Serrapeptase, also known as serratiopeptidase, is a proteolytic enzyme originally isolated from the bacterium Serratia marcescens. It has been promoted for its purported anti-inflammatory and fibrinolytic (fibrin-dissolving) properties, including use to support or treat various forms of fibrosis, such as pulmonary fibrosis and post-surgical adhesions.

There is limited scientific evidence suggesting that serrapeptase may help degrade fibrin and some extracellular matrix components, which are involved in the development of fibrosis. Some in vitro and animal studies have shown that serrapeptase can reduce inflammation and modulate tissue remodeling. However, robust clinical trials in humans specifically examining its efficacy for established fibrotic diseases are lacking. A few small human studies have investigated its use in conditions associated with inflammation and edema, but not directly in well-characterized fibrotic diseases.

Systematic reviews and authoritative guidelines note insufficient high-quality evidence to support the use of serrapeptase for fibrosis in clinical settings. Most available research is preliminary, with methodological limitations or lack of relevant clinical endpoints. Thus, while there is a plausible mechanism and weak preliminary data, scientific validation for the use of serrapeptase in treating or supporting fibrosis is currently limited.