Comparation of in vitro fibril-forming properties and antioxidant activities of collagen extracted from four by-products (skin, fin, cartilage, notochord) of sturgeon (Acipenser gueldenstaedti)

Abstract

Abstract To efficient utilize sturgeon by-products, we clarified and compared the structural and biological properties of collagens extracted from fin, skin, notochord, and cartilage of sturgeon. The structural properties of collagen were analyzed by SDS-PAGE and FTIR. The in vitro biological properties of four sturgeon collagen were evaluated from fibril-forming ability of collagen molecule and the antioxidant activity of low molecular collagen peptides. Collagen fibril-forming ability and morphology were detected by turbidity assay and SEM observation. The antioxidant activities of collagen peptides were determined by Hydroxyl and ABTS radical scavenging assay. SDS-PAGE results showed that the main type of skin and fin collagen was attributed to type I collagen, and that of cartilage and notochord collagen was attributed to type II collagen. FTIR results revealed four collagens maintained intact triple helical structure. Type II collagens could self-assemble into fibrils only at low phosphate ion concentration, whereas type I collagens could self-assemble into fibrils at long range of phosphate ion concentration. The fibril diameter of type I collagen was higher than that of type II collagen. The antioxidant activity of notochord and skin collagen peptides was higher than that of the other two collagen peptides. The results of this study will provide helpful information for the application of sturgeon collagen in the functional food and biomedical material industries. Meanwhile, it will promote the effective use of collagen from different sturgeon by-products.