Synopsis

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

Lysozyme is an enzyme naturally present in various bodily secretions, such as saliva, tears, and mucus, where it plays a role in the innate immune defense by hydrolyzing the peptidoglycan layer of bacterial cell walls, particularly in Gram-positive bacteria. Historically, lysozyme has been isolated from egg whites and used as a food preservative due to its antimicrobial properties. In the context of supporting or serving as an alternative to antibiotics, there is some scientific basis for its use, primarily in vitro and animal studies. These studies suggest lysozyme can reduce bacterial load and may work synergistically with certain antibiotics, potentially lowering the required dose or enhancing efficacy. However, its effectiveness in treating established infections in humans is limited by its spectrum of activity (mainly Gram-positive organisms) and by the fact that many pathogenic bacteria have evolved mechanisms to resist lysozyme action.

Clinical trials in humans are sparse and typically focus on lysozyme as a supportive agent (e.g., in oral health or as adjunctive therapy in respiratory infections), rather than as a standalone alternative to antibiotics for systemic infections. Thus, while there is a scientific rationale for its antibacterial role, the current evidence does not robustly support lysozyme as a replacement for antibiotics in clinical practice. Its main value lies in supportive roles or in combination therapies, pending further research.

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