EFFECT OF SUBSTRATE CONCENTRATION AND FeCl2 ADDITION ON L-ASPARAGINASE ACTIVITIES OF BACTERIA SYMBIONTS BROWN ALGAE Sargassum sp. AND ITS POTENTIAL AS A NEW ANTI-DENGUE AGENTS

Abstract

The disintegration of the amide link, causing L-Asparaginase catalyzes the hydrolysis process of L-Asparagine into ammonia and aspartic acid. The purposes of this study were to determine the optimal conditions for enzyme production and enzymatic activity, including their potential as a new anti-dengue of L-asparaginase from Klebsiella sp. The Nessler method used a UV-Visible spectrophotometer to determine the L-asparaginase activity by measuring ammonia levels produced by L-asparaginase catalysis. The ideal fermentation period was at the 48th hour, and the optimal substrate concentration was 10 g/L with an activity value of 49.572 U/mL, and the optimal FeCl2 concentration was 0.5 g/L with an activity value of 60.1183 U/mL, and protein content of 0.1878 mg/mL. The optimum conditions for L-asparaginase, which has an activity value of 61.1182 U/mL, were observed at pH 8 and 37 °C. The optimum cofactor concentration of FeCl2 was 0.5 mM, which resulted in an activity value of 106.5046 U/mL. Both the inhibition percentage and CC50 value were 80% and 167.15 μg/mL respectively, showing that the L-asparaginase has a high antidengue potential.