| Summary: | Myrosinase is an enzyme of cruciferous vegetables, hydrolyse glucosinolates. The breakdown products are involved in plant defence against insect and also have anti-fungal property. Myrosinase has been purified to apparent homogeneity from 5 days old germinated cauliflower seedlings having a specific activity of 12.71 units/mg proteins with 54.6 % recovery, using ammonium sulfate fractionation followed by gel filtration chromatography on Sephadex G-100. Effect of some metal ions and carbohydrates on the activity of partially purified cauliflower myrosinase was studied. Sr+2 at 4 mM concentration exhibited marked activating effect on the activity up to 2.7 fold while Fe+2 significantly inhibited. However, Sn+2 and Ba+2 increased the activity to a certain extent and then suppressed. On the other hand, some metal ions [Fe+2, Fe+3, Cu+2 and Zn+2] strongly inhibited the activity even at lower concentrations. Several carbohydrates viz., glucose, fructose, sucrose, maltose and sorbitol even at comparatively higher concentrations had little detectable inhibitory effects. Activation kinetics of myrosinase in presence of Sn+2 and Sr+2 were studied between 0- 20min. The rate of reaction was almost constant till 15 min and then slight deactivation was recorded at various concentrations used.
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