Purification, product characterization and kinetic properties of lipoxygenase from olive fruit (Olea europaea L.)

Lipoxygenase from olive fruit was purified to homogeneity for the first time after differential centrifugations and by hydrophobic chromatography. The enzyme had a molecular mass of 98 kDa and exhibited a maximal activity at pH 6. Lipoxygenase had a better affinity for linoleic acid (Km=82.44 microM...

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Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 44(2006), 7-9 vom: 01. Juli, Seite 450-4
1. Verfasser: Lorenzi, V (VerfasserIn)
Weitere Verfasser: Maury, J, Casanova, J, Berti, L
Format: Aufsatz
Sprache:English
Veröffentlicht: 2006
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Enzyme Inhibitors Plant Proteins alpha-Linolenic Acid 0RBV727H71 Masoprocol 7BO8G1BYQU Propyl Gallate 8D4SNN7V92 mehr... Linoleic Acid 9KJL21T0QJ Lipoxygenase EC 1.13.11.12
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245 1 0 |a Purification, product characterization and kinetic properties of lipoxygenase from olive fruit (Olea europaea L.) 
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520 |a Lipoxygenase from olive fruit was purified to homogeneity for the first time after differential centrifugations and by hydrophobic chromatography. The enzyme had a molecular mass of 98 kDa and exhibited a maximal activity at pH 6. Lipoxygenase had a better affinity for linoleic acid (Km=82.44 microM) than for linolenic acid (Km = 306.26 microM). It is inhibited by linoleate:oxygen oxidoreductase (LOX) inhibitors like nordihydroguaiaretic acid (NDGA) or propyl gallate. The reaction product was 13-hydroperoxy octadecadienoic acid when linoleic acid was used as substrate 
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700 1 |a Casanova, J  |e verfasserin  |4 aut 
700 1 |a Berti, L  |e verfasserin  |4 aut 
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