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Published on: March 9, 2021
Purification, product characterization and kinetic properties of lipoxygenase from olive fruit (Olea europaea L.)
V Lorenzi1, J Maury, J Casanova
1Université de Corse, UMR 6134 CNRS, quartier Grossetti, BP 52, 20250 Corte, France.
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.
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