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Abstract
L-asparaginase is the first pharmaceutical enzyme with anticancer properties that has been intensively studied by researchers and scientists from across the globe. Lang discovered Lasaparginase for the first time in 1904. Aspartame is a methyl ester of aspartic acid and phenylalanine dipepetides. This research aims to isolate Rhodococcus spp from water and soil samples, assess their L-asparaginase activity, and characterize the enzyme. For the isolation of Rhodococcus spp, soil and water samples were collected from lagoons and oceans. Isolation and counting were performed using the method of serial dilution and pour plate. Using the method of streak plate, a pure culture of these isolates was created. Bergy's Manual of Determinative Bacteriology was used to identify isolated actinomycetes. At 120 mm and 280 C for seven days, L-asparaginase was created in Erlenmeyer flasks containing growth medium supplemented with the enzyme L-asparaginase, one of which served as a control and the other of which contained 0.5g of aspartame. A spectrophotometer was used to measure the optical density at 600 nm. In this study, three Rhodococcus species were isolated, and a microbiological screening for L-asparaginase activity and protein concentration indicated that all three were capable of producing L-asparaginase. The asparaginase production of the three isolates of marine soil varied between 5.636-0.04 and 68.363-0.05 mol/min/ml. The best protein concentration was found on the third day, with isolates from soil samples generating the greatest protein (223.571 mg/ml) and isolates from ocean samples producing the least protein (7.285 mg/ml) on the seventh day. Rhodococcus spp isolated from ocean, lagoon, and soil samples is a feasible source of L-asparaginase with excellent substrate specificity and high yield, according to this study.
