Purification and Characterization of Extracellular Alkaline Phosphatase from an Alkalophilic Bacterium(Biological Chemistry)

概要

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From some Japanese soil, we isolated a strain of alkalophilic bacterium, Bacillus sp. OK-1, that excreted alkaline phoshatase into the culture broth. From the cell-free supernatant, the enzyme was successively purified by acetone fractionation, Sephadex column chromatography, and DEAE-cellulose column chromatography. The final preparation thus obtained showed only a single band when analyzed by SDS-polyacrylamide gel electrophoresis. The molecular weight was estimated as 108,000, and was composed of two subunits having the same molecular weight. The purified enzyme had a pH optimum of 11 and was fairly stable between pH 5〜12. This enzyme was inactivated by EDTA. Cobalt ions restored the enzyme activity. The Km was 0.037 mM. On the basis of its properties, this metalloenzyme seems to be a novel extracellular alkaline phosphatase.
社団法人日本農芸化学会の論文
1988-07-23