Chi Zhang, Yuqi Zhang, Zhiying Wang
Aug 1, 2017
Citations
3
Influential Citations
54
Citations
Journal
Journal of Functional Foods
Abstract
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 (EC 50 = 4.58 ± 0.15 μM) and relatively high ACE inhibitory capacity (IC 50 = 3.68 ± 0.13 μM). Tyr-Asn-Leu-Lys-Glu-Arg-Tyr-Ala-Ala-Trp (IC 50 = 1.35 ± 0.23 μM) and Tyr-Asn-Arg-Leu-Pro-Glu-Leu (IC 50 = 3.42 ± 0.39 μM) exhibited the most potent ACE inhibitory activity. Ile-Ala-Asp-His-Phe-Leu showed the highest DPP-IV inhibitory activity with an IC 50 value of 610.1 ± 82.6 μM. 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.