1987•Korean Journal of Food Science and TechnologyRequires access

Purification and Characterization of Mungbean Lipoxygenase

Seung-Yeol Kim, Heesoo Lee

Abstract

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 . The enzyme activity was inhibited by antioxidants such as nordihydroguiaretic arid and chelating agents.

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Key concepts: Size-exclusion chromatography, Sephadex, Chemistry, Enzyme, Chromatography, Ammonium sulfate, Fractionation, Lipoxygenase