从酿酒酵母中部分纯化和研究脂氧合酶的一些性质。

Partial purification and some properties of lipoxygenase from Saccharomyces cerevisiae.

机构信息

Department of Food Science and Agricultural Chemistry, McGill University, 21 111 Lakeshore, H9X 3V9, Ste Anne de Bellevue, Québec, Canada.

出版信息

World J Microbiol Biotechnol. 1995 Sep;11(5):494-6. doi: 10.1007/BF00286359.

DOI:10.1007/BF00286359

PMID:24414899

Abstract

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.

摘要

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。