유안염석과 column chromatography 및 gel여과등으로 비활성이 23.4U/mg이 되는 정제된 mungbean lipoxygenase를 12%의 수율로 얻었다. 정제효소의 작용최적 pH는 8.4이었으며 linoleic acid를 기질로 사용하였을 때 Km값은 0.25mM이었다. 정제효소는 pH $5.0{sim}7.0$범위와 $50^{circ}C$이하의 온도에서 비교적 안정하였다. 효소의 활성은 항산화제인 NDGA에 의해 현저히 저해되었고 chelating agents에 의해 저해되었다.
Mungbean Lipoxygenase was purified by ammonium sulfate fractionation, DEAE-sephacel column chromatography and sephadex G-200 gel filtration. The specific activity of pfurified enzyme was 23.4U/mg protein and the yield was 12%. Optimal activity of the enzyme was observed at pH 8.4 and the enzyme had Km value of 0.25mM for linoleic acid. The enzyme was stable in the range of pH 5.0-7.0 and at temperature below $50^{circ}C$. The enzyme activity was inhibited by antioxidants such as nordihydroguiaretic arid and chelating agents.
