Comparative Characterization of Type‐I Collagen From Different Tissues of Labeo rohita With Potential for Dermal Applications

ABSTRACT

Collagen provides multifunctional pharmacological benefits to skin; a comparatively promising source of collagen from fish processing trimmings/by‐products would be necessary for various dermal applications. Therefore, this research identifies different sections of rohu fish ( Labeo rohita ), such as bones (FCB), muscles (FCM), and scales (FCS), as sources for collagen. Herein, collagen content was compared among different fish tissues, where the extraction was carried out using an acid‐soluble method followed by pepsin digestion. Biochemical analysis of FCM revealed the presence of 92.61% ± 1.607% collagen out of the total protein content, which was significantly greater than in FCB and FCS. HPLC analysis showed that FCM was rich in hydroxyproline (295.8 ± 0.021 residues per 1000 residues) and proline (32.15 ± 0.003 residues per 1000 residues), which are the highly dominant amino acids in Type‐I collagen. Distinct α ₁ and α ₂ chains were observed for the extracted collagen‐rich sample using gel electrophoresis, indicating the presence of Type‐I collagen. Furthermore, surface morphology analysis of the extract revealed a highly porous architecture. Approximately 50% weight loss was observed at 300°C during thermal degradation studies. The higher amino acid content of FCM accounted for its superior in vitro antioxidant properties against ABTS and DPPH free radicals (> 90%) compared to standard marine collagen. Pepsin digestion of acid‐soluble collagen improved its antimicrobial properties against E. coli and S. aureus due to the probable exposure of bioactive peptides. Additionally, collagen extracted at different concentrations maintained HaCaT cell viability > 90%, indicating that fish muscle could be a promising source of collagen for dermal applications.