Collagenases degrade native helical collagen fibrils. The enzyme has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. It is a type II enzyme that contains greater clostripain activity. It is generally used for heart, bone, muscle, thyroid, cartilage, and liver cells. Ca²⁺ is required for its activation while metal chelating agents such as cysteine, EDTA or o-phenanthroline inhibits its activity.

• Enzyme Commission Number: E.C.3.4.24.3
• Soluble in water
• Ideal for collagen structural and biosynthetic studies

Clostridial collagenase I or clostridiopeptidase A degrades the helical regions in native collagen preferentially at the Y-Gly bond in the sequence -Pro-Y-Gly-Pro- where Y is most frequently a neutral amino acid. This bond in synthetic peptide substrates may also be split.

For tissue dissociation most researchers employ either crude collagenase preparations or chromatographically purified collagenase combined with other enzymes such as elastase, trypsin, and/or papain. Collagenase from Clostridium histolyticum has been used in a study to investigate the survivability of collagen micronetworks in the presence of collagenase, and to investigate the degradation of collagen by the cariogenic bacteria, Streptococcus mutans.

Unit definition: One unit liberates one µmole of L-leucine equivalents from collagen in 5 hours at 37 °C, pH 7,5.