Exploring collagen diversity in the bone of mesopotamian catfish (Silurus triostegus, Heckel, 1843)

Collagen, a pivotal extracellular matrix biomolecule ubiquitous in connective tissues, drew substantial attention due to its widespread presence, notably in skin and bone. This pioneering study delves into the extraction, characterization, and amino acid profiling of acid-soluble collagens (ASC) obtained from the bone (ASC-B) of the Mesopotamian catfish, Silurus triostegus, (Heckel, 1843). Notably, this research marks the inaugural exploration of this species as a collagen source. Fourier transform infrared spectroscopy (FTIR) confirmed the integrated and native nature of both collagens, while X-ray diffraction (XRD) results indicated the preservation of helical structures in both skin and bone collagens. UV-Vis spectra highlighted prominent absorptions at 230 nm. SEM studies revealed the porous and fibrous structure of ACS-B Collectively considering UV–Vis and FTIR results alongside the amino acid composition, the extracted collagens were characterized as type I collagen. The collagen isolated from the catfish emerges as a potential alternative source of vertebrate collagens with prospective applications in diverse industries, including diet, medical, and pharmaceutical sectors.