Abstract
l-Asparaginase from Brevibacillus borstelensis ML12 was purified and sequentially studied for biochemical characterization. A 1.94 fold purification using 80% ammonium sulphate fractionation was obtained. The molecular weight was found out to be 39.5 kDa following SDS-PAGE method. The purified l-Asparaginase showed enzyme stability in the alkaline range7.6–8.8 and maximum activity at pH 8.6. Co2+ proved to be a good activator in all the three respective concentrations (5mM10 mM, 20 mM) that were selected in the study. Effect of various surfactants, bile salt, organic reagents, chelators were also incorporated and Tween 80 and bile salt were found to enhance enzyme activity. Vmax and Km values were calculated by using Lineweaver-Burk plot and the values came out to be 204.081 μmol ml-1 min-1 and 0.253 mM respectively. Thermo kinetics study revealed that deactivation energy as obtained from Arrhenius equation was 10.882 kJmol-1. The z-value was calculated as 185.16K in case of thermal inactivation of asparaginase.
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