Bacterial collagenase is the enzyme capable of breaking down native Type I collagen, specifically targeting the triple-helical domain. It cleaves collagen molecules at multiple sites within the triple helix, effectively breaking down the collagen structure into smaller peptides. This makes bacterial collagenase highly effective in the degradation of collagen, and it is commonly used in research and medical applications, including wound debridement and tissue culture.
While glycosidase, trypsin, and chymotrypsin are enzymes that act on various substrates, they are not capable of efficiently breaking down the collagen triple helix at multiple sites. Trypsin and chymotrypsin are proteases that cleave peptide bonds, but they are not specific to collagen. Glycosidase primarily acts on carbohydrates, not proteins.
Thus, bacterial collagenase is the enzyme capable of breaking down native Type I collagen at more than one site.