Use of black soldier fly (Hermetia illucens) prepupae amino acids as anti Aeromonas hydrophila enterotoxin in vivo

Abstract

Aeromonas hydrophila is an opportunistic freshwater. These bacteria cause gastroenteritis and septicemia in animals and humans. Hemolysin and aerolysin, are important in the pathogenesis of A. hydrophila. Prepupae Black soldier fly (BSF) can be used as an antibacterial using its active substance against hemolysin and aerolysin. This study aimed to determine how the interaction of prepupae BSF amino acids with A. hydrophila enterotoxin in silico and protein level in various substrates in vivo. The study consisted of BSF larva of T1 (fed fruit waste), T2 (fed fermented fruit waste), T3 (fed tofu waste), T4 (fed fermented tofu waste), and T5 (fed fermented fruit waste and tofu waste). Data on the difference of protein level of prepupae among groups were analyzed statistically using the ANOVA test. The study showed that the highest protein content of BSF prepupae was found in treatment T3 dan T4. Protein docking analysis showed that L-arginine had the most hydrogen interaction (11 H-bonds) with aerolysin and 10 H-bonds against hemolysin, indicating an antibacterial role. The most favorable interacting residues of 17 amino acids against hemolysin were ARG73, ASP74, THR541, ALA523, and ASN483, while the residues of the active site against aerolysin were ASP92, ARG394, SER354, TYR348, ARG356, VAL396, PRO395, and ASP350. Amino could inhibit the hemolytic toxin of Aeromonas by interacting with binding site residues. The better the nutritional value of the substrate given to BSF larvae, the higher the protein content of BSF prepupae. Proteins from BSF prepupae can be antibacterial candidates against A. hydrophila.

Keywords

• aeromonas hydrophila
• prepupae
• insects
• protein
• in silico