Title of article
Purification, product characterization and kinetic properties of lipoxygenase from olive fruit (Olea europaea L.)
Author/Authors
Lorenzi، نويسنده , , V. and Maury، نويسنده , , J. and Casanova، نويسنده , , J. and Berti، نويسنده , , L.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2006
Pages
5
From page
450
To page
454
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.
Keywords
lipoxygenase , Olive , Purification , Product specificity , characterization
Journal title
Plant Physiology and Biochemistry
Serial Year
2006
Journal title
Plant Physiology and Biochemistry
Record number
2121497
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