Journal
JOURNAL OF FUNCTIONAL FOODS
Volume 5, Issue 4, Pages 1854-1862Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jff.2013.09.006
Keywords
Skipjack roe; Angiotensin I converting enzyme (ACE); Antioxidant; Bioactive peptides; Isolation; Characterisation
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Funding
- Office of the Higher Education Commission
- CHE Ph.D. Scholarship
- TRF Senior Research Scholar Program
- Natural Sciences and Engineering Research Council of Canada
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Bioactive peptides from protein hydrolysate of defatted skipjack (Katsuwonus pelamis) roe with 5% degree of hydrolysis (DH) prepared by Alcalase digestion were isolated and characterised. Two active fractions with ABTS radical scavenging activity (973.01-1497.53 mu mol TE/mg sample) and chelating activity (0.05-0.07 mu mol EE/mg sample) from consecutive purification steps including ultrafiltration, cation exchange column chromatography and reverse phase high performance liquid chromatography (RP-HPLC), were subjected to analysis of amino acid sequence by LC-MS/MS. Seven dominant peptides with 6-11 amino acid residues were identified as DWMKGQ MLVFAV, MCYPAST, FVSACSVAG, LADGVAAPA, YVNDAATLLPR and DLDLRKDLYAN. These peptides were synthesised and analysed for ACE-inhibitory activity and antioxidative activities. MLVFAV exhibited the highest ACE inhibitory activity (IC50 = 3.07 mu M) (p < 0.05) with no antioxidative property, whilst DLDLRKDLYAN showed the highest metal chelating activity, ABTS radical and singlet oxygen scavenging activities. Therefore, peptides prepared from skipjack roe could be further employed as a functional food ingredient. (C) 2013 Elsevier Ltd. All rights reserved.
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