Isolation of antioxidative and ACE inhibitory peptides from protein hydrolysate of skipjack (Katsuwana pelamis) roe

被引:95
作者
Intarasirisawat, Rossawan [1 ,2 ]
Benjakul, Soottawat [1 ]
Wu, Jianping [2 ]
Visessanguan, Wonnop [3 ]
机构
[1] Prince Songkla Univ, Fac Agroind, Dept Food Technol, Hat Yai 90112, Songkhla, Thailand
[2] Univ Alberta, Dept Agr Food & Nutr Sci, Edmonton, AB T6G 2P5, Canada
[3] Natl Sci & Technol Dev Agcy, Natl Ctr Genet Engn & Biotechnol, Klongluang 12120, Pathum Thani, Thailand
基金
加拿大自然科学与工程研究理事会;
关键词
Skipjack roe; Angiotensin I converting enzyme (ACE); Antioxidant; Bioactive peptides; Isolation; Characterisation; SPONTANEOUSLY HYPERTENSIVE-RATS; ANGIOTENSIN-CONVERTING ENZYME; FRAME PROTEIN; GELATIN HYDROLYSATE; PURIFICATION; IDENTIFICATION; MUSCLE;
D O I
10.1016/j.jff.2013.09.006
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
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.
引用
收藏
页码:1854 / 1862
页数:9
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