Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process
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)...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2018-01-01
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| Series: | International Journal of Food Properties |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/10942912.2018.1477159 |
| _version_ | 1819142764461293568 |
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| author | Josafat M. Ezquerra-Brauer Enrique Márquez-Ríos Betzabe E. López-Corona Víctor M. Ocaño-Higuera Hugo E. Ramírez-Guerra Octavio Cota-Arriola Wilfrido Torres-Arreola |
| author_facet | Josafat M. Ezquerra-Brauer Enrique Márquez-Ríos Betzabe E. López-Corona Víctor M. Ocaño-Higuera Hugo E. Ramírez-Guerra Octavio Cota-Arriola Wilfrido Torres-Arreola |
| author_sort | Josafat M. Ezquerra-Brauer |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-22T12:15:32Z |
| format | Article |
| id | doaj.art-7eaf77e95854452d87c441e5139a1eac |
| institution | Directory Open Access Journal |
| issn | 1094-2912 1532-2386 |
| language | English |
| last_indexed | 2024-12-22T12:15:32Z |
| publishDate | 2018-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | International Journal of Food Properties |
| spelling | doaj.art-7eaf77e95854452d87c441e5139a1eac2022-12-21T18:26:10ZengTaylor & Francis GroupInternational Journal of Food Properties1094-29121532-23862018-01-0121182183410.1080/10942912.2018.14771591477159Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking processJosafat M. Ezquerra-Brauer0Enrique Márquez-Ríos1Betzabe E. López-Corona2Víctor M. Ocaño-Higuera3Hugo E. Ramírez-Guerra4Octavio Cota-Arriola5Wilfrido Torres-Arreola6Universidad de SonoraUniversidad de SonoraUniversidad de SonoraUniversidad de SonoraUniversidad de SonoraUniversidad Estatal de SonoraUniversidad de SonoraCollagen 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.http://dx.doi.org/10.1080/10942912.2018.1477159Jumbo squidMuscleCookingCollagenCross-linking |
| spellingShingle | Josafat M. Ezquerra-Brauer Enrique Márquez-Ríos Betzabe E. López-Corona Víctor M. Ocaño-Higuera Hugo E. Ramírez-Guerra Octavio Cota-Arriola Wilfrido Torres-Arreola Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process International Journal of Food Properties Jumbo squid Muscle Cooking Collagen Cross-linking |
| title | Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process |
| title_full | Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process |
| title_fullStr | Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process |
| title_full_unstemmed | Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process |
| title_short | Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process |
| title_sort | physicochemical changes of pepsin solubilized and insoluble collagen in jumbo squid dosidicus gigas muscle after cooking process |
| topic | Jumbo squid Muscle Cooking Collagen Cross-linking |
| url | http://dx.doi.org/10.1080/10942912.2018.1477159 |
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