Comparison of collagen characteristic from the skin and swim bladder of Gulf corvina (Cynoscion othonopterus)
| Autor: | Yadira Cortes-Santiago, Luis M. Enríquez-Paredes, Sergio Rodríguez-Morales, Lus M. López, Honorio Cruz-López, Luis Jesús Villarreal-Gómez, Leticia Olivera-Castillo |
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| Rok vydání: | 2021 |
| Předmět: |
Fish Proteins
chemistry.chemical_classification Air Sacs Imino acid Fish species Cell Biology General Medicine Biology Molecular biology Collagen Type I Perciformes chemistry Swim bladder Animals Fish Denaturation (biochemistry) Cynoscion othonopterus human activities Type I collagen Skin Developmental Biology |
| Zdroj: | Tissue and Cell. 72:101593 |
| ISSN: | 0040-8166 |
| Popis: | 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 β 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. |
| Databáze: | OpenAIRE |
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