農産物のトリヒドロキシベンゼン酸化酵素に関する研究　ＩＩＩ　　カブのフロログルシノール酸化酵素の精製とその性質

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タイトル別名
  • Purification of Phloroglucinoloxidase from Turnip and Its Properties
  • カブ ノ フロログルシノール サンカ コウソ ノ セイセイ ト ソノ セイシツ

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Phloroglucinoloxidase (PhO) was found in roots of turnip (Brassica raga L.). Enzyme purification was performed by ammonium sulfate fractionation, ion exchange chromatography and gel filtration, and the enzyme was purified 33-fold. The enzyme was homogeneous on disc electrophoresis. The molecular weight of the enzyme was estimated to be about 27, 000 by gel filtration. The enzyme solution exhibited absorption maxima at 277, 403, 492 and 633 nm. The enzyme oxidized phioroglucinol and phloroglucinolcarboxylic acid but did not oxidize diphenols, such as catechol, resorcinol and hydroquinone. The enzyme showed pronounced peroxidase (POD) activity. The optimum pH of the enzyme was 7.6_??_8 for PhO and 5 for POD. PhO activity was more stable than POD activity at relatively high temperature. Both activities were inhibited by sodium diethyldthioicarbamate, potassium cyanide and L-ascorbic acid. PhO activity was markedly accelerated by Mn2+ and inhibited considerably by Cu2+. On the other hand, POD activity was not influenced by these metal ions.

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