Isolation and characterisation of acid soluble collagens and pepsin soluble collagens from Eel (Anguilla japonica Temminck et Schlegel) skin and bone

Abstract

Eel (Anguilla japonica) is an important and valuable food fish in East Asia and its by-products have been reported to include bioactive and profitable components. This study aimed to extract, characterise, and compare the structure and properties of acid-soluble collagens (ASCs) and pepsin-soluble collagens (PSCs) from the skin and bone of eel (Anguilla japonica), providing insights into their composition, structure, and properties for various applications. The yields of ASC-S (from skin), PSC-S (from skin), ASC-B (from bone), and PSC-B (from bone) were 12.16%, 15.54%, 0.79%, and 1.34% on a dry weight basis, respectively. Glycine, the dominant amino acid, accounted for 16.66% to 22.67% of total amino acids in all samples. SDS-PAGE and FTIR analyses showed the typical triple-helical structure of type I collagen with slight variations in molecular order in extract and intermolecular cross-linking between skin and bone collagens. The denaturation temperature (Tmax1) measured by differential scanning calorimetry (DSC) is 81.39 °C and 74.34 °C, respectively, for ASC-B and ASC-S. Bone collagen has higher thermal resistance than skin collagen. Surface morphology imaged using a scanning electron microscope (SEM) showed that the bone collagen had a denser network structure, whilst the skin collagen was more fibrous and porous. The findings suggest that eel-derived collagens from skin and bone can serve as potential alternatives in the food, cosmetic, and healthcare industries.