橄榄果实（油橄榄）脂氧合酶的纯化、产物表征及动力学特性
Purification, product characterization and kinetic properties of lipoxygenase from olive fruit (Olea europaea L.).
作者信息
Lorenzi V, Maury J, Casanova J, Berti L
机构信息
Université de Corse, UMR 6134 CNRS, quartier Grossetti, BP 52, 20250 Corte, France.
出版信息
Plant Physiol Biochem. 2006 Jul-Sep;44(7-9):450-4. doi: 10.1016/j.plaphy.2006.09.001. Epub 2006 Sep 18.
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.
通过差速离心和疏水色谱法首次将橄榄果实中的脂氧合酶纯化至同质。该酶的分子量为98 kDa，在pH 6时表现出最大活性。脂氧合酶对亚油酸（Km = 82.44 microM）的亲和力比对亚麻酸（Km = 306.26 microM）的亲和力更好。它受到亚油酸：氧氧化还原酶（LOX）抑制剂如去甲二氢愈创木酸（NDGA）或没食子酸丙酯的抑制。当以亚油酸为底物时，反应产物为13-氢过氧十八碳二烯酸。
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