| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2016754 | Plant Physiology and Biochemistry | 2006 | 5 Pages |
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 μM) than for linolenic acid (Km = 306.26 μM). 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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Authors
V. Lorenzi, J. Maury, J. Casanova, L. Berti,