| Abstrakt: |
Collagen was previously derived from bovine and porcine sources, but its usage is restricted due to its expensive cost, halal issue, and potential allergic reaction. This work utilized the soluble acid collagen (ASC) method to extract bioactive collagen components from commercial jellyfish captured from the Port Klang area in Malaysia, and 20% collagen yield from jellyfish was successfully extracted (based on the wet weight basis). The jellyfish collagen was confirmed to be type II collagen, which is made up of one α and one β chain, as confirmed by the SDS-PAGE pattern. The molecular weight of the α chain was 140 kDa. The amino acid composition in jellyfish collagen was identical to chicken foot type II collagen. The transition temperature (Tmax) of jellyfish collagen was obtained at 32°C, as determined by differential scanning calorimetry (DSC). Fourier Transform Infrared (FTIR) spectroscopy determines five significant collagen peaks: Amide A, Amide B, Amide I, Amide II, and Amide III, demonstrating the structure of jellyfish collagen. From the potential zeta study, the jellyfish collagen is stable up to pH nine, and the jellyfish collagen starts to denature at higher pH. Based on these findings, jellyfish collagen has a high potential to replace conventional bovine and porcine-based collagen as a sustainable and safer source of collagen for usage in various industries, especially in the nutraceuticals and cosmeceuticals industries. [ABSTRACT FROM AUTHOR] |
