Fish Collagen – Molecular Structure After Thermal Treatment

Modern medicine widely uses exogenous collagen as a good material for tissue regeneration, also as a natural substrate for cell attachment and proliferation, used to create dressings and to support the treatment of burn and diabetic wounds, or finally as a source of amino acids in the form of a dietary supplement. Collagen is a safe material that has high biocompatibility and biodegradability as well as good cell adhesion. Due to the possibility of transferring Creutzfeld-Jacob’s disease (Bovine Spongiform Encephalopathy) from animals to the human body, interest in collagen from fish is currently increasing. The collagen we examined was derived from the skin of the silver carp fish (Hypophtalmichthys molitrix) and was obtained by the method of hydration in an aqueous lactic acid solution. The topography of the test sample was performed with the AFM method, showing its fibrillar structure with dimensions equivalent to those given in iterature. Raman spectroscopy was used to study fish collagen using a Renishaw Ramanscope with a helium-neon laser at a wavelength of 633 nm. Analysis of Raman spectra allowed to determine the content of amino acids in collagen, as well as glycine, proline and hydroxyproline. It also showed the native nature of the material at 20 °C. The partial renaturation of the secondary structure of this material heated to about 85 °C and cooled was also proved. Raman spectroscopy has been presented as an effective method for testing biopolymers.