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Study on the role of uncharacterized enzymes belonging to glycoside hydrolase family 131 in biomass degradation

Research Project

Project/Area Number 26660277
Research Category

Grant-in-Aid for Challenging Exploratory Research

Allocation TypeMulti-year Fund
Research Field Environmental agriculture(including landscape science)
Research InstitutionTokyo University of Agriculture and Technology

Principal Investigator

Tonozuka Takashi  東京農工大学, (連合)農学研究科(研究院), 准教授 (50285194)

Co-Investigator(Renkei-kenkyūsha) YOSHIDA MAKOTO  東京農工大学, 大学院農学研究院, 准教授 (30447510)
Project Period (FY) 2014-04-01 – 2016-03-31
Project Status Completed (Fiscal Year 2015)
Budget Amount *help
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Keywordsバイオマス / 担子菌 / 糖質加水分解酵素
Outline of Final Research Achievements

This study focuses on enzymes belonging to glycoside hydrolase family 131, CcGH131A and CcGH131B, from a basidiomycete, Coprinopsis cinerea. A heterologous expression system of CcGH131A using Pichia pastoris was constructed, and the crystal structure of CcGH131A in a complex with ligand was determined. The cDNA of CcGH131B was cloned, and a heterologous expression system of CcGH131A using Escherichia coli was constructed. The protein was crystallized and the structure was determined. An experiment using fluorescence spectroscopy was performed to analyze the interaction between the proteins and polysaccharides. The results suggest that the substrate specificities of CcGH131A and CcGH131B are expected to be markedly different.

Report

(3 results)
  • 2015 Annual Research Report   Final Research Report ( PDF )
  • 2014 Research-status Report
  • Research Products

    (8 results)

All 2016 2015

All Journal Article (6 results) (of which Peer Reviewed: 6 results,  Acknowledgement Compliant: 5 results,  Open Access: 1 results) Presentation (2 results)

  • [Journal Article] A Surface Loop in the N-Terminal Domain of <i>Pedobacter heparinus </i>Heparin Lyase II is Important for Activity2016

    • Author(s)
      Mori, M., Ichikawa, M., Kiguchi, Y., Miyazaki, T., Hattori, M., Nishikawa, A. and Tonozuka, T.
    • Journal Title

      Journal of Applied Glycoscience

      Volume: 63 Issue: 1 Pages: 7-11

    • DOI

      10.5458/jag.jag.JAG-2015_019

    • NAID

      130005126301

    • ISSN
      1344-7882, 1880-7291
    • Related Report
      2015 Annual Research Report
    • Peer Reviewed / Open Access
  • [Journal Article] A glycoside hydrolase family 31 dextranase with high transglucosylation activity from Flavobacterium johnsoniae2016

    • Author(s)
      Gozu, Y., Ishizaki, Y., Hosoyama, Y., Miyazaki, T., Nishikawa, A. and Tonozuka, T.
    • Journal Title

      Biosci. Biotechnol. Biochem.

      Volume: 印刷中 Issue: 8 Pages: 1562-1567

    • DOI

      10.1080/09168451.2016.1182852

    • Related Report
      2015 Annual Research Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Journal Article] Structural and biochemical characterization of novel bacterial α-galactosidases belonging to glycoside hydrolase family 312015

    • Author(s)
      Takatsugu Miyazaki, Yuichi Ishizaki, Megumi Ichikawa, Atsushi Nishikawa and Takashi Tonozuka
    • Journal Title

      Biochemical Journal

      Volume: in press Issue: 1 Pages: 145-158

    • DOI

      10.1042/bj20150261

    • Related Report
      2015 Annual Research Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Journal Article] Crystal structure and mutational analysis of isomalto-dextranase, a member of glycoside hydrolase family 272015

    • Author(s)
      Okazawa, Y., Miyazaki, T., Yokoi, G., Ishizaki, Y., Nishikawa, A. and Tonozuka, T.
    • Journal Title

      J. Biol. Chem.

      Volume: 290 Issue: 43 Pages: 26339-26349

    • DOI

      10.1074/jbc.m115.680942

    • Related Report
      2015 Annual Research Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Journal Article] The side chain of a glycosylated asparagine residue is important for the stability of isopullulanase.2015

    • Author(s)
      Takatsugu Miyazaki, Hiroyuki Yashiro, Atsushi Nishikawa and Takashi Tonozuka
    • Journal Title

      Journal of Biochemistry

      Volume: 157 Issue: 4 Pages: 225-234

    • DOI

      10.1093/jb/mvu065

    • Related Report
      2014 Research-status Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Journal Article] Crystal structure and substrate-binding mode of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8.2015

    • Author(s)
      Takatsugu Miyazaki, Megumi Ichikawa, Hitoshi Iino, Atsushi Nishikawa and Takashi Tonozuka
    • Journal Title

      Journal of Structural Biology

      Volume: 190 Issue: 1 Pages: 21-30

    • DOI

      10.1016/j.jsb.2015.02.006

    • Related Report
      2014 Research-status Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Presentation] 担子菌Coprinopsis cinerea由来タンパク質CcGH131BのX線結晶構造解析2016

    • Author(s)
      奥山舜朔、林昌宏、砂川直輝、石田卓也、五十嵐圭日子、吉田誠、西河淳、殿塚隆史
    • Organizer
      日本農芸化学会
    • Place of Presentation
      札幌コンベンションセンター(北海道札幌市白石区)
    • Year and Date
      2016-03-28
    • Related Report
      2015 Annual Research Report
  • [Presentation] 担子菌Coprinopsis cinerea由来機能未知タンパク質CcGH131Aの結晶構造解析2016

    • Author(s)
      林昌宏、奥山舜朔、田中祐太郎、田村瑞、砂川直輝、石田卓也、梅澤究、吉田誠、五十嵐圭日子、西河淳、殿塚隆史
    • Organizer
      2015年度量子ビームサイエンスフェスタ
    • Place of Presentation
      つくば国際会議場(茨城県つくば市)
    • Year and Date
      2016-03-15
    • Related Report
      2015 Annual Research Report

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Published: 2014-04-04   Modified: 2017-05-10  

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