Kollagenase

Kollagenase, or collagenase, is an enzyme that hydrolyzes collagen, the primary structural protein of connective tissue. It belongs to the metalloprotease family and exists in multiple forms. In humans, the term usually refers to the collagenases MMP-1, MMP-8, and MMP-13, which efficiently cleave native fibrillar collagens types I, II, and III. Bacterial collagenases, notably from Clostridium histolyticum, are widely used in laboratory and clinical contexts.

Mechanism and regulation: Collagenases target the triple-helical region of collagen, breaking the peptide bond in a conserved sequence and producing partially degraded molecules. They are zinc-dependent metalloproteases; many require calcium for stability. Mammalian MMPs are secreted as inactive proenzymes and activated by proteolytic removal of a propeptide. Activity is regulated by tissue inhibitors of metalloproteinases (TIMPs).

Applications: In research, collagenases are used to dissociate tissues and isolate cells from connective tissues. Commercially available bacterial collagenases enable efficient digestion of extracellular matrix for cell culture. In medicine, enzymatic debridement of necrotic tissue uses collagenase preparations such as Santyl. Collagenase clostridium histolyticum formulations (for example, Xiaflex) are approved for Dupuytren’s contracture and Peyronie’s disease, where targeted breakdown of collagen cords or plaques reduces contracture.

Safety and regulation: Collagenase products are regulated as drugs or medical devices in many jurisdictions and require appropriate handling to minimize tissue damage and allergic reactions. In research, enzyme preparations are used under standard biosafety conditions and are treated as biological reagents.