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KMID : 0380619870190040295
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Korean Journal of Food Science and Technology
1987 Volume.19 No. 4 p.295 ~ p.299
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Purification and Characterization of Mungbean Lipoxygenase
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Abstract
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Mungbean Lipoxygenase was purified by ammonium sulfate fractionation, DEAF-sephacel column chromatography and sephadex G-200 gel filtration. The specific activity of pfurified enzyme was 23.4U/㎎ 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℃. The enzyme activity was inhibited by antioxidants such as nordihydroguiaretic acid and chelating agents.
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