Serrapeptase is processed commercially in the laboratory through fermentation. It was originally found in the silkworm where it is naturally present in its intestine. This immunologically active enzyme is completely bound to the alpha 2 macroglobulin in biological fluids. Histologic studies reveal powerful anti-inflammatory effects of this naturally occurring enzyme.

The mechanisms of action of serrapeptase at the sites of various inflammatory processes consist fundamentally of a reduction of the exudative phenomena and an inhibition of the release of the inflammatory mediators. This peptidase induces fragmentation of fibrinous aggregates and reduces the viscosity of exudates, thus facilitating drainage of these products of the inflammatory response and thereby promoting the tissue repair process. Studies suggest that serrapeptase has a modulatory effect on specific acute phase proteins that are involved in the inflammatory process. This is substantiated by a report of significant reductions in C3 and C4 complement, increases in opsonising protein and reductions in concentrations of haptoglobulin, which is a scavenger protein that inhibits lysosomal protease.