Extraction, Purification, Characterization And Anticancer Activity Of L-Asparaginase From Novel Plant Source: Caryota Urens (Shivjata)

Abstract

L-asparaginase was screened for during the current study in several Caryota urens plant sections. One possible source for L-asparaginase synthesis was identified as the unripe fruit with the highest enzyme activity (925U/ml). The discovery of L-asparaginase in Caryota urens is a first. The enzyme was 38% pure, with an 85-fold purification factor, and 3325U/ml of total enzyme activity after purification. It was discovered that the enzyme's kinetic parameters, Km and Vmax, were 13.8 mM and 100μM/ml, respectively. The partly purified enzyme was shown to be a single protein with a molecular weight of 47 kDa by SDS-PAGE electrophoresis. The cytotoxic effects of L-asparaginase against the K562 and PBMC (peripheral blood mononuclear cell) cell line were investigated; the results showed 26% and 96% (IC50 23.03μg/ml) of cytotoxicity, respectively. Future research can examine the effectiveness of L-asparaginase from Caryota urens L., as it exhibits little glutaminase activity and reduced toxicity toward PBMC.