Histological Distribution and Characterization of Collagen in European eel (Anguilla anguilla) Muscle

Abstract

ABSTRACTThe histologic structure of eel muscle was observed, and the acid solubilized collagen (ASC) and pepsin solubilized collagen (PSC) from eel muscle were prepared and examined. The collagenous fiber amount in both head and tail seemed to be higher than that in the trunk. The Glu, Asp, Arg, Ala, Leu, and Lys contents accounted for about 54% of total amino acids in the eel muscle. There were no significant differences in the amino acid composition and ultraviolet spectra between ASC and PSC. The molecular weights of α1 subunit in both collagens were 129 and 123 kDa, respectively; but their molecular weights of α2 subunit were 113 kDa. According to peptide mapping analysis, it was found that there were obvious differences in primary structures between ASC and PSC. The amide A band positions of ASC and PSC appeared at 3320 cm−1 and 3312 cm−1 of Fourier transform infrared spectra, respectively. No obvious difference was found in the thermal stability of both collagens, probably due to the synergistic effect of molecular weight and hydrogen bonds.