Physicochemical Properties and Biocompatibility Evaluation of Collagen from the Skin of Giant Croaker ( Nibea japonica )

Collagen and collagen peptides are widely used as cosmetic ingredients. In the present study, acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were extracted from giant croaker ( ) skin. The proline hydroxylation rates of ASC and PSC were 38.1% and 39.3%. The denaturation temperatures (T ) were approximately 34.5 °C for both ASC and PSC. The results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fourier transform infrared spetroscopy (FTIR) demonstrated that ASC and PSC were mainly type I collagen. Furthermore, As, Pb and Hg contents in the extracted collagen were lower than the national standards of China. In addition, collagen had good moisture absorption and retention properties when compared to glycerol. The collagen was also not cytotoxic to NIH-3T3 fibroblast cells, indicating that skin collagen can be utilized in cosmetic applications.