Department of Food Science and Agricultural Chemistry, McGill University, 21 111 Lakeshore, H9X 3V9, Ste Anne de Bellevue, Québec, Canada.
World J Microbiol Biotechnol. 1995 Sep;11(5):494-6. doi: 10.1007/BF00286359.
A partially purified lipoxygenase extract was obtained from the yeast Saccharomyces cerevisiae by precipitation with solid (NH4)SO4 at 20% to 80% saturation. The enzyme had two pH optima, at pH 8.0 and 10.0, with respective apparent K m values of 13 and 9.5 μM. At both pH optima, the lipoxygenase demonstrated highest substrate specificity towards linoleic acid, followed by linolenic acid; although the enzyme had less specificity towards mono-linolein than di-linolein at pH 8.0, the reverse was true at pH 10.0.
通过用固体（NH4）2SO4在 20%至 80%饱和度下沉淀，从酵母酿酒酵母中获得部分纯化的脂氧合酶提取物。该酶具有两个 pH 最优值，在 pH 8.0 和 10.0 时，相应的表观 Km 值分别为 13 和 9.5 μM。在两个 pH 最优值下，脂氧合酶对亚油酸表现出最高的底物特异性，其次是亚麻酸; 尽管在 pH 8.0 时，该酶对单亚油酸的特异性比对二亚油酸低，但在 pH 10.0 时则相反。
