فهرست نشریات علمی دسترسی آزاد ایران

Marine-derived collagen has attracted increasing attention as a sustainable and halal alternative to terrestrial sources; however, detailed chemical and peptide-level characterization of collagen from tropical sea cucumbers remains limited. In this study, Type I collagen was isolated from Holothuria scabra collected from a tropical coastal region in Southeast Asia using a three-stage extraction protocol involving alkaline pretreatment, acetic acid hydrolysis, and phosphate-buffer extraction. The extracted collagen was subjected to comprehensive chemical characterization and peptide profiling using liquid chromatography–electrospray ionization mass spectrometry (LC–ESI–MS). Quantitative analysis revealed a protein content of 44.8%, indicating effective removal of non-collagenous components during pretreatment. LC–ESI–MS profiling identified characteristic peptide fragments corresponding to collagen-specific amino acid sequences, with dominant ions observed at m/z 372.4, 429.3, 585.3, and 673.4, attributed to proline-, glycine-, arginine-, and serine-containing peptides, respectively. Fragmentation analysis suggested a conserved Gly–Pro–X motif consistent with the primary structure of Type I collagen, while revealing peptide signatures distinct from those of bovine-derived collagen. Collectively, these molecular-level findings provide new chemical insight into marine collagen architecture and highlight the potential of H. scabra as a viable, halal, and sustainable biomaterial for biomedical and pharmaceutical applications.