CHARACTERIZATION OF L-ASPARAGINASE FROM CAPSICUM ANNUM L.

L-asparagine is the most abundant metabolite for storage and transport of nitrogen that is utilized in protein biosynthesis in plants. L-asparaginase catalyzes the deamination of L-asparagine to aspartic acid and ammonia. The present study is aimed to characterize L-asparaginase from Capsicum annum L.Crude L-asparaginase was partially purified by salting out using 20% to 80% of ammonium sulphate. The activity of L-asparaginase was measured in the aqueous extract of fruits by Nesselerization method. The specific enzyme activity after 80% saturation was 4841.78 IU/mg. Optimum incubation period for L-asparaginase was found 60 min. The enzyme showed stability at alkaline pH and has pH 8 as optimum pH. L-asparaginase have maximum activity at 37oC. Highest activity of L-asparaginase was at 6mM substrate concentration. Kinetic parameter study revealed high affinity of enzyme towards L-aspargine with high velocity. Partially purified enzyme have molecular weight of 25.41 kDa estimated by Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE).