RESUMO
Collagens extracted from different tissues and fish species display different physicochemical properties, thus novel sources require characterization. Gulf corvina (Cynoscion othonopterus) is processed industrially for food. Of the by-products, the swim bladder is used for fish maw, but other tissues are treated as waste. In the present study, pepsin-soluble collagen from Gulf corvina skin and swim bladder was extracted and characterized. Skin produced a higher collagen yield (82 ± 1.53 %) than swim bladder (69 ± 1.60 %). Both collagens exhibited electrophoresis bands corresponding to ([α1(I)]2α2(I)) and ß chains, all characteristic of type I collagen. Spectra analysis showed the collagens to maintain their triple-helix structure. The skin collagen had a lower denaturation temperature (29.8 °C) than the swim bladder collagen (32.5 °C), due to its relatively low imino acid content (168 vs. 190 /1000 residues, respectively). Both collagens were highly soluble in acidic pH ranges; Zeta potential values were 5.5 for the skin collagen and 6.2 for the swim bladder collagen. Gulf corvina skin and swim bladder are excellent sources of type I collagen with similar physicochemical properties.
