Characterization of collagen from haddock skin and wound healing properties of its hydrolysates.

Collagen, one of the most abundant structural proteins found in vertebrates, has been extensively used for biomedical applications. The objectives of this study were to isolate and characterize acid-soluble collagen (ASC) from haddock (Melanogrammus aeglefinus) skins and to investigate the biological function of ASC hydrolysates in wound healing. Amino acid composition, SDS-PAGE and FTIR suggested that the ASC is most likely type I collagen with well-maintained helical structures. Both the denaturation and shrinkage temperatures of ASC isolated from haddock skins were lower than those of mammalian collagens. The average molecular weights of hydrolysates decreased with the increase in HCl concentration as well as hydrolysis times. ASC and hydrolysates with more molecules (53.8 kDa) decreased the bleeding and clotting times and promoted order 2 vessel formation effectively. All the experimental groups, including the ASC group and its hydrolysate groups, could accelerate epithelialization and shorten the wound healing time of mice. The ASC from haddock skin could therefore serve as an alternative collagen for skin wound healing.