Properties of collagen extracted from Amur sturgeon Acipenser schrenckii and assessment of collagen fibrils in vitro

The objective of this study was to assess the nature of the collagens from the Amur sturgeon to determine its possibility as a potential collagen source for biomedical applications. From a sturgeon (1.22 kg), 6.0 g (dry wt) of skin collagen (SC), 4.1 g of swim bladder collagen (SBC), and 0.4 g of notochord collagen (NC) were obtained. SC and SBC were characterized as type I, and NC as type II collagen. Denaturation temperatures of SC, SBC, and NC were calculated as 28.5, 30.5, and 33.5 °C, respectively. Gene expression of the type I procollagen α2 chain of Amur sturgeon (ascol1a2) was specifically higher than ascol1a1 expression in the swim bladder, suggesting a unique composition of α chains in this organ. SC and SBC had better abilities of fibril formation with unique higher-order structures compared with porcine type I collagen. The maximum transition temperature (Tm) of reassembled fibrils formed in a buffer solution containing NaCl at 0 and 140 mM was 34.4 °C and 38.9 °C in SC, and 40.1 °C and 40.7 °C in SBC, respectively. These characteristic features suggested that sturgeon collagens could be used in the biomedical industries in future applications. •A significant quantity of type I and type II collagen could be extracted from Amur sturgeon.•Biochemical properties of both type I and type II collagens were studied, and organ collagen specificity was found.•Skin collagen and swim bladder collagen had better abilities of fibril formation compared with porcine type I collagen.•Analysis of the characteristics of the primary structure of type I collagen at the molecular level was clarified.