Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process
| Autor: | Víctor Manuel Ocaño-Higuera, Wilfrido Torres-Arreola, Octavio Cota-Arriola, Betzabe Ebenhezer Lopez-Corona, Enrique Márquez-Ríos, Hugo E. Ramírez-Guerra, Josafat Marina Ezquerra-Brauer |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Cooking process
Connective tissue lcsh:TX341-641 chemistry.chemical_compound 0404 agricultural biotechnology Pepsin medicine Cooking Fourier transform infrared spectroscopy Pyridinoline Chromatography biology lcsh:TP368-456 Jumbo squid 04 agricultural and veterinary sciences 040401 food science Electrophoresis lcsh:Food processing and manufacture medicine.anatomical_structure chemistry Solubilization biology.protein Muscle Collagen lcsh:Nutrition. Foods and food supply Food Science Cross-linking |
| Zdroj: | International Journal of Food Properties, Vol 21, Iss 1, Pp 821-834 (2018) |
| ISSN: | 1532-2386 1094-2912 |
| Popis: | Collagen is the major connective tissue (CT) protein and one of the main constituents of the jumbo squid (Dosidicus gigas). Therefore, physicochemical changes of pepsin-solubilized collagen (PSC) and insoluble collagen (IC) were studied after cooking (100°C/30 min) of muscle (mantle, fins, and arms). Different pyridinoline (Pyr) contents (the major cross-linking molecule in collagen fibers) were found in the fresh muscle of the three anatomical regions. After the cooking process, a decrease from 10 to 30% in the thermal resistance of collagen was observed, depending on the anatomical region and fraction evaluated. Furthermore, the electrophoretic profile, Fourier transform infrared (FTIR) spectroscopy, and the amino-acid profile revealed that structural changes occurred in the two different collagen fractions caused by the thermal process, and the changes were greater in the mantle. Under the conditions applied in this study, collagen fractions from the squid arms showed more stability during the cooking process due to the high cross-linking degree of their fibers. |
| Databáze: | OpenAIRE |
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