Tatsuji Sakamoto
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
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Research Interests
Tatsuji Sakamoto has a total of 1 co-authors. Here are the top co-authors by number of shared publications:
Jean-François Thibault
Division of Applied Biochemistry, Graduate School of Agriculture and Biological Science, Osaka Prefecture University, Osaka 599-8531, Japan,1 and Unité de Recherche sur les Polysaccharides, leurs Organisations et Interactions, Institut National de la Recherche Agronomique, BP 71627-44316 Nantes Cedex 3, France2
1 shared publication
Latest Publications
- Open Access
- 1 July 2001
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 67 (7) , 3319-3321
Exo-Arabinanase of Penicillium chrysogenum Able To Release Arabinobiose from α-1,5- l -Arabinan
An exo-arabinanase, designated Abnx, was purified from a culture filtrate of Penicillium chrysogenum 31B by ammonium sulfate precipitation, anion-exchange chromatography, and hydrophobic chromatography. Abnx had an apparent molecular mass of 47 kDa. The enzyme released only arabinobiose from the nonreducing terminus of α-1,5- l -arabinan and showed no activity towards p -nitrophenyl-α- l -arabinofuranoside and α-1,5- l -arabinofuranobiose. Abnx is the first enzyme with this mode of action.
- 1 July 2001
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 67 (7) , 3319-3321
Open AccessExo-Arabinanase of Penicillium chrysogenum Able To Release Arabinobiose from α-1,5- l -Arabinan
An exo-arabinanase, designated Abnx, was purified from a culture filtrate of Penicillium chrysogenum 31B by ammonium sulfate precipitation, anion-exchange chromatography, and hydrophobic chromatography. Abnx had an apparent molecular mass of 47 kDa. The enzyme released only arabinobiose from the nonreducing terminus of α-1,5- l -arabinan and showed no activity towards p -nitrophenyl-α- l -arabinofuranoside and α-1,5- l -arabinofuranobiose. Abnx is the first enzyme with this mode of action.