Generation and Characterization of Novel Bioactive Peptides from Fish and Beef Hydrolysates

Bioactive peptides were successfully produced from fish (Gadidae) and beef skeletal muscles after being hydrolyzed for 8 h with pepsin. Subsequently, they purified using a Sep-Pak C18 cartridge reversed-phase high-performance liquid chromatography (RP-HPLC). The molecular weights of pure determined to be 2364.4 3771.8, respectively. According Edman degradation, the peptide was composed 21 amino acid residues (F21), while 34 (B34). F21 B34 displayed angiotensin-converting enzyme inhibitory activity half maximal concentration (IC50) values 7.3 µg/mL 5.8 µg/mL, exhibited antioxidant an IC50 value 389.9 whereas no activity. Moreover, antimicrobial effects against wide spectrum food-borne pathogens spoilage bacteria. derived muscle proteins are promising strategy production functional food materials safe preservatives.