ABSTRACTPhaseolus vulgariscv, haricot seed lipoxygenase was extracted and partially purified. The precipitation of an active lipoxygenase fraction with solid ammonium sulfate (at 20–50 of saturation) increased its activity by a factor of 3. The pH for optimum activity was 7.3. The addition of 40 mM potassium cyanide resulted in a doubling of the enzyme activity. Enzyme activity was completely lost on storage at 4°C for 48 hr. The activity of haricot lipoxygenase extract was considerably greater on linoleic acid than on its esters, and decreased in the order: mono‐di>trilinolein. The haricot lipoxygenase shares many of the characteristics of the corresponding enzyme found in several seed sou
展开▼