We purified a lipoxygenase to homogeneity from eggplant (Solanum melongena Linne) fruits employing the established visible spectrophotometric assay, in which the products of the lipoxygenase-catalyzed reaction, hydroperoxyfatty acids, oxidizes 2,2’-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] diammonium salt in the presence of a catalyst cytochrome c to yield chromophores in the visible region. This allowed for the rapid detection of the lipoxygenase activity and was helpful in accomplishing the efficient purification of the lipoxygenase. The purified lipoxygenase was a monomeric enzyme with a molecular weight of 95,000, s20, w of 5.3 S, and all isoelectric point of 4.4. The specific activity and Km value for the linoleate oxygenation were 7.8 μmol min-1 mg-1 and 0.8 mM, respectively, at 25 °C and pH 7.0, The enzyme contained 1.3 g-atom of nonheme iron per enzyme.
|Number of pages||6|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 1995 Jan 1|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology