期刊
JOURNAL OF FUNCTIONAL FOODS
卷 35, 期 -, 页码 224-235出版社
ELSEVIER
DOI: 10.1016/j.jff.2017.05.032
关键词
Bighead carp; Bioactive peptides; Antioxidant; Dipeptidyl peptidase IV inhibition; Angiotensin converting enzyme inhibition; In silico prediction
资金
- Earmarked Fund for China Agriculture Research System [CARS-46]
- National Science and Technology Ministry of China [2017YFD0400200]
- Chinese Universities Scientific Fund [15056148]
- Tianjin Project of Transformation and Extension of Agricultural Science and Technology Achievements [201404020]
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 +/- 0.15 mu M) and relatively high ACE inhibitory capacity (IC50 = 3.68 +/- 0.13 mu M). Tyr-Asn-Leu-Lys-Glu-Arg-Tyr-Ala-Ala-Trp (IC50 = 1.35 +/- 0.23 mu M) and Tyr-Asn-Arg-Leu-Pro-Glu-Leu (IC50 = 3.42 +/- 0.39 mu M) 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 +/- 82.6 mu M. 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. (C) 2017 Elsevier Ltd. All rights reserved.
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