Synopsis

Source of validity: Scientific
Rating (out of 5): 2

Lactoperoxidase is an enzyme present in various secretions, including milk, saliva, and tears, and it is known for its antimicrobial properties. Its use in supporting or treating cuts is justified by a modest but growing body of scientific evidence. The enzyme functions by catalyzing the oxidation of thiocyanate ions in the presence of hydrogen peroxide, producing hypothiocyanite, a compound with strong antimicrobial activity. This mechanism can help reduce the risk of infection in wounds such as cuts. Several in vitro studies have demonstrated that lactoperoxidase exhibits bacteriostatic and bactericidal effects against a range of pathogenic microorganisms commonly associated with wound infections, such as Staphylococcus aureus and Pseudomonas aeruginosa. While lactoperoxidase is widely used in oral hygiene products and food preservation, its direct application for wound care is less common and has not been extensively studied in clinical settings. Some topical formulations for skin or wound care may include lactoperoxidase or lactoperoxidase-containing extracts, aiming to harness its antimicrobial properties. However, clinical trials evaluating its efficacy specifically for treating cuts are limited, and most available data come from laboratory or animal studies. As such, while the scientific rationale for using lactoperoxidase to support the healing of cuts is plausible and supported by basic research, there is a lack of robust clinical evidence. Therefore, its use is rated as a 2 on the evidence scale, reflecting early-stage scientific validation but not yet widespread clinical endorsement.

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