vibriolysin

Vibriolysin is a thermostable zinc metalloprotease enzyme secreted by the marine microorganism *Vibrio proteolyticus* and related species[1][4][6]. It preferentially cleaves peptide bonds with bulky hydrophobic groups in P2 and P1' positions—most notably favoring phenylalanine at P1'[4]. Vibriolysin is under investigation as an enzymatic debridement agent for burn wound eschar; it selectively hydrolyzes denatured proteins such as fibrin, elastin, and collagen in necrotic tissue while sparing viable tissue[1][3]. This selectivity allows for rapid removal of dead tissue without causing bleeding or damaging healthy cells[3]. The enzyme has also been studied for its role in bacterial pathogenicity (notably in cholera), but its primary pharmaceutical application is topical use for burns and burn infections[3][6].

Brand names

VibrilaseNeutral Proteinase

Other names

vibriolysinAeromonas proteolytica neutral proteinaseaeromonolysin