Purification L-asparaginase from Acinetobacter baumannii and study of antitumor activity | ||||
| Microbes and Infectious Diseases | ||||
| Articles in Press, Accepted Manuscript, Available Online from 04 June 2025 | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/mid.2025.388626.2831 | ||||
 View on SCiNiTO | ||||
| Author | ||||
Amenah RAMI Abdullah 
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| Department of Biotechnology, Collage of Science, University of Baghdad, Iraq | ||||
| Abstract | ||||
| Background: Acinetobacter baumannii is a member of the genus Acinetobacter and the family Moraxellaceae of the Eubacteria class Proteobacteria. Microbial L-asparaginase's capacity to act as an oncological agent has been thoroughly studied and applied. L-asparaginase has various applications in the culinary, pharmaceutical, and medical industries. Objectives To evaluate L-asparaginase's potential as a selective anticancer drug by evaluating its cytotoxic activity against tumor cell lines, such as PC-3 (prostate cancer), A375 (melanoma), and HdFn (normal human fibroblasts as a control) Methods: After first screening several bacterial isolates to determine which produced the most activity, the enzyme was purified in multiple steps using ion exchange chromatography, gel filtration, and ammonium sulfate precipitation. The effects of pH and temperature on the enzyme's stability and activity were also examined. Using an MTT assay, the cytotoxic activity of L-aspargense against PC-3, A375, and FTC133 cells was evaluated. The cells were cultivated for 24 hours at 37 °C in CO2 (5%) incubation after being seeded into a flat 96-well plate (100 µL per well) at a concentration of 1 × 106 cells per well. Results: demonstrated maximum activity at 37°C and pH 7 and 8. The effect of other ions and inhibitors was also evaluated; some ions, such as HgCl₂, acted as inhibitors, whereas NaCl increased activity. L-asparaginase's potential as an antitumor treatment agent was highlighted by MTT cytotoxicity experiments, which showed that it had selective cytotoxic effects against cancer cell lines while sparing normal cells. Conclusions: The study's findings demonstrated that the L-asparaginase enzyme, which was isolated and refined from Acinetobacter baumannii, had unique enzymatic properties and encouraging anticancer activity. | ||||
| Keywords | ||||
| L-asparaginase; Acinetobacter baumannii; enzyme purification; anticancer activity; cytotoxicit | ||||
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