Properties of Broad Bean Lipoxygenase

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Abstract
An improved method of assay of lipoxygenase (E.C.1·13·1·13) was introduced by initiating and following the reaction in the spectrophotometric cell. The enzyme was extracted from broad bean (View faba) and purified fifty folds. It oxidized linoleate but not oleate and the rate of linoleate and linolenate oxidation were found to be practically the same. The enzyme had an optimum pH of 6.0 and an optimum temp of 30°C. The activation energy was found to be 7.1 KCal/mole and the Km for linoleate 2.8 × 10a‐3M.