Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry

被引:298
作者
Ren, Jiaoyan [1 ]
Zhao, Mouming [1 ]
Shi, John [2 ]
Wang, Jinshui [1 ]
Jiang, Yueming [3 ]
Cui, Chun [1 ]
Kakuda, Yukio [4 ]
Xue, Sophia Jun [2 ]
机构
[1] S China Univ Technol, Coll Light Ind & Food Sci, Guangzhou 510640, Peoples R China
[2] Agr & Agri Food Canada, Food Res Ctr, Guelph, ON N1G 5C9, Canada
[3] Chinese Acad Sci, S China Bot Garden, Guangzhou 510650, Peoples R China
[4] Univ Guelph, Dept Food Sci, Guelph, ON N1G 2W1, Canada
关键词
grass carp muscle; antioxidant peptides; high-speed counter-current chromatography; electrospray ionization-mass spectrometry;
D O I
10.1016/j.foodchem.2007.11.010
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Grass carp muscles were hydrolyzed with various proteases (papain, bovine pancreatin 6.0, bromelain, neutrase 1.5MG and alcalase 2.4L) to extract antioxidant peptides. The hydrolysates were assessed using methods of hydroxyl radical scavenging ability and lipid peroxidation inhibition activity. Hydrolysate prepared with alcalase 2.4L was found to have the highest antioxidant activity. It was purified using ultrafiltration and consecutive chromatographic methods including ion-exchange chromatography, multilayer coil high-speed counter-current chromatography, and gel filtration chromatography. The purified peptide, as a potent antioxidant, was identified as Pro-Ser-Lys-Tyr-Glu-Pro-Phe-Val (966.3 Da) using RP-HPLC connected on-line to an electrospray ionization mass spectrometry. As well, it was found that basic peptides had greater capacity to scavenge hydroxyl radical than acidic or neutral peptides and that hydrophobic peptides contributed more to the antioxidant activities of hydrolysates than the hydrophilic peptides. In addition, the amino acid sequence of the peptide might play an important role on its antioxidant activity. (C) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码:727 / 736
页数:10
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