Fourier transform infrared spectroscopy analysis and anti-inflammatory properties of crude collagen solution andcollagen hydrogel of Tilapia fish Oreochromis niloticus

Collagen derived from tilapia fish, has the potential to compensate for the loss of collagen, provide antiinflammatory assistance, and can be used as a natural alternative source of treatment in the pharmaceutical field. Burn wounds causes prolonged influx of proinflammatory cytokines and immune cells, resulting in an extensive inflammatory period, that damages the extracellular matrix containing collagen. This study aimed to determine the collagenic functional groups of the crude collagen solution and collagenhydrogel of Oreochromis niloticus (O. niloticus), via Fourier Transform Infrared Spectroscopy (FTIR) analysis, and to evaluate its anti-inflammatory properties in vitro. The crude collagen fibril was extracted using the Acid Soluble Collagen (ASC) method. The collagen obtained was prepared into crude collagen solution and collagenhydrogel treatments and were eventually subjected to FTIR analysis. An anti-inflammatory test was conducted to evaluate the protein denaturation properties of the crude collagen solution and collagenhydrogel of concentration 1 mg/mL, 0.5 mg/mL, and 0.25 mg/mL. FTIR results revealed presence of Amide I and Amide A for both treatments, confirming for the presence of collagen. The anti-inflammatory test had displayed an inhibition for protein denaturation (p=0.002) for the crude collagen solution (21.006% -9.023%) and collagenhydrogel (51.573%-50.166%) of all concentrations. In conclusion, from the conducted FTIR analysis and anti-inflammatory test, the crude collagen solution and collagenhydrogel, obtained from O. niloticus, displayed the presence of the Amide I and Amide A, as well as anti-inflammatory properties.