Studies on Acylase Activity and Microorganisms. XXIII. Purification of δ-Ornithine Acylase : 5-N-Acylornithine Amidohydrolase.

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Since KT 801 (Pseudomonas sp.) isolated from soil showed mardedly high δ-ornithine acylase (5-N-acylornithine amidohydrolase) activity, purification of the enzyme have been attempated. In the first place, cultural conditions for the production of this enzyme were investigated. As a result, it was confirmed that a medium containing 0.1% 5-N-benzoyl-L-ornithine, 1% peptone and some inorganic salts is most suitable for the enzyme production and that more δ-ornithine acylase is produced by shaken culture or submerged culture in jar fermentor than by stationary culture. Then, δ-ornithine acylase was extracted by means of freezing and thawing method from KT 801 cells. By this method, 60〜70% of the enzyme activity estimated in cell suspension was extracted, although only 5〜8% of cellular proteins was extracted. Subsequently, δ-ornithine acylase was purified by fractionation with ammonium sulfate and chromatography on DEAE cellulose and DEAE Sephadex A-50. The specific activity of the purified enzyme preparation was 41,280 μM/hr./mg. and it was represented abut 300 fold purification over the original cell suspention. This enzyme preparation gave single peak in Tiselius electrophoresis or analytical ultracentrifuge.
社団法人日本薬学会の論文
1967-10-25