Lactoperoxidase inhibition of some natural phenolic compounds: Kinetics and molecular docking studies

Abstract

The inhibition effects of some phenolic compounds from natural products such as taxifolin, resveratrol, olivetol, cynarine, and phloretin on bovine milk lactoperoxidase (LPO) enzyme were examined. For this aim, LPO was purified by the affinity chromatography technique with a yield of 77.68% in 421.32 times. The kinetic value, K-i, was calculated from the equations obtained from drawn graphs. In order to discover inhibition mechanism of phenolic compounds, induced fit docking process was performed on the LPO receptors. The binding affinity of the compounds was calculated and at the best-scored ligand-receptor complex, residues responsible for enzyme inhibition were detected. As a result, this molecule demonstrated the potential inhibitory effect on LPO. According to the results of kinetic study. It has shown a noncompetitive inhibition effect, Phloretin's K-i value was determined by 48.89 +/- 14.22 nM. Practical applications There are natural antimicrobial systems, such as the lactoperoxidase (E.C.1.11.1.7; LPO) system, which eliminates the harmful effects of microorganisms in milk. The chemical reactions in this system are catalyzed by the LPO. In the dairy industry, the LPO system is considered critical for the preservation of pasteurized milk, yogurt, raw milk, and cheese. The system is used for improvement the protection condition of milk at high temperatures.