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). - See more at: .
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