Comparison of collagen characteristics of sea- and freshwater-rainbow trout skin

Abstract

Proximate composition, volatile basic nitrogen content, and concentrations of collagen in skin samples from either sea- (S-RT) or freshwater-rainbow trout (F-RT) were characterized and compared, to assess the effect of the sea or freshwater habitat on these parameters. Results of amino acid composition, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, thermal denaturation assay and Fourier transform infrared (FT-IR) spectroscopy of acid-soluble collagens were comparable between the two sample sets. Both acid-soluble collagens from sea- and freshwater-rainbow trout skins contained glycine as the major amino acid and high alanine, proline, and hydroxyproline contents, and was found to be predominantly composed of alpha 1-, alpha 2-, and beta-chains. FT-IR spectra of ASCs from S-RT and F-RT skins were quite similar. These findings suggest that different rainbow trout habitats (seawater and freshwater) do not affect amino acid composition and molecular weight properties of ASCs from S-RT and F-RT skins.