Optimization of enzyme activity of l-asparaginase derived from enterobacter agglomerans sb 221 bacterial symbiont of brown algae sargassum sp.

Abstract

L-asparaginase an enzyme belonging to the class of hydrolases which enable hydrolyze L-Asparagine to L-aspartic acid and ammonia is used in leukemia cancer treatment. L-asparaginase was purified from Enterobacter agglomerans SB 221, epiphytic bacterial symbiont of brown algae, Sargassum sp. This research aimed to optimize the concentration of L-Asn substrate, fermentation time, and CoCl2 concentration for high enzyme production. Also, the optimum pH, temperature, and CoCl2 concentration for the most efficient enzymatic activity were determined. Nessler Method determined the enzymatic activity of L-asparaginase. The optimum concentration of L-Asn substrate was found to be 10 g/L with the fermentation time of 48 hours, and the activity value of 49.572 U/mL. The optimum concentration of CoCl2 was 1.9 mM, with an activity value of 72.236 U/mL and the protein concentration of 0.2269 mg/mL. Enzyme activity was optimum at pH 8 and 37 o C temperature, yielding an activity value of 71.842 U/mL. The optimum concentration of CoCl2 was 0.25 mM, with an activity value of 111.315 U/mL. These findings suggest that the enzyme activity of L-asparaginase can be increased by the addition of 10 g/L of L-Asn as the substrate and 0.25 mM of CoCl2 as the cofactor. Sargassum binderi, the most abundant algae in the seawaters of Indonesia, can be used as a natural source of anticancer therapy, especially leukemia.

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