Preliminary Study on the Functions of Peptides Obtained from White Mullet (Ophiocephalus argus var. Kimnra) Meat

To explore the functions of peptides obtained from white mullet (Ophiocephalus argus var. Kimnra) meat, the meat was hydrolyzed via simulated digestion in vitro, and the functions (milk secretion ability, antioxidant activity, angiotensin-converting enzyme (ACE) inhibitory activity, and Fe²⁺ chelation) of the obtained peptide were evaluated. The results indicated that both low-dose and high-dose peptide promoted milk secretion in lactating rats in vivo; the peptides had scavenging effects on free radicals of 1,1-diphenyl-2-trinitrophenylhydrazine (DPPH), 2,2'-azino-bis (3-ethylbenzo-thiazoline-6-sulfonic acid) diammonium salt (ABTS), OH^-, and O^2-, and the EC₅₀ concentrations were 55.94 mg/mL, 10.14 mg/mL, 52.92 mg/mL, and 28.53 mg/mL, respectively. The peptides had an inhibitory effect on ACE, and the IC₅₀ concentration was 15.81 mg/mL. The peptides had a chelating ability to Fe²⁺, and the IC₅₀ concentration was 69.05 mg/mL. These results indicate that peptides obtained from white mullet meat exhibit milk secretion-promoting ability, antioxidant activity, ACE-inhibitory activity, and Fe²⁺ chelation, making this an effective approach for isolating specific functional peptides and identifying their sequences from the digested solution of white mullet meat.