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...
| Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 44(2006), 7-9 vom: 01. Juli, Seite 450-4 |
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| Weitere Verfasser: | , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2006
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| 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... |
| Zusammenfassung: | 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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| Beschreibung: | Date Completed 18.12.2006 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2690 |