Turkish Journal of Veterinary & Animal Sciences




In the current study gelatin was recovered from scales of farmed sea bass (Dicentrarchus labrax). The first part of the study was planned to determine the yield of acid-soluble collagen and pepsin-soluble collagen from the scales. Both collagens were characterized as type I collagen, containing \alpha-1 and \alpha-2 chains. In the second part, gelatin was extracted using acetic acid and functional properties were determined in this product. Gelatin protein value was found to be 96% and the yield was found to be 18.49%. Proline and hydroxyproline values in the amino acid were found to be high. The gel strength of gelatin was 305 g and viscosity of the gelatin was 33 cP. The gelatin was identified as type A gelatin due to its properties. Fourier transform infrared spectroscopic analysis showed the characteristic similarities of gelatin produced from sea bass scales and calf skin.


Collagen, gelatin, gel strength, sea bass scales, imino acids

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