Comprehensive analysis of collagen: unveiling the distinctive characteristics and amino acid profiles from skin and bone of Mesopotamian spiny Eel, Mastacembelus mastacembelus (Banks & Solander, 1794)

Abstract

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) and skin (ASC-S) of the Mesopotamian spiny eel, Mastacembelus mastacembelus (Banks & Solander, 1794). Notably, this research marks the inaugural exploration of this species as a collagen source. Both ASC-S and ASC-B from spiny eel skin and bone exhibited glycine as the predominant amino acid, constituting 29.88 and 29.77 g/100g of collagen for ACS-S and ACS-B, respectively. 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 both ACS-S and ASC-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 spiny eel emerges as a potential alternative source of vertebrate collagens with prospective applications in diverse industries, including diet, medical, and pharmaceutical sectors.