Protein isolation of Pterois volitans venomous with a heating process for antibacterial activity assay

Pterois volitans is an invasive native predatory fish species in the Indo-Pacific ocean that disrupt the food chain and damage coral reefs which cause ecosystem imbalances. These fish have venomous spines that made them inedible and avoided by a predator. Due to its rapid growth, utilization of this venom can be useful along with controlling the population. Recent studies show the benefits of phospholipase A2, which is a protein compound that contained in the venom has antibacterial activity and expected to be an antibacterial agent. In this study, we used heating and gradual purification to obtain the optimum concentration of Phospholipase A2. The protein isolates were analyzed using the Marinetti method, determination of concentration by Lowry test, identification of protein with SDS-Page, and the antibacterial activity test using agar diffusion. The results of phospholipase A2 obtained from the extract of P. volitans venom by purification method ammonium sulfate at 80% saturation with a heating time of 35 minutes had a specific enzyme activity of 0.0206 units / μg and can inhibit E. coli bacteria 98.81% and Salmonella sp. inhibit 89.28% with a concentration of 3.77 μg / ml.