A Preliminary Characterization of a Novel Recombinant Clostridial Collagenase Blend

Clostridial collagenases are essential biotechnological tissue dissociation agents owing to their ability cleave different types of collagen. Standardization collagenase-based protocols has been hampered by impurities in products manufactured from Clostridium histolyticum . To enhance the purification process, we produced recombinant collagenase classes G and H, taking advantage Escherichia coli expression system. The respective gene sequences were derived C. modified addition a C-terminal polyhistidine tag. Harvested bacteria lysed protein was affinity purified using His-tag column. purity, identity, integrity eluted H determined SDS electrophoresis Western blot. proteolytic activity blend (rColGH) standard FALGPA assay. verified standardized method for isolation rat pancreatic islets. Biocompatibility validated viability assay on isolated Two batches rColGH compared commercially available collagenase. Based our results, conclude that is functional non-toxic novel worth further characterization optimization order make it competitive commercial product.