Anticancer Activity of L-asparaginase Produced from Amycolatopsis japonica

Abstract

The ability of L-asparaginase to inhibit the formation of cancer cells has aroused scientists' curiosity in biological realms. In cancer cells, L-asparaginase suppresses protein synthesis by hydrolyzing L-asparagine to L-aspartic acid and ammonia. As a result, it's a crucial therapeutic enzyme in the treatment of Acute Lymphoblastic Leukemia in combination with other drugs (ALL). This enzyme has recently been discovered to be useful in a number of scientific fields, including clinical research, pharmacology, and the food business. Purification, characterization, and assessment of the cytotoxic effect of Amycolatopsis japonica L-asparaginase were the goals of this study. Amycolatopsis japonica was isolated from the plant rhizosphere and L-asparaginase was recovered. With a molecular weight of 37.5 KDa, partially purified L-asparaginase from A. japonica had a total activity of 1968.98 U with 26.696 mg total protein and a specific activity of 73.75 U/mg, 6.42 purification fold, and 42.86 percent recovery yield. In the presence of EDTA, Mg2+, pH8, 45oC, and 0.13 mM L-asparagine, L-asparaginase from A. japonica demonstrated good activity and stability, with Km and Vmax values of 0.13 mM L-asparagine and 0.43U/ mL, respectively. The cytotoxicity of L- asparaginase from A.japonica against a colon cancer cell line was high; with an IC50 value of 36 L. Amycolatopsis japonica could be a source of L-asparaginase, which could be a new target for cancer cells.