Structural, physicochemical properties and function of swim bladder collagen in promoting fibroblasts viability and collagen synthesis

Collagen is an active macromolecule, but direct comparisons between different sources were scarce. The purpose of this study was to compare collagen from three fish species to find a collagen with higher bioactivity. Collagen from the swim bladder of Ctenopharyngodon idella, Nibea coibor and Protonibea diacanthus were isolated and named CASC, NASC and PASC, respectively. SDS-PAGE and spectroscopic analysis indicated that ASCs contained triple-helix type I collagen. The microstructure of collagen after lyophilization was uniform and porous. In addition, DSC analysis of the ASCs showed that the denaturation temperature (Td) and melting temperature (Tm) were 79 °C–93 °C and ∼216 °C, respectively. Moreover, the antioxidant activity of ASCs and its effect on fibroblast viability and collagen synthesis were investigated. Current studies have shown that ASCs had antioxidant capacity and were not toxic to fibroblasts. NASC had a higher antioxidant capacity (Hydroxyl, DPPH and ABTS radical scavenging rates were 33.73%, 33.49% and 89.81%, respectively) and significantly promoted fibroblast viability compared to the other two ASCs. It was further found that NASC can promote collagen synthesis in fibroblasts. Collagen extracted from swim bladder may be a promising functional product for the food, cosmetics and biomedical fields.