Abstract
ABSTRACT Phaseolus vulgaris cv, haricot seed peroxidase was extracted and partially purified. The precipitation of an active peroxidase fraction with solid ammonium sulfate (at 35‐90% saturation) increased its activity by a factor of 3. The pH for optimum activity was 5.4. The addition of 4 μm hydrogen peroxide increased the activity 92‐fold; however, enzyme activity was decreased by higher concentrations of this reagent. Carbonyl compounds resulting from peroxidase activity were isolated as their dinitrophenylhydrazones and then purified by preparative TLC. Subsequent GC‐MS analysis revealed that acetone was the principal carbonyl compound resulting from enzyme activity.
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