Biochemical and Biological Characterization of Type-I Collagen from Scomberomorus commerson Skin as a Biomaterial for Medical Applications

Marine collagen, as a biomedical material, has been taken into consideration because of low immunogenicity, biodegradibility, as well as being water soluble, safe, and easily-extractable. We extracted acid-soluble collagen (ASC) from Scomberomorus commerson fish skin found in Persian Gulf, Iran and conducted chemical and physical characterizations using various techniques including thermo gravimetric analysis (TGA), scanning electron microscopy (SEM), X-ray diffraction, Fourier transformation infrared (FTIR), sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS-PAGE), and MTT assay of the ASC. Our results showed that the yield of ASC was 20.30%. SEM observation demonstrated that the structure of the extracted collagen was fibrils with irregular dense sheet-like structures. SDS-PAGE analysis showed that S.commerson ASC had α (α 1 and α 2 ) and β chains, presumably belonging to type I collagen. The amount of amino acids and proline in ASC was 18 per 1,000 residues and 90.7 per 706.1 residues, respectively. Also, 27.06% of the collagen was composed of glycine. FTIR analysis and the spectrum X-ray diffraction demonstrated that the S . commerson skin collagen had a triple-helix structure with the ASC denaturation temperatures of 45 °C and 291.89 ºC. Cell activity and proliferation testing demonstrated that S. commerson collagen sample promote cell growth and proliferation and its hydrophilicity leads to cell attachment. In conclusion, the S. commerson fish skin can perform as an affordable collagen source for medical biomaterials and pharmaceutical applications.