Fish collagen

Chitosan and Fish Collagen as Biomaterials for Regenerative Medicine... 

Fish collagen fibrillar gels have not been studied, with the exception of shark collagen (Nomura et al., 2000a,b), probably due to their low denaturation temperature (Tt]), which renders these materials difficult to handle. The Tt] of shark collagen solution is approximately 30°C (Nomura et al., 1995), which results in the dissolution of the fibrillar gel of this collagen at 37°C (Nomura et al., 2000a). This indicates that the gel could not be practically used at the actual physical temperature of human medical application. The Tt] of chum salmon is approximately 19 °C (Kimura et al., 1988 Matsui et al., 1991), which is the main reason to be unstable at the actual physical temperature of human body. As the... 

Rose, C. Mandal, A B. Interaction of SDS and Urea with Cat Fish Collagen Hydrodynamic, Thermodynamic, Conformation and Geometric Studies. Int. J. Biological Macromolecides, 1996,18,41-53. 

The third protein fraction in fish muscle is the connective tissue proteins, mostly collagens. Fish contains less collagen than land animal muscle, and the type of collagen is different in that it is more heat labile, and even in the native state does not form the same crosslinks as in land animal muscle, giving a tough texture. The fish collagen is thus much more delicate, and consequently can find alternative use. 

Pietrucha, K. and Banas, M. (2010). The effect of different methods of cross-linking of fish collagen on some its properties. http //www. bio-polymers.macromol.in. 

In the present work results of phosphorus-containing polypeptides on the base of some substrates (peptides, gelatin and fish collagen) synthesis research are presented. The chemical structure of a product, sorption properties and thermal-oxidative degradation are investigated. 

The template synthesis of increase capacity toward cations Cu + sorbents were carried out by addition into water suspension of fish collagen 50% cuprum sulfate water solution in mass relation of fish collage to CuSO as 5 1. Then the S5mthesis was conducted in same previous manner. For more effective desorption residual cations Cu from the polymeric die was applied double consecutive wash by 0.1 normal HCl solution, 0.1 normal NaOH solution and water until neutral pH. 

The fish collagen swells limited in water and produces a suspension, which stables in acid medium. The concentration of amino group according to formalin titration in the fish collagen was 1.1 mol/g. The fish collagen contains in 10% more amino group then the gelatin peptides. 

To decrease hydrolysis and swelling the fish collagen during phospho-nomethylation reaction sodium sulfate was added in reaction mixture as a graining reagent. The results of the experiment are presented in Table 3. 

The using of template synthesis permitted to increase SEC at 2-3 times, but led to diminish quantity of phosphorus in the product in few times. It ean be explained by inhibition of part of the reactionary centers (amino groups) of the fish collagen beeause the complexes of amino groups with eations Cu form and reduetion Cu to Cu passes during the synthesis. 

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