The Isolation and Separation of Hydrophobic Bioactive Peptide Obtained From Tilapia ( <scp> <i>Oreochromis niloticus</i> </scp> ) Skin Hydrolysate Using Macroporous Resins

Recently, tilapia fish skin (TFS) has been applied to treat wounds. However the biological compounds in TFS have not been identified yet. Therefore, the objective of this study is to isolate and purify specific hydrophobic bioactive peptides using macroporous resin (XAD 7HP). Recovery rates for total peptides obtained by Bacillus licheniformis alcalase and Aspergillus oryzae protease were (81.26% ± 0.19%) and (80.21% ± 0.18%). Both purified hydrophobic bioactive peptides obtained by protease (BBPP) and alcalase (BBPA) presented high antioxidant capacity (30.4 ± 0.5) and (42.1 ± 0.6) mg trolox/g peptides, respectively, measured by the FRAP method. BBPA and BBPP presented significant antimicrobial activity, with inhibition halo diameters of (10 and 11.3 mm) for Staphylococcus aureus and (12.2 and 13 mm) for Pseudomonas aeruginosa, respectively. BBPA and BBPP showed antinociceptive activity presented by the significant effect to decrease the number of abdominal contortions; BBPA (10 mg/kg) showed greater capacity than indomethacin (20 mg/kg). Liquid chromatography-mass spectrometry (LC-MS) identified the primer sequence of amino acids of BBPA as the following: HYP, ASP, SER, GLU. GLY, HIS, ARG, THR, ALA, PRO, TYR, VAL, LYS, ILE, LEU, and PHE. Therefore, BBPA can be used for different applications in the food and pharmaceutical areas.