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 μM, 0.0315 μM, 0.0373 μM, 0.0506 μM, and 0.0221 μM, while their Ki values were 0.0059±0.0012 μM, 0.0672±0.0247 μM, 0.0973±0.0369 μM, 0.0664±0.0190 μM, and 0.0470±0.0159 μM, respectively. Naringin exhibited the most potent inhibitory effect, competitively inhibiting LPO. Therefore, naringin could serve as a novel reversible LPO inhibitor.