sphaeroides synthesizes phytopathogenic glycan-like cyclic glucan

    丹生拳志郎, 元内省, 今場司朗, 鹿島騰真, KIM Inhyuk, 北野義直, 中井博之, 中島将博

    日本農芸化学会大会講演要旨集(Web)   2025   2025

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  • α-1,6-Cyclized β-1,2-glucanを基本骨格とする多様な新規糖鎖の発見とその合成酵素群の機能解明

    キム インヒョク, 元内省, 今場司朗, 鹿島騰真, 北野義直, 中井博之, 中島将博

    日本応用糖質科学会大会・応用糖質科学シンポジウム講演要旨集   74th-14th   2025

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  • 多様化するGH186の反応機構の中で見つかった世界初のanomer-inverting transglycosylation

    元内省, 今場司朗, 小林海渡, 中井博之, 中島将博

    日本応用糖質科学会大会・応用糖質科学シンポジウム講演要旨集   73rd-13th   2024

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  • ビフィズス菌を選択的に増殖させるガラクトシル-β-1,4-ラムノースを用いた偽膜性腸炎原因菌の生育抑制効果

    平野里佳, 平野里佳, 阪中幹祥, 吉見一人, 吉見一人, 山内祐子, 山内祐子, 後藤愛那, 片山高嶺, 片山高嶺, 飯田宗穂, 加藤完, 大野博司, 吹谷智, 横田篤, 西本完, 北岡本光, 北岡本光, 中井博之, 栗原新, 栗原新

    日本実験動物学会総会講演要旨集(Web)   70th   2023

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  • ビフィズス菌を特異的に増殖させる次世代型プレバイオティクスの開発と応用

    平野里佳, 阪中幹祥, 杉本直久, 江口省吾, 奈良未沙希, 片山高嶺, 北岡本光, 中井博之, 栗原新

    日本乳酸菌学会誌   30 ( 2 )   2019

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  • 酵素合成法による機能性オリゴ糖の創出

    中井博之

    応用糖質科学   8 ( 1 )   51‐55   2018.2

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  • Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes

    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

    GLYCOBIOLOGY   28 ( 1 )   3 - 8   2018.1

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  • Listeria innocua由来β‐グルコシダーゼの結晶構造解析

    中島将博, 吉田龍太, 宮永顕正, 中井博之, 田口速男

    KEK Progress Report (Web)   ( 2016-8 )   ROMBUNNO.283 (WEB ONLY)   2017.1

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  • Lachnoclostridium phytofermentans由来1,2-β-オリゴグルカンホスホリラーゼの結晶構造解析

    中島将博, 古川那由太, 宮永顕正, 中井博之, 田口速男

    Photon Factory Activity Report   35   2017

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  • β-1,2-グルカン関連酵素群の機能と構造

    中島将博, 阿部紘一, 阿部紘一, 田中信清, 宮永顕正, 中井博之, 伏信進矢, 五十嵐圭日子, 北岡本光, 鮫島正浩, 田口速男

    応用糖質科学   7 ( 3 )   2017

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  • Trichoderma reesei由来β‐グルコシダーゼII(Cel1A)の糖転移生成物の解析

    戸谷一英, 二階堂望, 佐野孝晃, 小野寺一樹, 尾形慎, 中島将博, 中井博之

    応用糖質科学   6 ( 3 )   56 - 56   2016.8

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  • ABCトランスポーターソホロオリゴ糖結合タンパク質のリガンド認識の構造基盤

    阿部 紘一, 中島 将博, 砂川 直輝, 石田 卓也, 五十嵐 圭日子, 鮫島 正浩, 宮永 顕正, 中井 博之, 田口 速男, 荒川 孝俊, 伏信 進矢

    応用糖質科学   6 ( 3 )   62 - 62   2016.8

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  • Thermodynamic analysis and crystal structure of a solute-binding protein of ABC transporter specific for sophorooligosaccharides

    阿部紘一, 中島将博, 砂川直輝, 石田卓也, 五十嵐圭日子, 鮫島正浩, 宮永顕正, 中井博之, 田口速男, 荒川孝俊, 伏信進矢

    量子ビームサイエンスフェスタ(Web)   2015   2016

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  • Cellobionic acid phosphorylase involved in oxidative cellulose degradation

    仁平高則, 杉本直久, 中井博之

    Cellul Commun   22 ( 4 )   175 - 179   2015.12

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  • 新規β‐マンノシドホスホリラーゼの発見

    知久和寛, 仁平高則, 鈴木絵里香, 西本完, 北岡本光, 中井博之, 大坪研一

    応用糖質科学   5 ( 2 )   120 - 127   2015.5

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  • Trichoderma reesei由来β‐グルコシダーゼの基質特異性

    SATO DAISUKE, HIRASAWA TATSUMI, OKADA HIROFUMI, OGATA MAKOTO, NAKAJIMA MASAHIRO, NAKAI HIROYUKI, TOTANI KAZUHIDE

    日本農芸化学会大会講演要旨集(Web)   2015   3E32A14 (WEB ONLY)   2015.3

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  • Trichoderma reesei由来のβ‐グルコシダーゼの基質特異性

    TOTANI KAZUHIDE, HIRASAWA TATSUMI, SUZUKI TAKAHISA, OGATA MAKOTO, NAKAJIMA MASAHIRO, NAKAI HIROYUKI, OKADA HIROFUMI

    応用糖質科学   4 ( 3 )   (53)   2014.8

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  • Cp-8 Talaromyces funiculosus由来1,2-β-グルカン分解酵素の遺伝子同定及び機能解析(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    田中 信清, 阿部 紘一, 中島 将博, 成川 恵, 北岡 本光, 中井 博之, 山下 哲郎, 田口 速男

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B50   2014.8

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  • Cp-6 Listeria innocua由来β-グルコシダーゼの機能構造相関(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    吉田 龍太, 中島 将博, 宮永 顕正, 中井 博之, 北岡 本光, 田口 速男

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B49   2014.8

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  • Cp-14 GH94セロビオン酸ホスホリラーゼの基質特異性の構造基盤(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    Nam Young-Woo, 仁平 高則, 北岡 本光, 中井 博之, 荒川 孝俊, 伏信 進矢

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B51   2014.8

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  • Cp-12 GH130に属する糖質加水分解酵素β-1,2-マンノシダーゼの発見(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    知久 和寛, 仁平 高則, 鈴木 絵里香, 西本 完, 北岡 本光, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B51   2014.8

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  • Cp-13 新規ホスホリラーゼを用いたセロビオン酸の合成(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    斉藤 由華, 仁平 高則, 西本 完, 北岡 本光, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B51   2014.8

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  • S3-7 複合糖鎖の代謝に関与する新規βマンノシドホスホリラーゼの発見(応用糖質科学シンポジウム,日本応用糖質科学会平成26年度大会(第63回))

    知久 和寛, 仁平 高則, 鈴木 絵里香, 西本 完, 北岡 本光, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B63   2014.8

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  • Cp-7 1,2-β-グルカナーゼの同定(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    阿部 紘一, 中島 将博, 豊泉 大幸, 山下 哲郎, 中井 博之, 北岡 本光, 田口 速男

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B49   2014.8

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  • Cp-11 Listeria innocua由来1,2-β-オリゴマンナンホスホリラーゼのX線結晶構造解析(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    津田 智弘, 仁平 高則, 北岡 本光, 中井 博之, 荒川 孝俊, 伏信 進矢

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B50   2014.8

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  • Cp-9 Saccharophagus degradans 2-40由来4-O-β-D-マンノシル-D-グルコースホスホリラーゼによる非還元性二糖の生産(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    鈴木 絵里香, 知久 和寛, 仁平 高則, 西本 完, 北岡 本光, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B50   2014.8

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  • Cp-10 新規1,2-β-オリゴマンナンホスホリラーゼ(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    仁平 高則, 知久 和寛, 鈴木 絵里香, 西本 完, 北岡 本光, 伏信 進矢, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B50   2014.8

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  • Cp-5 ホスホリラーゼを用いた1,2-β-グルコオリゴ糖調製と1,2-β-グルカン大量合成(ホスホリラーゼ,一般講演,日本応用糖質科学会平成26年度大会(第63回))

    豊泉 大幸, 阿部 紘一, 中島 将博, 中井 博之, 北岡 本光, 田口 速男

    応用糖質科学 : 日本応用糖質科学会誌   4 ( 3 )   B49   2014.8

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  • S2-5 Analysis of Surface Binding Sites (SBS) within GH62, GH13 and GH77(Recent Progress of Carbohydrate Bioengineering)

    Wilkens C., Cockbum D., Andersen S., Petersen B.O., Ruzanski C., Field R., Hindsgaul O., Nakai H., McCleary B., Smith A., Abou Hachem M., Svensson B.

    Bulletin of applied glycoscience   4 ( 3 )   B29   2014.8

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  • ニゲラン代謝に関わるClostridium phytofermentans由来の新規ホスホリラーゼの発見

    仁平高則, 宮嶋双葉, 知久和寛, 北岡本光, 中井博之, 大坪研一

    応用糖質科学   4 ( 2 )   147 - 153   2014.5

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  • Heterozygote IL36RN mutations in a European case of early-onset generalized pustular psoriasis challenge the concept of private mutation

    N. Rajan, N. Sinclair, H. Nakai, Y. Shimomura, S. Natarajan

    BRITISH JOURNAL OF DERMATOLOGY   170 ( 4 )   E11 - E11   2014.4

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  • セロビオン酸ホスホリラーゼの発見

    仁平高則, 斉藤由華, 西本完, 北岡本光, 五十嵐圭日子, 伏信進矢, 中井博之, 大坪研一

    日本農芸化学会大会講演要旨集(Web)   2014   2014

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  • Cp-8 Chloroflexus aurantiacus J-10-fl由来の耐熱性コージビオースホスホリラーゼの機能解析(ホスホリラーゼ,一般講演,日本応用糖質科学会平成25年度大会(第62回))

    斉藤 由華, 仁平 高則, 知久 和寛, 北岡 本光, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   3 ( 3 )   B41   2013.8

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  • S3-4 ニゲラン代謝に関わるClostridium phytofermentans由来の新規ホスホリラーゼの発見(応用糖質科学シンポジウム,日本応用糖質科学会平成25年度大会(第62回))

    仁平 高則, 宮嶋 双葉, 知久 和寛, 北岡 本光, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   3 ( 3 )   B52   2013.8

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  • Cp-9 2-O-α-グルコシルグリセロールホスホリラーゼによるβGlc1P加水分解の分子機構および構造基盤(ホスホリラーゼ,一般講演,日本応用糖質科学会平成25年度大会(第62回))

    北岡 本光, 仁平 高則, 斉藤 由華, 東原 幸起, 伏信 進矢, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   3 ( 3 )   B42   2013.8

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  • Cp-7 新規酵素β-1,4-マンノシルN-アセチルグルコサミンホスホリラーゼ(ホスホリラーゼ,一般講演,日本応用糖質科学会平成25年度大会(第62回))

    鈴木 絵里香, 仁平 高則, 北岡 本光, 西本 完, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   3 ( 3 )   B41   2013.8

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  • ホスホリラーゼを利用した安価原料からの機能性オリゴ糖合成

    仁平高則, 中井博之, 大坪研一

    Bio Ind   30 ( 5 )   47 - 54   2013.5

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  • Key aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 .ALPHA.-glucosidase contribute to recognition of long-chain substrates

    TAGAMI Takayoshi, OKUYAMA Masayuki, NAKAI Hiroyuki, KIM Young-min, MORI Haruhide, TAGUCHI Kazunori, SVENSSON Birte, KIMURA Atsuo

    Biochimica et Biophysica Acta   1834 ( 1 )   329 - 335   2013.1

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  • 糖質関連酵素が触媒する糖質合成反応を活用した新規オリゴ糖の生産開発

    中井博之, 仁平高則, 北岡本光, 大坪研一

    応用糖質科学   2 ( 4 )   223 - 224   2012.11

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  • Bp1-7 Acholeplasma laidlawii PG-8A由来ラミナリビオースホスホリラーゼ(ホスホリラーゼおよび関連酵素,一般講演,日本応用糖質科学会平成24年度大会(第61回))

    仁平 高則, 斉藤 由華, 北岡 本光, 西本 完, 中井 博之, 大坪 研一

    応用糖質科学 : 日本応用糖質科学会誌   2 ( 3 )   B37   2012.8

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  • S3-5 The utilization routes of iso maltooligosaccharides by probiotics : an enzymatic and genetic overview

    Abou Hachem M., Moller M., Fredslund F., Andersen J.M., Majumder A., Nakai H., Lahtinen S.J., Yong J.-G., Klaenhammer T.R., Barrangou R., Lo Leggio L., Svensson B.

    Bulletin of applied glycoscience   2 ( 3 )   B59   2012.8

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  • プレバイオティクスとして有用な新規機能性オリゴ糖の生産開発

    中井博之, SVENSSON Birte, 大坪研一

    応用糖質科学   2 ( 2 )   117 - 121   2012.5

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  • 高機能性食品素材として有用なオリゴ糖の生産技術開発とその高度利用 加リン酸分解酵素(ホスホリラーゼ)を利用して高収率生産

    中井博之

    化学と生物   49 ( 10 )   669 - 671   2011.10

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  • 新しく見出されたイソマルトオリゴ糖不均化酵素の遺伝子クローニングと異種宿主発現

    鐘ケ江倫世, KIM Young‐Min, 中井博之, 本同宏成, 奥山正幸, 森春英, 木村淳夫

    日本農芸化学会大会講演要旨集   2008   191   2008.3

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  • 新規なイソマルトオリゴ糖生成酵素の単離と性質

    鐘ケ江倫世, KIM Young‐Min, 中井博之, 奥山正幸, 森春英, 木村淳夫

    J Appl Glycosci   54 ( Suppl. )   43   2007.7

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  • ホタテガイ由来塩素イオン依存性α‐amylaseの構造と機能

    飯塚貴久, 小林和之, 中井博之, 奥山正幸, 森春英, 奈良岡哲志, 千葉誠哉, 木村淳夫

    J Appl Glycosci   54 ( Suppl. )   32   2007.7

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  • デキストラン関連酵素が有するデキストラン結合ドメインの機能解析

    中井博之, 金泳民, 原口慶子, 奥山正幸, 森春英, 舟根和美, 小林幹彦, 木村淳夫

    日本農芸化学会大会講演要旨集   2007   65   2007.3

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  • ホタテガイ閉殻筋由来α‐glucosidaseのマルチプルフォームの構造解析

    飯塚貴久, 中井博之, 奥山正幸, 森春英, 奈良岡哲志, 千葉誠哉, 木村淳夫

    日本農芸化学会大会講演要旨集   2007   206   2007.3

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  • クロマルハナバチ(Bombus terrestris)α‐グルコシダーゼ:アロステリック酵素の性質解明と遺伝子発現

    佐藤なつ子, 鳥羽瀬輝, 中井博之, 西本完, 森春英, 奥山正幸, 木村淳夫

    生化学   3P-0212   2007

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  • クロマルハナバチ,Bombus ignitus,α‐GlucosidaseアイソザイムIの長鎖基質認識に関わるアミノ酸残基の決定

    佐藤なつ子, 中井博之, 森春英, 奥山正幸, 千葉誠哉, 木村淳夫

    J Appl Glycosci   53 ( Suppl. )   31   2006.8

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  • GST融合タンパク質を用いたイネα‐glucosidaseの澱粉粒吸着および分解機構の解析

    谷沢茂紀, 中井博之, 奥山正幸, 森春英, 千葉誠哉, 木村淳夫

    J Appl Glycosci   53 ( Suppl. )   43   2006.8

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  • ホタテガイ閉殻筋に存在するイオン要求性α‐glucosidaseの精製とその諸性質

    飯塚貴久, 中井博之, 奥山正幸, 森春英, 奈良岡哲志, 千葉誠哉, 木村淳夫

    J Appl Glycosci   53 ( Suppl. )   30   2006.8

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  • セイヨウミツバチα‐glucosidaseアイソザイムIIのβ→αループ8変異酵素の機能解析

    佐藤なつ子, 中井博之, 森春英, 奥山正幸, 千葉誠哉, 木村淳夫

    日本農芸化学会大会講演要旨集   2006   154   2006.3

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  • セイヨウミツバチα‐Glucosidase IIのV167N変異酵素は高いK<sub>m</sub>およびk<sub>0</sub>を与え,マルハナバチα‐Glucosidase IIの性質を示した

    佐藤なつ子, 中井博之, 奥山正幸, 森春英, 千葉誠哉, 木村淳夫

    J Appl Glycosci   52 ( Suppl. )   24   2005.7

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  • —ホタテガイ中腸腺由来イオン依存性α‐glucosidase—

    飯塚貴久, 福川太郎, 西岡謙吾, 中井博之, 奥山正幸, 森春英, 吉田孝, 千葉誠哉, 木村淳夫

    J Appl Glycosci   52 ( Suppl. )   26   2005.7

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  • 植物α‐Glucosidase,特にイネ酵素の分子解析と発芽時の澱粉粒分解に関する研究

    中井博之, 谷沢茂紀, 松原一樹, 奥山正幸, 森春英, 千葉誠哉, 佐野芳雄, 木村淳夫

    J Appl Glycosci   52 ( Suppl. )   52   2005.7

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  • 植物α‐GlucosidaseのC末端領域は単独で澱粉粒に吸着する‐GST融合タンパク質による解析‐

    谷沢茂紀, 中井博之, 奥山正幸, 森春英, 千葉誠哉, 木村淳夫

    J Appl Glycosci   52 ( Suppl. )   25   2005.7

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  • イネGlycoside Hydrolase Family 31様遺伝子の発現解析

    中井博之, 伊藤真吾, 奥山正幸, 森春英, 千葉誠哉, 佐藤芳雄, 木村淳夫

    日本農芸化学会大会講演要旨集   2005   30   2005.3

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  • イネGlycoside hydrolase family 31様タンパク質の機能解析

    谷沢茂紀, 中井博之, 奥山正幸, 森春英, 千葉誠哉, 佐野芳雄, 木村淳夫

    日本農芸化学会大会講演要旨集   2005   31   2005.3

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  • クロマルハナバチ,Bombus ignitus,α‐Glucosidaseアイソザイムの精製・諸性質および一次構造の解析

    佐藤なつ子, 高橋有志, 中井博之, 光畑雅宏, 奥山正幸, 森春英, 千葉誠哉, 木村淳夫

    日本農芸化学会大会講演要旨集   2005   30   2005.3

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  • 植物α‐Glucosidaseの生澱粉吸着に関与するアミノ酸残基の解析

    中井博之, 谷沢茂紀, 奥山正幸, 森春英, 山本健, 佐野芳雄, 千葉誠哉, 木村淳夫

    J Appl Glycosci   51 ( Suppl. )   41   2004.7

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  • クロマルハナバチ,Bombus ignitus,α‐Glucosidase Iの精製と諸性質

    佐藤なつ子, 高橋有志, 中井博之, 光畑雅宏, 奥山正幸, 森春英, 千葉誠哉, 木村淳夫

    J Appl Glycosci   51 ( Suppl. )   40   2004.7

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  • 植物α‐Glucosidaseに見出された新規な生澱粉結合部位の解析

    中井博之, 奥山正幸, 森春英, 山本健, 千葉誠哉, 佐野芳雄, 木村淳夫

    日本農芸化学会大会講演要旨集   2004   254   2004.3

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  • 赤米および日本晴で発芽時に作用するα‐Glucosidaseの一次構造の解析

    中井博之, 伊藤達也, 松原一樹, 奥山正幸, 森春英, 千葉誠哉, 佐野芳雄, 木村淳夫

    日本農芸化学会大会講演要旨集   2003   100   2003.3

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  • 赤米α‐Glucosidaseの限定分解とそれによる諸性質への影響

    中井博之, 伊藤達也, 森春英, 千葉誠哉, 木村淳夫

    日本農芸化学会大会講演要旨集   2002   127   2002.3

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  • 赤米α‐Glucosidaseの精製と諸性質

    中井博之, 林正敏, 森春英, 木村淳夫, 千葉誠哉

    日本農芸化学会誌   75   65   2001.3

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Awards

  • ポスター賞

    2021.9   日本応用糖質科学会  

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  • 2020年度大会トピックス賞

    2020.3   日本農芸化学会  

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  • 奨励賞

    2017.9   日本応用糖質科学会  

    中井 博之

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  • 2017年度大会トピックス賞

    2017.3   日本農芸化学会  

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  • 長瀬研究振興賞

    2016.4   公益財団法人 長瀬科学技術振興財団  

    中井 博之

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  • 安藤百福賞発明発見奨励賞

    2016.3   公益財団法人 安藤スポーツ・食文化振興財団  

    中井 博之

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  • 食の新潟国際賞 21世紀希望賞

    2014.10   公益財団法人 食の新潟国際賞財団  

    中井 博之

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  • インテリジェント・コスモス奨励賞

    2013.5   公益財団法人 インテリジェント・コスモス学術振興財団  

    中井 博之

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  • 酵素応用シンポジウム研究奨励賞

    2012.6   一般財団法人 天野エンザイム科学技術振興財団  

    中井 博之

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  • Poster Award

    2010.7   Plant Polysaccharide and Applied Glycoscience Workshop 2010  

    中井 博之

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  • 1st Poster Award

    2007.4   7th Carbohydrate Bioengineering Meeting  

    中井 博之

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  • Best Poster Award

    2004.7   Plant Polysaccharide Workshop  

    中井 博之

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  • 平成16年度大会記者会見報道用トピックス賞

    2004.3   日本農芸化学会  

    中井 博之

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Research Projects

  • 糖質の構造と生理活性の相関解明に向けた機能性糖質の創生

    Grant number：22K05437

    2022.4 - 2025.3

    System name：科学研究費助成事業

    Research category：基盤研究(C)

    Awarding organization：日本学術振興会

    中井 博之

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    Grant amount：\4290000 （ Direct Cost: \3300000 、 Indirect Cost：\990000 ）

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  • Screening of novel carbohydrate phosphorylase using carbohydrate assimilation modified Escherichia coli

    Grant number：19K05824

    2019.4 - 2022.3

    System name：Grants-in-Aid for Scientific Research

    Research category：Grant-in-Aid for Scientific Research (C)

    Awarding organization：Japan Society for the Promotion of Science

    Nakai Hiroyuki

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    Grant amount：\4290000 （ Direct Cost: \3300000 、 Indirect Cost：\990000 ）

    Phosphorylases are exolytic enzymes catalyzing phosphorolysis of particular glycosides to produce sugar 1-phosphate with strict substrate specificity. The reaction is reversible, enabling the practical synthesis of oligosaccharides. However, there is little variation among phosphorylases and this limits their utilization for the production of oligosaccharides. Therefore, it would be beneficial to identify phosphorylases with previously unreported substrate specificities. In this study, we performed screening of novel enzymes by bioinformatics method and metagenomics method specialized for novel phosphorylase using carbohydrate assimilation modified Escherichia coli.

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  • Screening of novel carbohydrate phosphorylase using metagenomics

    Grant number：16K07688

    2016.4 - 2019.3

    System name：Grants-in-Aid for Scientific Research

    Research category：Grant-in-Aid for Scientific Research (C)

    Awarding organization：Japan Society for the Promotion of Science

    NAKAI Hiroyuki

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    Grant amount：\4810000 （ Direct Cost: \3700000 、 Indirect Cost：\1110000 ）

    Phosphorylases are exolytic enzymes catalyzing phosphorolysis of particular glycosides to produce sugar 1-phosphate with strict substrate specificity. The reaction is reversible, enabling the practical synthesis of oligosaccharides. However, there is little variation among phosphorylases and this limits their utilization for the production of oligosaccharides. Therefore, it would be beneficial to identify phosphorylases with previously unreported substrate specificities. In this study, we developed a metagenomics screening method specialized for novel phosphorylase using E. coli with altered carbohydrate utilization.

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  • Studies on the energetically efficient metabolic pathway of N-glycans in intestinal bacteria

    Grant number：26440022

    2014.4 - 2017.3

    System name：Grants-in-Aid for Scientific Research

    Research category：Grant-in-Aid for Scientific Research (C)

    Awarding organization：Japan Society for the Promotion of Science

    NIHIRA Takanori, NAKAI Hiroyuki

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    Grant amount：\5200000 （ Direct Cost: \4000000 、 Indirect Cost：\1200000 ）

    The kinetic and structural analyses of β-1,4-mannosyl-N-acetyl-glucosamine phosphorylase which is a key enzyme in novel metabolic pathway for N-glycan where phosphorylase participates, were carried out to elucidate this metabolic pathway in intestinal bacteria. The enzymes from some microbes have strict regioselectivity and acceptor specificity against N-acetyl-glucasamine and N,N’-diacetyl-chitobiose as acceptors in reverse phosphorolysis. The three-dimensional structure of β-1,4-mannosyl-N-acetyl-glucosamine phosphorylase from Bacteroides thetaiotaomicron has not yet been determined. This structure analysis is carried out continuously now.
    To investigate of an uncharacterized gene which is predicted to participate in N-glycan metabolism existing close to phosphorylase gene, the hydrolytic reaction of the protein encoded by this gene was examined using various N-glycans as the substrate candidates. However, this protein did not show hydrolytic reaction.

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  • Screening of carbohydrate phosphorylases enabling practical synthesis of oligosaccharides

    Grant number：26850062

    2014.4 - 2016.3

    System name：Grants-in-Aid for Scientific Research

    Research category：Grant-in-Aid for Young Scientists (B)

    Awarding organization：Japan Society for the Promotion of Science

    Nakai Hiroyuki

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

    Phosphorylases are exolytic enzymes catalyzing phosphorolysis of particular glycosides to produce sugar 1-phosphate with strict substrate specificity. The reaction is reversible, enabling the practical synthesis of oligosaccharides. However, there is little variation among phosphorylases and this limits their utilization for the production of oligosaccharides. Therefore, it would be beneficial to identify phosphorylases with previously unreported substrate specificities. In this study, two phosphorylase homologues belonging to glycoside hydrolase family 130 are characterized to be novel phosphorylases showing distinct chain-length specificities toward β-1,2-oligomannan.

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  • Enzymactic synthesis of functional oligosaccharides by nocel carbohydrate phosphorylases

    Grant number：24780095

    2012.4 - 2014.3

    System name：Grants-in-Aid for Scientific Research

    Research category：Grant-in-Aid for Young Scientists (B)

    Awarding organization：Japan Society for the Promotion of Science

    NAKAI Hiroyuki

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    Grant amount：\4680000 （ Direct Cost: \3600000 、 Indirect Cost：\1080000 ）

    Phosphorylases are exolytic enzymes catalyzing phosphorolysis of particular glycosides to produce sugar 1-phosphate with strict substrate specificity. The reaction is reversible, enabling the practical synthesis of oligosaccharides. However, there is little variation among phosphorylases and this limits their utilization for the production of oligosaccharides. Therefore, it would be beneficial to identify phosphorylases with previously unreported substrate specificities. In this study, several bacterial phosphorylase homologues belonging to glycoside hydrolase family 65, 94, and 130 are characterized to be novel phosphorylases showing unreported substrate specificities. In addition, a variety of heterooligosaccharides were synthesized by the reverse phosphorolysis catalyzed by the novel phosphorylases.

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  • 新規糖質加リン酸分解酵素を活用した機能性オリゴ糖のライブラリー化

    Grant number：23880010

    2011.8 - 2013.3

    System name：科学研究費助成事業

    Research category：研究活動スタート支援

    Awarding organization：日本学術振興会

    中井 博之

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    Grant amount：\3250000 （ Direct Cost: \2500000 、 Indirect Cost：\750000 ）

    生体内糖質代謝に関与する糖質加リン酸分解酵素(ホスホリラーゼ)による糖質合成収率は極めて高く、産業上有用な酵素になり得る。しかしながら、既知のホスホリラーゼは14種類のみと報告例が少なく、今後生産可能なオリゴ糖のバリエーション拡大には、新たなホスホリラーゼの発見が必須であった。本研究では様々な生物種のゲノム情報を活用して、これまでに報告例のない新規なホスホリラーゼを見出し、各種酵素の糖受容体特異性を明らかにすることで、新規オリゴ糖のライブラリー化を試みた。まず真正細菌由来のホスホリラーゼ様タンパク質(Cphy1874、Cphy1019)をコードする遺伝子をPCR法により単離し、大腸菌による異種宿主発現系を確立した。Cphy1874はリン酸存在下でグルコース2分子がα-1,3結合したニゲロースを加リン酸分解すること、さらにβ-グルコース1-リン酸(糖供与体)とグルコース(糖受容体)を出発材料とした際はニゲロースを高収率合成することが分かった。本結果により、Cphy1874はこれまでに報告例のない新規加リン酸分解酵素ニゲロースホスホリラーゼであることが明らかになった。Cphy1019については、リン酸存在下で既知のグルコ2糖に対して加リン酸分解活性を示さなかったが、糖質合成反応にてL-ラムノースを糖受容体とした際にのみ合成活性を示した。反応生成物の構造を核磁気共鳴分光法にて確認したところ、3-O-α-D-グルコシル-L-ラムノースであったことから、Cphy1019は新規加リン酸分解酵素3-O-α-D-グルコシル-L-ラムノースホスホリラーゼであることが判明した。今回得られた両新規酵素の詳細な糖受容体特異性を調査することで、これまでに6個の新規α-1,3グルコシルヘテロ2糖の合成に成功している。

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Teaching Experience

  • 応用生命・食品科学セミナーI

    2024
    Institution name：新潟大学

  • 統合化学入門

    2024
    Institution name：新潟大学

  • 卒業論文I

    2023
    Institution name：新潟大学

  • 科学英語演習

    2023
    Institution name：新潟大学

  • 食品科学演習II

    2023
    Institution name：新潟大学

  • 卒業論文II

    2023
    Institution name：新潟大学

  • 食品科学演習I

    2023
    Institution name：新潟大学

  • 分析化学実験(農)

    2022
    Institution name：新潟大学

  • Topics in Food Sciences

    2022
    Institution name：新潟大学

  • 農学入門I

    2022
    Institution name：新潟大学

  • 米利用科学論

    2022
    Institution name：新潟大学

  • 農学入門II

    2022
    Institution name：新潟大学

  • 糖質科学論

    2021
    Institution name：新潟大学

  • スタディ・スキルズAIIc

    2021
    Institution name：新潟大学

  • スタディ・スキルズAIc

    2021
    Institution name：新潟大学

  • 応用生命・食品科学概論

    2021
    Institution name：新潟大学

  • 食品科学概論

    2020
    Institution name：新潟大学

  • 応用生命・食品科学セミナーⅡ

    2020
    Institution name：新潟大学

  • 農産食品学

    2018
    Institution name：新潟大学

  • 応用生命・食品科学概論

    2018
    -
    2021
    Institution name：新潟大学

  • 農学入門Ⅱ

    2018
    Institution name：新潟大学

  • 応用生命・食品科学特論

    2018
    Institution name：新潟大学

  • 基礎化学

    2017
    Institution name：新潟大学

  • 食と健康の科学

    2017
    Institution name：新潟大学

  • 農学入門Ⅰ

    2017
    -
    2018
    Institution name：新潟大学

  • 生物化学実験

    2016
    -
    2022
    Institution name：新潟大学

  • Topics in Food Sciences

    2016
    -
    2022
    Institution name：新潟大学

  • 食品安全学

    2016
    -
    2022
    Institution name：新潟大学

  • 食品製造学

    2016
    -
    2017
    Institution name：新潟大学

  • 自然科学総論Ⅳ

    2016
    Institution name：新潟大学

  • 米利用科学論

    2015
    -
    2022
    Institution name：新潟大学

  • 食品・栄養科学演習Ⅰ

    2015
    -
    2019
    Institution name：新潟大学

  • 食品・栄養科学演習Ⅱ

    2015
    -
    2018
    Institution name：新潟大学

  • 食品・栄養科学実験

    2015
    -
    2018
    Institution name：新潟大学

  • 実地見学

    2015
    -
    2016
    Institution name：新潟大学

  • 研究発表演習(中間発表)

    2015
    Institution name：新潟大学

  • 米科学論

    2015
    Institution name：新潟大学

  • 生命・食料科学セミナーBⅠ

    2015
    Institution name：新潟大学

  • 文献詳読Ⅰ

    2015
    Institution name：新潟大学

  • 生命・食料科学特定研究BⅠ

    2015
    Institution name：新潟大学

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