Dehydroacetic acid hydrolaseの性質 (デヒドロ酢酸の微生物による分解-2,3-(微生物による麹酸代謝に関する研究-11,12-))

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In the course of our investigation on the microbiological degradation of γ-pyrone compounds, we have assumed that dehydroacetic acid is metabolized to triacetic acid lactone and then triacetic acid by Pseudomonas sp. This paper deals with the purification procedure and some properties of dehydroacetic acid hydrolase which converts dehydroacetic acid to triacetic acid lactone. The enzyme has been partially purified by ammonium sulfate fractionation and chromatography on Sephadex G-75 column. The purified enzyme showed 17_??_20 fold higher specific activity compared with that of crude enzyme. Optimum pH and temperature for the enzyme activity were 8.0 and 45_??_50°C, respectively. But the enzyme lost almost all the activity at 70°C for 5 min. It was activated by the addition of magnesium ion (2.8×10-3M) and manganese ion (1.0×10-3M) and was strongly inhibited with EDTA, α, α'-dipyridyl and sodium arsenate. Triacetic acid lactone has been followed both by paper chromatography and by coloration with hydroxylamine and ferric chloride.