Synopsis

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

Lactoperoxidase is an enzyme naturally present in milk and various secretions such as saliva and tears. It is part of the innate immune system and exhibits antimicrobial properties through the catalytic oxidation of thiocyanate ions in the presence of hydrogen peroxide, resulting in the formation of hypothiocyanite, a compound with antimicrobial activity. The topical use of lactoperoxidase has been explored for supporting the healing of external ulcerations, particularly in the context of oral ulcers (aphthous stomatitis), skin ulcers, and wounds susceptible to infection.

Scientific validation for the use of lactoperoxidase in treating external ulcerations stems from several in vitro and in vivo studies. These studies have demonstrated that lactoperoxidase-containing formulations can reduce microbial load, limit infection, and promote a more favorable environment for wound healing. Clinical studies, especially in the field of oral health, have shown that oral care products containing lactoperoxidase (often in combination with other enzymes such as lysozyme and glucose oxidase) can accelerate healing of ulcerative lesions and reduce associated symptoms, likely due to their antimicrobial and anti-inflammatory effects.

However, the evidence base is modest rather than robust, with most studies being small, short-term, or focused on oral rather than cutaneous ulcers. There is a need for larger, high-quality randomized controlled trials to confirm efficacy, particularly for non-oral ulcerations. Despite this, the mechanistic rationale and initial clinical data provide moderate scientific support for the topical use of lactoperoxidase in managing external ulcerations.

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