Collagenase clostridium histolyticum


Collagenase clostridium histolyticum
Accession Number
DB00048 / 9X7O8V25IT
Collagenase Santyl

Collagenase clostridium histolyticum is an enzyme produced through the bacterium Clostridium histolyticum that dismantles collagen. it's miles used as a powder-and-solvent injection package for the treatment of Dupuytren's contracture, a situation wherein the hands bend towards the palm and can not be absolutely straightened, and Peyronie's sickness, a connective tissue ailment related to the increase of fibrous plaques inside the tender tissue of the penis. BioSpecifics technologies developed the preparation, that's manufactured and advertised with the aid of Auxilium prescribed drugs as Xiaflex in the US and by Sobi as Xiapex in Europe.



Used in the treatment of skin ulcers and sever burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area.


Used to promote debridement of necrotic tissue in the treatment of severe burns and dermal ulcers including decubitus ulcers.


Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus