Preliminary evaluation of vibriolysin, a novel proteolytic enzyme composition suitable for the debridement of burn wound eschar.
Vibriolysin, a proteolytic enzyme secreted by the marine microorganism Vibrio proteolyticus, was evaluated for its efficacy as an enzymatic debridement agent. Initial in vitro experiments revealed that the protease readily hydrolyzed proteinaceous components of eschar (e.g., fibrin, elastin, and in particular, collagen). Enzyme selectivity towards the digestion of denatured proteins but not viable elements was demonstrated in vitro and in vivo by treatment of full-thickness burn wounds with a porcine model. The full-thickness wound eschar was rapidly hydrolyzed by a hydrophilic vibriolysin composition with a resultant wound bed that appeared pink and viable. Vibriolysin exhibited desirable properties heretofore not described for the enzymatic debridement agents, in particular, its selective hydrolysis of dead but not viable tissue, debridement in the absence of bleeding, compatibility with adjunct therapies, and its unique shelf-life stability in a hydrophilic composition at ambient temperature.
Durham
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DR
W.R. Grace & Co.-Conn, Washington Research Center, Columbia, MD 21044.
Fortney
D Z
DZ
Nanney
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LB
D000287:Administration, Topical; D000818:Animals; D001426:Bacterial Proteins; D002056:Burns / Q000628:therapy*; D003646:Debridement / Q000379:methods; D004355:Drug Stability; D006868:Hydrolysis; D008666:Metalloendopeptidases / Q000008:administration & dosage / Q000627:therapeutic use*; D013552:Swine
D001426:Bacterial Proteins; D008666:Metalloendopeptidases; C073831:vibriolysin protein, Vibrio proteolyticus