Journal
JOURNAL OF FUNCTIONAL FOODS
Volume 16, Issue -, Pages 234-242Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jff.2015.04.042
Keywords
Ctenopharyngodon idella; Hydrolysate; Antioxidant activity; Peptides
Categories
Funding
- National Natural Science Foundation of China [31401478, 31471639]
- National Key Technologies R&D Program of China [2012BAD29B06]
- Doctoral Program of Higher Education of China [20113326130001]
Ask authors/readers for more resources
Protein derived from grass carp (Ctenopharyngodon idella) skin was hydrolyzed by using Alcalase to obtain antioxidant peptides. Three antioxidant peptides were isolated from the protein hydrolysate and their amino acid sequences were determined to be Pro-Tyr-Ser-Phe-Lys (640.74 Da), Gly-Phe-Gly-Pro-Glu-Leu (618.89 Da) and Val-Gly-Gly-Arg-Pro (484.56 Da). The three purified peptides exhibited high scavenging activity on DPPH radical (IC50 2.459, 3.634 and 6.063 mM, respectively), hydroxyl radical (IC50 3.563, 2.606 and 4.241 mM, respectively) and ABTS radical (IC50 0.281, 0.530 and 0.960 mM, respectively) in a dose-dependent manner. In addition, all peptides also effectively inhibited the peroxidation in linoleic acid model system. The high activity of purified peptides was attributed to the small sizes and the peculiar amino acid residues within their peptide sequences. Results indicated that the novel peptides isolated from grass carp skin possess potent antioxidant activities and might be used for food preservation and medicinal purposes. However, more detailed studies are required to explore their antioxidant abilities in vivo. (C) 2015 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available