Unveiling the Suppressive Potential of Phenolic Compounds on Bovine Milk Lactoperoxidase

Lactoperoxidase (LPO) is a crucial enzyme found in milk, tears, and saliva, protecting newborns from harmful microorganisms. This study examined the effects of phenolic substances (naringin, morin, esculin, homovanillic acid, and phloridzin) on purified LPO. LPO was purified from bovine milk using affinity chromatography, yielding 66.6 % with a purity of 387.5-fold. Three methodologies were employed to assess inhibitory properties: spectrophotometric techniques, molecular docking, and MM-GBSA. The compounds ' IC50 values were 0.0024 mu M, 0.0315 mu M, 0.0373 mu M, 0.0506 mu M, and 0.0221 mu M, while their Ki values were 0.0059 +/- 0.0012 mu M, 0.0672 +/- 0.0247 mu M, 0.0973 +/- 0.0369 mu M, 0.0664 +/- 0.0190 mu M, and 0.0470 +/- 0.0159 mu M, respectively. Naringin exhibited the most potent inhibitory effect, competitively inhibiting LPO. Therefore, naringin could serve as a novel reversible LPO inhibitor. This study investigates the inhibition profiles of certain phenolic compounds-naringin, morin, esculin, homovanillic acid, and phloridzin-against the bovine lactoperoxidase (LPO) enzyme. Naringin demonstrates significant inhibition, exhibiting a Ki value of 0.0059 +/- 0.0012 mu M. Molecular docking analyses of naringin were conducted utilizing the 3D crystallographic structure of the enzyme to determine the most favorable binding poses. image