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Author Takasaki, Yoshiyuki ♦ Takano, Shuntaro
Source J-STAGE
Content type Text
Publisher Japan Society for Bioscience, Biotechnology, and Agrochemistry
Language English
Abstract Crude mannose isomerase preparation from Xanthomonas rubrilineans S-48 which converts D-mannose to D-fructose was further purified by ammonium sulfate fractionation and DEAE-cellulose column chromatography. The specific activity of the purified enzyme solution was about 35-fold of original crude preparation. By using this purified enzyme solution, several enzymatic properties were investigated. (1) The Michaelis constant was $1.2×10^{-2}M.$ (2) The enzyme was sensitive against temperature, but $Ca^{++}$ protected the enzyme to some extent from the effect of temperature. (3) The enzyme was stable in the pH range from 6 to 9. (4) The enzyme was not inhibited by glucose, xylose, mannitol, sorbitol, mannonic acid, mannuronic acid and so on, but strongly inhibited by D-arabinose and L-fucose, and Ki values of these inhibitors were $1.1×10^{-2}M$ and $7.1×10^{-4}M$ respectively.
ISSN 00021369
Learning Resource Type Article
Publisher Date 1964-01-01
e-ISSN 18811280
Journal Agricultural and Biological Chemistry(bbb1961)
Volume Number 28
Issue Number 9
Page Count 5
Starting Page 605
Ending Page 609


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