Study on some characteristics of fish scale collagen modified by UV irradiation

Collagen is a structural protein composed of three alpha-chains wound together in a tight triple helix, occurring abundantly in the skin and connective tissues of mammals, as well as other clades of the animal kingdom. Many studies have demonstrated that collagen has good biocompatibility and contains essential amino acids of great value to the medical and pharmaceutical industry. In this study, collagen was extracted from common carp (Cyprinus carpio) scales and physically modified by UV irradiation. Methods of IR, HPLC and FESEM analysis were used for determination of functional group, chemical composition and morphological changes of modified collagen samples. The denaturation temperature of collagen samples was determined based on the change in relative viscosity of collagen solution as increasing temperature from 10 C-o to 50 C-o. Finally, hemostatic activity of the modified collagen samples was assessed in vitro. The obtained results showed that UV-treatment of collagen led to significant changes in its properties. After UV treatment, the thermal stability and hemostatic ability of modified collagen samples was improved. Overall, total irradiation duration of 3.6s to 6s was adequate, and produced collagen samples with improved thermal stability and hemostatic activity.