Biochemical characterization and inhibition of thermolabile hemolysin from <i>Vibrio parahaemolyticus</i> by phenolic compounds

Vibrio parahaemolyticus ( Vp ), a typical microorganism inhabiting marine ecosystems, uses pathogenic virulence molecules such as hemolysins to cause bacterial infections of both human and animals. The thermolabile hemolysin TLH lyses erythrocytes by phospholipase B/A2 enzymatic activity in egg-yolk lecithin. However, few studies have been characterized the biochemical properties use molecular target for natural compounds an alternative control infection. Here, we evaluated inhibition parameters recombinant using hemolytic assays determined interactions silico docking analysis. highest was at pH 8 50 °C, it inactivated 20 min 60 °C with Tm = 50.9 °C. Additionally, flavonoids quercetin, epigallocatechin gallate, morin inhibited IC50 values 4.5 µM, 6.3 9.9 respectively; while phenolics acids were not effective inhibitors this enzyme. Boltzmann Arrhenius equation analysis indicate that is activities agrees docking, suggesting could interact active site’s amino acids. Future research necessary evaluate antibacterial against vivo.