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| Content Provider | Springer Nature Link |
|---|---|
| Author | Yan, Mingyan Li, Bafang Zhao, Xue |
| Copyright Year | 2009 |
| Abstract | Collagen of squid (Ommastrephes bartrami) skin was examined in the present study. Histology showed that collagen fiber in the skin was partially cross-linked with muscle fiber. Acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were extracted from the skin and characterized. The results of amino acid composition and electrophoretic patterns revealed that ASC and PSC were both type I collagen, containing α1 and α2 chains. FTIR (fourier transform infrared spectroscopy) investigations confirmed the existence of helical arrangements in PSC of squid skin. The denaturation temperature (T$_{d}$) and shrinkage temperature (T$_{s}$) of PSC were 29.4°C and 52.8°C, respectively. |
| Starting Page | 191 |
| Ending Page | 196 |
| Page Count | 6 |
| File Format | |
| ISSN | 16725182 |
| Journal | Journal of Ocean University of China |
| Volume Number | 8 |
| Issue Number | 2 |
| e-ISSN | 19935021 |
| Language | English |
| Publisher | SP Science Press |
| Publisher Date | 2009-04-24 |
| Publisher Place | Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | isolation characterization collagen thermal stability squid Oceanography |
| Content Type | Text |
| Resource Type | Article |
| Subject | Oceanography Ocean Engineering |
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