Characterization of acid soluble collagen from skin of variable torpedo ray(Torpedo sinuspersici) and antibacterial activity

This study explores the extraction and characterization of acid-soluble collagen (ASC) from the skin of Torpedo sinuspersici , commonly known as the varied torpedo ray. The isolated collagen was analyzed using SDS-PAGE, UV–visible spectroscopy, Fourier-transform infrared (FTIR) spectroscopy, and scanning electron microscopy (SEM). SDS-PAGE confirmed the presence of type I collagen, comprising two α chains (α1 and α2, ∼92 kDa) and one β chain (∼172 kDa). UV–visible analysis showed a characteristic absorbance below 250 nm, while FTIR spectra revealed prominent amide bands (A, B, I, II, and III), indicating key functional groups. SEM imaging provided insights into the collagen’s crystalline structure. High-performance liquid chromatography (HPLC) revealed glycine as the dominant amino acid, followed by proline and hydroxyproline. The findings highlight the potential of ray fish skin as a sustainable source of collagen, with demonstrated antibacterial activity against clinically relevant bacterial strains. These results support its application in developing biomaterials with antimicrobial properties.