A novel L‐asparaginase from the symbiotic Enterobacter aerogenes isolated from Eucheuma sp

This study was aimed to purify and characterize the enzyme L‐asparaginase from endophytic microorganisms of Eucheuma sp. in Puntondo Island, South Sulawesi, Indonesia. Research stages were ammonium sulfate precipitation, dialysis, and Sephadex G‐75 gel filtration chromatography and Sephadex CMC‐50 ion‐exchange chromatography matrices. The result of test activities of ammonium sulfate fraction showed the highest range of 40%–60% the activity value of 6.71 IU/ml. The highest protein content was obtained on a 0%–20% fraction of 2.76 mg/ml. Temperature and pH assessments indicated that L‐asparaginase had optimum activity at 37°C and pH 8, respectively. At the stage of dialysis, the highest protein content was 5.17 IU/ml in a 0%–20% fraction, and the highest enzyme activity was 1.23 IU/ml in a 20%–40% fraction. The results of gel filtration chromatography fractions G‐75 were F5–F10, with a specific activity of 0.60 U/mg, 2.05 times higher purity level than the crude extract enzyme. The results of CMC‐50 ion‐exchange chromatography showed that F54 and F55 fractions had a specific activity of 106.97 and 295.38 U/mg, respectively, with a purity level of 366.34 and 1,011.57 times higher than the crude extract enzyme. Novelty impact statement Enterobacter aerogenes strain P5, an endophytic bacterium from Eucheuma sp., can produce pure L‐asparaginase enzyme with a high specific activity applied in pharmaceuticals nutraceutical applications.