Purification and Properties of β-Fructofuranosidase from Clostridium perfringens
1997
Ishimoto, Makoto | Nakamura, Atsuko
β-Fructofuranosidase [EC 3.2.1.26] in Clostridium perfringens was induced in the presence of sucrose and suppressed in the presence of glucose or maltose. The enzyme seems to be present in protoplasm in a soluble state. The β-fructofuranosidase from C. perfringens cells grown on sucrose was purified by ammonium sulfate precipitation, DEAE-cellulose chromatography, Sephadex G-150 gel filtration, and hydroxylapatite chromatography to a homogeneous state. The molecular weight was 37,000 by gel filtration using Sephadex G-150 and by SDS-polyacrylamide gel electrophoresis. The amino acid composition is not much different from those of other microorganisms, but the Glx content was a little higher. The enzyme was inhibited by heavy metals, such as Hg² ⁺, Cu² ⁺, and Ag⁺, as well as pCMB; the activity was restored by incubating with mercaptoethanol. Fructose and amines including Tris and aniline had inhibitory effects.
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