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 (Td) and shrinkage temperature (Ts) of PSC were 29.4°C and 52.8°C, respectively.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
