Updated on 2026/07/21
博士(学術) ( 2008.7 三重大学 )
微生物
タンパク質・酵素
フォールディング
構造安定性
calorimetry
Life Science / Applied biochemistry
Life Science / Applied microbiology
Environmental Science/Agriculture Science / Environmental agriculture
Niigata University Faculty of Agriculture
2011.4
Kuwansei Univ. Graduate School of Science and Technology
2008.8 - 2011.3
Niigata University Graduate School of Science and Technology Life and Food Sciences Applied Life and Food Sciences Associate Professor
2016.4
Niigata University Graduate School of Science and Technology Life and Food Sciences Assistant Professor
2011.4 - 2016.3
Niigata University Abolition organization Applied Biological Chemistry Assistant Professor
2011.4 - 2016.3
Niigata University Graduate School of Science and Technology Life and Food Sciences Assistant Professor
2011.4 - 2016.3
Mie Univ. Graduate school of Bioresources 博士後期課程
2005.4 - 2008.7
THE BIOPHYSICAL SOCIETY OF JAPAN
THE JAPANESE BIOCHEMICAL SOCIETY
The Protein Society (USA)
PROTEIN SCIENCE SOCIETY OF JAPAN
THE JAPAN SOCIETY OF CALORIMETRY AND THERMAL ANALYSIS
JAPAN SOCIETY FOR BIOSCIENCE, BIOTECHNOLOGY, AND AGROCHEMISTRY
日本キチン・キトサン学会
Olga Gladyshchuk, Masaki Yoshida, Koume Togashi, Hayuki Sugimoto, Kazushi Suzuki
The Journal of General and Applied Microbiology 70 ( 1 ) 30 - 42 2024.7
Unfolding of the bacterial fibronectin type III domains from family 18 glycoside hydrolases Reviewed
Otagaki T, Nakajima A, Suzuki K, Sugimoto H
Chitin Chitosan Research 30 ( 1 ) 9 - 19 2024.4
Chitinase system of Aeromonas salmonicida, and characterization of enzymes involved in chitin degradation Reviewed International journal
Iuliia Pentekhina, Tatsuyuki Hattori, Dinh Minh Tran, Mizuki Shima, Takeshi Watanabe, Hayuki Sugimoto, Kazushi Suzuki
Bioscience, Biotechnology, and Biochemistry 84 ( 9 ) 1936 - 1947 2020.9
Hayuki Sugimoto, Yuichi Nakajima, Ayaka Motoyama, Erina Katagiri, Takeshi Watanabe, Kazushi Suzuki
Biopolymers 111 ( 1 ) e23339 2020.1
A novel chitin-binding mode of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12 revealed by solid-state NMR Reviewed
Tanaka, Hiroki, Akutsu, Hideo, Yabuta, Izumi, Hara, Masashi, Sugimoto, Hayuki, Ikegami, Takahisa, Watanabe, Takeshi, Fujiwara, Toshimichi
FEBS LETTERS 592 ( 18 ) 3173 - 3182 2018.9
Identification and characterization of chitinolytic bacteria isolated from a freshwater lake Reviewed
Dinh Minh Tran, Hayuki Sugimoto, Dzung Anh Nguyen, Takeshi Watanabe, Kazushi Suzuki
Bioscience, Biotechnology and Biochemistry 82 ( 2 ) 343 - 355 2018
Masuda Y, Miyake H, Tanaka A, Sugimoto H
Netsu Sokutei 44 ( 4 ) 135 - 138 2017
Differences in the roles of the two surface-exposed tyrosine residues, Y240 and Y481, of Serratia marcescens chitinase B during processive degradation of crystalline chitin Reviewed
Hayuki Sugimoto, Keita Nakamura, Yuji Nishino, Yuta Idezawa, Akiko Fujinuma, Kazushi Suzuki, Takeshi Watanabe
JOURNAL OF GENERAL AND APPLIED MICROBIOLOGY 61 ( 6 ) 255 - 261 2016
Analysis of subfamily C chitinases in bacterial glycoside hydrolase family 18 Reviewed
21 ( 3 ) 209 - 218 2015.11
Two-way traffic of glycoside hydrolase family 18 processive chitinases on crystalline chitin Reviewed
Kiyohiko Igarashi, Takayuki Uchihashi, Taku Uchiyama, Hayuki Sugimoto, Masahisa Wada, Kazushi Suzuki, Shohei Sakuda, Toshio Ando, Takeshi Watanabe, Masahiro Samejima
NATURE COMMUNICATIONS 5 3975 2014.6
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase Reviewed
Hayuki Sugimoto, Yasuo Noda, Shin-ichi Segawa
JOURNAL OF MOLECULAR BIOLOGY 412 ( 2 ) 304 - 315 2011.9
Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase Reviewed
Hayuki Sugimoto, Miho Nakaura, Shigenori Nishimura, Shuichi Karita, Hideo Miyake, Akiyoshi Tanaka
PROTEIN SCIENCE 18 ( 8 ) 1715 - 1723 2009.8
Stabilization mechanism of chloride ion on thermal denaturation of Arthrobacter sarcosine oxidase Reviewed
Sugimoto H, Nishiya Y, Miyake H, Tanaka A
Netsu Sokutei 35 76 - 80 2008
Thermodynamic effects of disulfide bond on thermal unfolding of the starch-binding domain of Aspergillus niger glucoamylase Reviewed
Hayuki Sugimoto, Miho Nakaura, Yoshie Kosuge, Kunio Imai, Hideo Miyake, Shuichi Karita, Akiyoshi Tanaka
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 71 ( 6 ) 1535 - 1541 2007.6
TANAKA Akiyoshi, SUGIMOTO Hayuki, MUTA Yuko, MIZUNO Takafumi, SENOO Keishi, OBATA Hitoshi, INOUYE Kuniyo
Bioscience, Biotechnology, and Biochemistry 67 ( 1 ) 207 - 210 2003.1
Regulation of the chitin degradation and utilization system by the ChiX small RNA in Serratia marcescens 2170 Reviewed
Kazushi Suzuki, Mari Shimizu, Naomi Sasaki, Chisana Ogawa, Haruka Minami, Hayuki Sugimoto, Takeshi Watanabe
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 80 ( 2 ) 376 - 385 2016.2
Construction of a CBP2l-defective mutant of Serratia marcescens 2170 Reviewed
SUGIMOTO Hayuki
21 ( 2 ) 46 - 51 2015
- Reviewed
SUGIMOTO Hayuki
応用糖質科学 4 107 - 112 2014
Construction and basic characterization of deletion mutants of the genes involved in chitin utilization by Serratia marcescens 2170 Reviewed
Shinya Takanao, Syouta Honma, Takuma Miura, Chisana Ogawa, Hayuki Sugimoto, Kazushi Suzuki, Takeshi Watanabe
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 78 ( 3 ) 524 - 532 2014
Identification of a Csr system in Serratia marcescens 2170 Reviewed
Manabu Ito, Kazuki Nomura, Hayuki Sugimoto, Takeshi Watanabe, Kazushi Suzuki
JOURNAL OF GENERAL AND APPLIED MICROBIOLOGY 60 ( 2 ) 79 - 88 2014
Involvement of Gln679, in addition to Trp687, in chitin-binding activity of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12 Reviewed
Masashi Hara, Hayuki Sugimoto, Michio Uemura, Ken-ichi Akagi, Kazushi Suzuki, Takahisa Ikegami, Takeshi Watanabe
JOURNAL OF BIOCHEMISTRY 154 ( 2 ) 185 - 193 2013.8
Regulation of Chitinase Production by the 5 '-Untranslated Region of the ybfM in Serratia marcescens 2170 Reviewed
Tadayuki Toratani, Kazushi Suzuki, Mari Shimizu, Hayuki Sugimoto, Takeshi Watanabe
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 76 ( 10 ) 1920 - 1924 2012.10
Phosphocholine-Containing Glycosyl Inositol-Phosphoceramides from Trichoderma viride Induce Defense Responses in Cultured Rice Cells Reviewed
Ryosuke Uchiyama, Kazuhiro Aoki, Hayuki Sugimoto, Nobuko Taka, Takane Katayama, Saki Itonori, Mutsumi Sugita, Fang-Sik Che, Hidehiko Kumagai, Kenji Yamamoto
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 73 ( 1 ) 74 - 78 2009.1
Structural and thermodynamic analyses of solute-binding protein from Bifidobacterium longum specific for core 1 disaccharide and lacto-N-biose I Reviewed
Ryuichiro Suzuki, Jun Wada, Takane Katayama, Shinya Fushinobu, Takayoshi Wakagi, Hirofumi Shoun, Hayuki Sugimoto, Akiyoshi Tanaka, Hidehiko Kumagai, Hisashi Ashida, Motomitsu Kitaoka, Kenji Yamamoto
JOURNAL OF BIOLOGICAL CHEMISTRY 283 ( 19 ) 13165 - 13173 2008.5
2P-079 Influences of the disulfide bond of the starch-binding domain of glucoamylase on the protein stability and refolding(The 46th Annual Meeting of the Biophysical Society of Japan)
Sugimoto Hayuki, Nakaura Miho, Nishimura Shigenori, Karita Shuichi, Miyake Hideo, Tanaka Akiyoshi
Seibutsu Butsuri 48 S87 2008
化学便覧 基礎編 改訂6版
日本化学会（ Role： Contributor , 10章「熱的性質」 6.4 高分子）
丸善出版 2021.1 （ ISBN:9784621305218 ）
熱量測定・熱分析ハンドブック
日本熱測定学会（ Role： Contributor , 5章 4.31 熱量測定とNMR）
丸善 2020.8 （ ISBN:9784621305072 ）
Stability of Lytic Polysaccharide Monooxygenases, LPMOs
Hayuki SUGIMOTO
KAGAKU TO SEIBUTSU 63 ( 4 ) 154 - 159 2025.4
Bacterial chitinases ad chitin degradation and utulization system
渡邉剛志, 杉本華幸, 鈴木一史
キチン・キトサン研究 20 ( 2 ) 2014
Development of a calorimetric analysis method to assess the degradation capacity of an insoluble substrate, chitin, by bacteria.
Grant number：24K09179
2024.4 - 2027.3
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
Grant amount：\4550000 （ Direct Cost: \3500000 、 Indirect Cost：\1050000 ）
Hyperactivation of redox enzymes in confined nano-environments
Grant number：18H01719
2018.4 - 2021.3
System name：Grants-in-Aid for Scientific Research
Research category：Grant-in-Aid for Scientific Research (B)
Awarding organization：Japan Society for the Promotion of Science
Tsujimura Seiya
Grant amount：\17550000 （ Direct Cost: \13500000 、 Indirect Cost：\4050000 ）
We demonstrated the hyperactivation of redox enzymes and the improvement of their durability by utilizing a meso-reaction field (=electrode) with a scale of several tens of nanometers. We elucidated the complex interaction between microspace, enzymes, water, and ions, and we clarified the effects of mesostructure and environmental factors in the space on the enzymes. In this way, we have provided a novel design for controlling nanospace and solution environment around the enzyme beyond the conventional morphology control. Furthermore, we developed porous electrode materials suitable for new enzymatic electrode reactions, leading a dramatic improvement in the performance of enzyme-based bioelectronics devices.
Elucidation of the mechanism underlying processive hydrolysis of crystalline chitin by bacterial chitinases.
Grant number：15K07355
2015.4 - 2018.3
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
Watanabe Takeshi, IGARASHI Kiyohiko, SUZUKI Kazushi, SUGIMOTO Hayuki
Grant amount：\4940000 （ Direct Cost: \3800000 、 Indirect Cost：\1140000 ）
The ultimate goal of this research is proposition of the universal and evolved model of the mechanism for crystalline chitin degradation and utilization by chitinolytic bacteria. Therefore, "the role of the protein (CBP21) that promote degradation of crystalline chitin", "the importance of CBP21 for the biological and ecological function of the chitinolytic bacteria", "the mechanism for biodegradation of α-chitin that exists in nature more abundantly" were studied. As a results, it became clear that CBP21 is especially important for degradation and utilization of chitin close to natural condition, an amino acid residue with aromatic ring of big resonating structure at the entrance of the catalytic cleft of chitinase is very important for hydrolysis of highly crystalline chitin substrate, and that one chitinase molecule jump to another chitin chain in different orientation and begins hydrolysis in opposite direction.
Elucidation of the role of aromatic amino acid residues in crystalline chitin hydrolysis and development to the mechanism of a-chitin hydrolysis
Grant number：24580104
2012.4 - 2015.3
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
WATANABE TAKESHI, IGARASHI Kiyohiko, SUZUKI Kazushi, SUGIMOTO Hayuki
Grant amount：\5460000 （ Direct Cost: \4200000 、 Indirect Cost：\1260000 ）
Chitin is a crystalline and rigid structural polysaccharide present in a variety of organisms. Elucidation of the mechanism underlying in the enzymatic degradation of crystalline chitin is very important not only from enzymological and biological view points, but also for utilization of biomass resources. In this study, critical roles of the aromatic amino acid residues, which are present on the surface of chitinase molecule and inside of its catalytic cleft, in processive hydrolysis of crystalline chitin was demonstrated.
Elucidation of the denatured structure of protein in equilibrium with the native one under a physiological condition.
Grant number：21570173
2009 - 2011
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
SEGAWA Shin-ichi, NODA Yasuo, YUTANI Katsuhide, SUGIMOTO Hayuki
Grant amount：\4810000 （ Direct Cost: \3700000 、 Indirect Cost：\1110000 ）
We have studied partially ordered structures remaining in unstructured disulfide-deficient variants of lysozyme by means of NMR and H/D exchange methods. In this residual structure, two residues of I55 and L56 involved in the bottom of the α-sheet were located in a hydrophobic pocket formed with A, B and C-helices in the β-domain. Lysozyme folding appears to be initiated around this site. On the other hand, H/D exchange reactions were studied in the native state of pyrrolidone carboxyl peptidase(PCP). The native structure was found to be divided into two domains by structural changes near at the residue 70.
基質をスライドさせて連続反応を行う結晶性多糖分解酵素・キチナーゼの作動機構の 解明
杉本華幸
Authorship：Principal investigator Grant type：Competitive
応用微生物学
Institution name：新潟大学農学部
遺伝子工学
Institution name：新潟大学農学部
微生物学実験
Institution name：新潟大学農学部
自然科学総論IV
地域交流ｻﾃﾗｲﾄ実習
生物化学I
土壌学概論
スタディ・スキルズAIb
統合化学入門
スタディ・スキルズAIIb
Topics in Biotechnology and Biochemistry
応用生命科学セミナー
微生物の物理化学
醸造学
スタディ・スキルズAIc
スタディ・スキルズAIIc
応用生命科学演習Ⅱ
卒業論文Ⅱ
応用生命科学実験
科学英語演習
卒業論文Ⅰ
応用生命科学演習Ⅰ
Topics in Biotechnology and Biochemistry
農学入門Ⅱ
農学入門Ⅰ
食品科学概論
応用生命・食品科学セミナーⅠ
応用生命・食品科学特論
分子微生物学特論
日本酒学A-2
日本酒学A-1
生命を知る
応用微生物学
基礎化学
微生物機能学
応用生命・食品科学概論
遺伝子工学
醸造学
微生物学実験
分子生命科学演習Ⅰ
分子生命科学演習Ⅱ
分子生命科学実験
