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Atlantic cod is processed industrially for food purposes, with several by-products being directed to animal feed and other ends. Looking particularly into swim bladders, the extraction of collagen can be a valuable strategy for by-product valorization, explored in the present work for the first time. Collagen was extracted using acetic acid (ASCsb) and pepsin (PSCsb) with yields of 5.72% (w/w) and 11.14% (w/w), respectively. SDS-PAGE profile showed that the extracts were compatible with type I collagen. FTIR, CD and XRD results suggest that the PSCsb structure underwent partial denaturation, with microDSC showing a band at 54 ºC probably corresponding to a melting process, while ASCsb structure remained intact, with preserved triple helix and a denaturation temperature of 29.6 ºC. Amino acid composition indicates that the total content of proline-like amino acids was 148/1000 residues for ASCsb and 141/1000 residues for PSCsb, with a hydroxylation degree of about 37%. The extracts exhibited a typical shear thinning behavior, interesting property regarding their further processing toward the development of biomaterials. In this regard, assessment of metabolic activity of human fibroblast cells cultured in the presence of collagen extracts with concentrations up to 3mg/mL revealed the absence of cytotoxic behavior. Collagen extracts obtained from Atlantic cod swim bladders shown attractive properties regarding their use in cosmetic or biomedical applications. ; The authors would like to acknowledge to European Union for the financial support under the scope of European Regional Development Fund (ERDF) through the Structured Project NORTE-01-0145-FEDER-000021 (Norte2020) and under the scope of the European Union Seventh Framework Programme (FP7/2007-2013) through grant agreement ERC-2012-ADG 20120216-321266 (ERC Advanced Grant ComplexiTE). The Portuguese Foundation for Science and Technology is also acknowledged for the PhD grant of A. L. A under Doctoral Programme Do ~ Mar (PD/BD/127995/2016), as well as ...

The extraction of collagen from fish skins is being proposed as strategy for valorization of marine origin by-products, being a sustainable alternative to mammal collagen. The method commonly uses solutions of organic acids, but new methodologies are arising, aiming to improve process yields and/or the properties of the resulting products. In this work, skins removed from salt brine Atlantic cod (Gadus morhua) were used to extract collagen, using water acidified with CO2, obtaining an extraction yield of 13.8% (w/w). Acidified water extracted collagen (AWC) presented a total content of proline-like amino acids of 151/1000 residues, with a degree of hydroxylation of 38%, and its SDS-PAGE profile is compatible with type I collagen. Moreover, FTIR, CD and XRD results suggest the presence of preserved triple helix, having a denaturation temperature of 32.3 °C as determined by micro-DSC. AWC exhibited a typical shear thinning behavior, interesting regarding their further processing, namely in jelly-like formulations. Additionally, the presence of AWC in MRC-5 human fibroblasts culture did not affect cell viability, demonstrating the non-cytotoxic behavior. Overall, the results support the efficiency of the proposed approach for collagen extraction and further enable the design of methodologies to address AWC use in biomedical or cosmetic context. ; This work has received funding from European Union, under the scope of European Regional Development Fund (ERDF) through the Structured Project NORTE-01-0145-FEDER000021 (Norte2020) and under the scope of the European Union Seventh Framework Programme (FP7/2007-2013) through grant agreement ERC-2012-ADG 20120216-321266 (ERC Advanced Grant ComplexiTE). The Portuguese Foundation for Science and Technology is also acknowledged for the grant of A.L.A under Doctoral Programme Do* Mar (PD/BD/127995/2016) and for the PhD grant of C. O. (Norte08-5369-000037) with financial support by Norte 2020. The authors would like to acknowledge Frigoríficos da Ermida, Lda. (Gafanha da ...