Also known as: Serratiopeptidase, Serratia peptidase
Serrapeptase is a proteolytic enzyme originally isolated from the bacterium Serratia marcescens in the intestine of the silkworm. It is used as an anti-inflammatory and mucolytic agent, with preliminary evidence supporting its role in reducing swelling and pain after surgical procedures.
Serrapeptase (serratiopeptidase) is a serine protease enzyme produced by Serratia marcescens, a bacterium found in the gut of the silkworm Bombyx mori. The enzyme is capable of degrading non-living tissue, blood clots, cysts, and arterial plaque in vitro, and has been used clinically in Japan and Europe since the 1960s as an anti-inflammatory agent. Its proposed mechanisms include fibrinolytic activity, reduction of bradykinin and other inflammatory mediators, and thinning of mucous secretions. Several small clinical trials have demonstrated benefits in post-surgical swelling reduction and sinusitis symptom relief, though the overall evidence base remains limited by small sample sizes and methodological heterogeneity. Serrapeptase is typically formulated as enteric-coated tablets to protect the enzyme from gastric acid degradation.
Several clinical trials have shown that serrapeptase can significantly reduce facial swelling, pain, and trismus following third molar extraction surgery compared to placebo.
Serrapeptase has demonstrated mucolytic properties that may thin sputum and improve expectoration in patients with chronic airway diseases, though large-scale confirmatory trials are lacking.
A small number of trials suggest serrapeptase reduces pain scores in inflammatory conditions, possibly through degradation of bradykinin at the site of inflammation.
On an empty stomach, 30 minutes before meals
Must be taken on an empty stomach to avoid enzymatic degradation and ensure systemic absorption. Enteric-coated formulations are essential.
Systemic anti-inflammatory effects
Convenient dosing with gastric protection
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