Physicochemical and functional properties of fish skin collagen hydrolysate extracted using microbial protease

The hydrolyzed form of collagen demonstrates various biological activities that are absent in its native structure. Enzymatic hydrolysis is frequently utilized to generate collagen hydrolysate from different animal tissues. However, the application of microbial proteases in this process is not widely documented. The resulting peptide fractions can vary considerably based on the collagen source and the specific enzymes employed. Extracting crude enzymes from microbial sources, which tend to be more economical than commercial proteases, has shown considerable promise for liberating bioactive peptides from collagen. Furthermore, the functional characteristics of the resulting hydrolysate can be improved by selecting appropriate enzymes and optimizing hydrolysis conditions. Despite this potential, the use of microbial proteases for such applications remains largely underexplored. This study intends to identify local microbial protease sources for the preparation of collagen hydrolysate from barramundi fish skin. The collagen hydrolysis process will be evaluated based on physicochemical parameters, including the degree of hydrolysis, hydroxyproline content, morphological analysis via scanning electron microscopy (SEM), and identification of chemical structure using Fourier Transform Infrared (FTIR) spectroscopy. Additionally, the biological activity, particularly the antioxidative potential of the collagen hydrolysate, will be assessed. The effectiveness of collagen hydrolysis using microbial proteases derived from bacterial and fungal sources will be compared with that of commercial proteases.