Synopsis

Source of validity: Scientific
Rating (out of 5): 3

Lactoperoxidase is an enzyme found in mammalian secretions such as milk, saliva, and tears. It plays a significant role in the innate immune system due to its antimicrobial properties. The primary mechanism of action involves catalyzing the oxidation of thiocyanate ions (SCN-) in the presence of hydrogen peroxide (H₂O₂), producing hypothiocyanite (OSCN-), a compound with broad-spectrum antimicrobial effects, including activity against Staphylococcus aureus and other Staphylococcus species.

Several in vitro studies have demonstrated that lactoperoxidase, particularly as part of the lactoperoxidase system (LPO/SCN-/H₂O₂), can inhibit the growth of Staphylococcus species, including antibiotic-resistant strains such as MRSA. These effects have been observed in both planktonic cultures and biofilm models, which are relevant to persistent infections. Some oral care products and topical formulations utilize lactoperoxidase for its antimicrobial properties, including for skin and mucosal health.

However, while the biochemical and microbiological rationale is strong, direct clinical evidence supporting the use of lactoperoxidase specifically for the treatment of Staph infections in humans is limited. Most studies are preclinical or ex vivo, and few robust clinical trials have been conducted. Therefore, lactoperoxidase is considered scientifically justified for supporting the control of Staph infections based on laboratory data, but the clinical evidence is not yet strong enough to warrant a higher rating.

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