Abstract
We investigated bioactive peptides obtained from muscle protein hydrolysate of bighead carp by evaluating in vitro dipeptidyl peptidase IV (DPP-IV) and angiotensin-converting enzyme (ACE) inhibitory capacities and antioxidant activity. Peptide sequences were identified from pepsin hydrolysates. Met-Lys-Ala-Val-Cys-Phe-Ser-Leu was one of the most effective sequences with 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity (EC50=4.58±0.15μM) and relatively high ACE inhibitory capacity (IC50=3.68±0.13μM). Tyr-Asn-Leu-Lys-Glu-Arg-Tyr-Ala-Ala-Trp (IC50=1.35±0.23μM) and Tyr-Asn-Arg-Leu-Pro-Glu-Leu (IC50=3.42±0.39μM) exhibited the most potent ACE inhibitory activity. Ile-Ala-Asp-His-Phe-Leu showed the highest DPP-IV inhibitory activity with an IC50 value of 610.1±82.6μM. All selected peptides were non-toxic, and most were non-allergenic according to in silico predictions. These results indicate the promising potential of bighead carp muscle hydrolysates as functional additives in foods and pharmaceuticals.
Published Version
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