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International Journal Of Medical, Pharmacy And Drug Research(IJMPD)

Anticancer Activity of L-asparaginase Produced from Amycolatopsis japonica

Mojisola O. Salami , Abiodun A. Onilude , Iqbal Choudhary , Rukesh Mahajan , Abideen A. Adekanmi


International Journal of Medical, Pharmacy and Drug Research(IJMPD), Vol-6,Issue-3, May - June 2022, Pages 1-15 , 10.22161/ijmpd.6.3.1

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Article Info: Received: 26 Mar 2022; Received in revised form: 21 May 2022; Accepted: 29 May 2022; Available online: 05 Jun 2022

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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.

L-asparaginase, Cancer cells, L-aspartic, Amycolatopsis japonica, Characterisation, Purification

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