Serratiopeptidase (SPT)

Serratiopeptidase, also known as serrapeptase or serralysin, is a proteolytic enzyme produced by the bacterium Serratia marcescens. It is a member of the Repeats-in-Toxin (RTX) family, characterized by a C-terminal RTX domain that binds calcium and is essential for the protein's folding and secretion. While traditionally utilized as an anti-inflammatory and mucolytic agent, recent research has identified its significant role in disrupting bacterial biofilms. The enzyme functions through a dual mechanism: its N-terminal catalytic domain degrades established biofilm matrix proteins via proteolysis, while its C-terminal RTX domain inhibits the initial stages of biofilm formation through a protease-independent mechanism. This non-proteolytic action is thought to involve the modulation of bacterial surface interactions and signaling pathways, such as the regulation of curli fiber assembly or phosphate-related stress responses. In clinical practice, serratiopeptidase is used to reduce edema and inflammation, and it is increasingly explored as an adjuvant therapy to enhance the efficacy of antibiotics against biofilm-associated infections. Its ability to degrade inflammatory mediators like bradykinin and fibrin further contributes to its therapeutic profile in managing pain and swelling. Despite its long history of use, the specific molecular targets of its RTX domain in biofilm regulation remain an area of active investigation.

Other names

SerrapeptaseSerralysinSerratia E-15 proteaseSerratia metalloproteaseSpepEC 3.4.24.40

Proteolytic degradation of biofilm matrix proteins and inflammatory mediators via the N-terminal catalytic domain; non-proteolytic inhibition of bacterial adhesion and signaling via the C-terminal RTX domain.