次世代木材防腐剤の開発
メンバー: 吉田誠
分野: 森林圏科学
所属: 農学研究院
キーワード: バイオマス変換、木材保存、木材腐朽菌、バイオ燃料、セルロース、ヘミセルロース、リグニン
研究概要
木材を腐朽から守るために使用される木材防腐剤は、多様な微生物に毒性を示す化合物に基づく作用機序を利用するため木材腐朽真菌類に特異的に毒性を発現させることは不可能である。
我々は、真菌が生産するセルロース結合性ピラノース脱水素酵素(PDH)が、細菌由来のピロロキノリンキノン(PQQ)を補酵素とすること、すなわち細菌から真菌へのPQQの供給が木材分解で重要な役割を果たすことを見いだした。本課題ではこの細菌から真菌へのPQQ供給系の遮断という全く新しいコンセプトに基づき、腐朽現象特異的に効果を示す木材防腐剤の開発を目指す。具体的には、PDHにおけるPQQ結合阻害剤を探索し、それをベースとした防腐性を創出する。さらに、PDHの生理的機能およびPQQ供給細菌を特定し、防腐性能発現機構の全貌を解明する。本課題は科研費基盤(B)[課題番号15H04526]のサポートにより実施されている。
主要論文・参考事項
1) Kiwamu Umezawa, Kouta Takeda, Takuya Ishida, Naoki Sunagawa, Akiko Makabe, Kazuo Isobe, Keisuke Koba, Hiroyuki Ohno, Masahiro Samejima, Nobuhumi Nakamura, Kiyohiko Igarashi, Makoto Yoshida*. A novel pyrroloquinoline quinone-dependent 2-keto-D-glucose dehydrogenase from Pseudomonas aureofaciens. Journal of Bacteriology 197, 1322-1329 (2015)
2) Kouta Takeda, Hirotoshi Matsumura, Takuya Ishida, Masahiro Samejima, Hiroyuki Ohno, Makoto Yoshida*, Kiyohiko Igarashi, and Nobuhumi Nakamura. Characterization of a Novel PQQ-Dependent Quinohemoprotein Pyranose Dehydrogenase from Coprinopsis cinerea Classified into Auxiliary Activities Family 12 in Carbohydrate-Active Enzymes. PLOS ONE 10, e0115722 (2015)
3) Hirotoshi Matsumura, Kiwamu Umezawa, Kouta Takeda, Naohisa Sugimoto, Takuya Ishida, Masahiro Samejima, Hiroyuki Ohno, Makoto Yoshida*, Kiyohiko Igarashi, Nobuhumi Nakamura. Discovery of a eukaryotic pyrroloquinoline quinone-dependent oxidoreductase belonging to a new auxiliary activity family in the database of carbohydrate-active enzymes. PLOS ONE 9, e104851 (2014)
お問い合わせ先
東京農工大学・先端産学連携研究推進センター
urac[at]ml.tuat.ac.jp([at]を@に変換してください)
Development of next-generation wood preservatives
Research members: Makoto Yoshida PhD.
Research fields: Forest and forest products science
Departments: Institute of Agriculture
Keywords: biomass conversion, wood protection, wood rotting fungi, biofuel, cellulose, hemicellulose, lignin
Summary
Wood preservatives are used to protect wood materials from deterioration by wood rotting fungi. Their mechanisms of action are normally based on the toxic compounds for various microorganisms, and thus, the development of next-generation preservatives which shows high specificity to wood decay would be needed from the viewpoint of environmental impact and public health.
Recently, we found a novel cellulose-binding pyranose dehydrogenase (PDH), and showed that PDH required pyrroloquinoline quinone (PQQ) as a cofactor. Since PQQ is well known to be produced only by limeted bacterial species, the transfer of PQQ from bacteria to fungi would be important to triger the catalytic reaction of this type of enzymes. In the present study, we have attempted to develop wood preservatives which shows high specificity to wood decay phenomena based on block of PQQ-transfer pathway from bacteria to fungi. The research is financially supported by JSPS KAKENHI Grant-in-Aid for Scientific Research (B) [Grant no.15H04526].
Reference articles and patents
1) Kiwamu Umezawa, Kouta Takeda, Takuya Ishida, Naoki Sunagawa, Akiko Makabe, Kazuo Isobe, Keisuke Koba, Hiroyuki Ohno, Masahiro Samejima, Nobuhumi Nakamura, Kiyohiko Igarashi, Makoto Yoshida*. A novel pyrroloquinoline quinone-dependent 2-keto-D-glucose dehydrogenase from Pseudomonas aureofaciens. Journal of Bacteriology 197, 1322-1329 (2015)
2) Kouta Takeda, Hirotoshi Matsumura, Takuya Ishida, Masahiro Samejima, Hiroyuki Ohno, Makoto Yoshida*, Kiyohiko Igarashi, and Nobuhumi Nakamura. Characterization of a Novel PQQ-Dependent Quinohemoprotein Pyranose Dehydrogenase from Coprinopsis cinerea Classified into Auxiliary Activities Family 12 in Carbohydrate-Active Enzymes. PLOS ONE 10, e0115722 (2015)
3) Hirotoshi Matsumura, Kiwamu Umezawa, Kouta Takeda, Naohisa Sugimoto, Takuya Ishida, Masahiro Samejima, Hiroyuki Ohno, Makoto Yoshida*, Kiyohiko Igarashi, Nobuhumi Nakamura. Discovery of a eukaryotic pyrroloquinoline quinone-dependent oxidoreductase belonging to a new auxiliary activity family in the database of carbohydrate-active enzymes. PLOS ONE 9, e104851 (2014)
Contact
University Research Administration Center(URAC),
Tokyo University of Agriculture andTechnology
urac[at]ml.tuat.ac.jp
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