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Author Sakai, Shuzo ♦ Yamanaka, Kei
Source J-STAGE
Content type Text
Publisher Japan Society for Bioscience, Biotechnology, and Agrochemistry
Language English
Abstract The crystalline D-mannitol dehyrogenase (D-mannitol:NAD oxidoreductase, EC 1.1.1.67) catalyzed the reversible reduction of D-fructose to D-mannitol. D-Sorbitol was oxidized only at the rate of 4%0 of the activity for D-mannitol. The enzyme was inactive for all of four pentitols and their corresponding 2-ketopentoses. The apparent optimal pH for the reduction of D-fructose or the oxidation of D-mannitol was 5.35 or 8.6, respectively. The Michaelis constants were 0.035M for D-fructose and 0.020M for D-mannitol. The enzyme was also found to be specific for NAD. The Michaelis constans were $1×10^{-5}M$ for $NADH_{2}$ and $2.7×10^{-4}M$ for NAD.
ISSN 00021369
Learning Resource Type Article
Publisher Date 1968-01-01
e-ISSN 18811280
Journal Agricultural and Biological Chemistry(bbb1961)
Volume Number 32
Issue Number 7
Page Count 6
Starting Page 894
Ending Page 899


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