title: Purification, product characterization and kinetic properties of lipoxygenase from olive fruit (Olea europaea L.).
abstract: 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.
authors.affiliation: Université de Corse, UMR 6134 CNRS, quartier Grossetti, BP 52, 20250 Corte, France.
authors.forename: V
authors.initials: V
authors.lastname: Lorenzi
authors.forename: J
authors.initials: J
authors.lastname: Maury
authors.forename: J
authors.initials: J
authors.lastname: Casanova
authors.forename: L
authors.initials: L
authors.lastname: Berti
mesh_terms: D002458:Cell Fractionation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005638:Fruit / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D019787:Linoleic Acid / Q000378:metabolism; D008084:Lipoxygenase / Q000302:isolation & purification / Q000378:metabolism*; D009637:Masoprocol / Q000494:pharmacology; D031658:Olea / Q000201:enzymology*; D010940:Plant Proteins / Q000302:isolation & purification / Q000378:metabolism*; D011435:Propyl Gallate / Q000494:pharmacology; D013379:Substrate Specificity; D017962:alpha-Linolenic Acid / Q000378:metabolism
chemical_list: D004791:Enzyme Inhibitors; D010940:Plant Proteins; D017962:alpha-Linolenic Acid; D009637:Masoprocol; D011435:Propyl Gallate; D019787:Linoleic Acid; D008084:Lipoxygenase