4.7 Article

Production and identification of antioxidant and angiotensin-converting enzyme inhibition and dipeptidyl peptidase IV inhibitory peptides from bighead carp (Hypophthalmichthys nobilis) muscle hydrolysate

Journal

JOURNAL OF FUNCTIONAL FOODS
Volume 35, Issue -, Pages 224-235

Publisher

ELSEVIER
DOI: 10.1016/j.jff.2017.05.032

Keywords

Bighead carp; Bioactive peptides; Antioxidant; Dipeptidyl peptidase IV inhibition; Angiotensin converting enzyme inhibition; In silico prediction

Funding

  1. Earmarked Fund for China Agriculture Research System [CARS-46]
  2. National Science and Technology Ministry of China [2017YFD0400200]
  3. Chinese Universities Scientific Fund [15056148]
  4. Tianjin Project of Transformation and Extension of Agricultural Science and Technology Achievements [201404020]

Ask authors/readers for more resources

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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