Characterization of Glycoside Hydrolase Family 6 Enzymes from Coprinopsis cinerea

Yuan LIU; Kiyohiko IGARASHI; Satoshi KANEKO; Takashi TONOZUKA; Masahiro SAMEJIMA; Kiyoharu FUKUDA; Makoto YOSHIDA

doi:10.1271/bbb.80888

Biochemistry & Molecular Biology Notes

Characterization of Glycoside Hydrolase Family 6 Enzymes from Coprinopsis cinerea

Yuan LIU, Kiyohiko IGARASHI, Satoshi KANEKO, Takashi TONOZUKA, Masahiro SAMEJIMA, Kiyoharu FUKUDA, Makoto YOSHIDA

Author information

Yuan LIU
Department of Environmental and Natural Resource Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
Kiyohiko IGARASHI
Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo
Satoshi KANEKO
Food Biotechnology Division, National Food Research Institute
Takashi TONOZUKA
Department of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
Masahiro SAMEJIMA
Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo
Kiyoharu FUKUDA
Department of Environmental and Natural Resource Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
Makoto YOSHIDA
Department of Environmental and Natural Resource Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology

Keywords: Coprinopsis cinerea, glycoside hydrolase family 6, basidiomycete, cellulose degradation, cellobiohydrolase

JOURNAL FREE ACCESS

2009 Volume 73 Issue 6 Pages 1432-1434

DOI https://doi.org/10.1271/bbb.80888

View "Advance Publication" version (June 7, 2009).

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Abstract

Recombinants, Cel6 from Coprinopsis cinerea (CcCel6)A, -B, and -C, were expressed by Escherichia coli. These enzymes produced cellobiose from phosphoric acid-swollen cellulose. When Avicel was used as the substrate, CcCel6A showed higher activity toward the substrate than CcCel6B or -C. In reaction with carboxymethylcellulose, CcCel6B and -C hydrolyzed the substrate, whereas CcCel6A failed to react.

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