Purification and Some Properties of Neuraminidase from the Culture Medium of Bacteroides melaninogenicus ATCC 15930 Isolated from Human Gingival Crevice

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The activity of bacterial neuraminidase in the oral cavity may have an important role in oral disease, but details of its biological function are unknown. This study deals with the purification and some properties of neuraminidase from culture medium of <I>Bacteroides melaninogenicus</I> ATCC 15930 which was isolated from human gingival crevice. Neuraminidase secreted by the cells into the culture medium was isolated and purified by procedures involving ultra filtration, DEAE-Sephacel column chromatography, fast protein liquid chromatography (FPLC), and high performance liquid chromatography (HPLC). The molecular weight of the purified enzyme was estimated to be 83, 000 by HPLC using a G4000SW column, and the isoelectric point was 5.1. The optimal pH of the purified enzyme activity was pH 4.8. A single protein band having a molecular weight of about 46, 000 was obtained by disc electrophoresis on polyacrylamide gel containing 0.1% sodium dodecyl sulfate. These findings suggest that the purified enzymeis formed of dimers. The substrate specifity of the enzyme is under investigation.
有限責任中間法人日本口腔衛生学会の論文