Purification and characterization of a natural antioxidant peptide from fertilized eggs

被引:47
作者
Duan, Xiang [2 ]
Ocen, Denis [2 ]
Wu, Fengfeng [2 ]
Li, Mei [2 ]
Yang, Na [2 ]
Xu, Jin [2 ]
Chen, Haiying [2 ]
Huang, Liqun [3 ]
Jin, Zhengyu [1 ,2 ]
Xu, Xueming [1 ,2 ]
机构
[1] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China
[2] Jiangnan Univ, Sch Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China
[3] Chinese Inst Radiat Protect, Taiyuan 030006, Shanxi Province, Peoples R China
关键词
Antioxidant; Chromatography; Fertilized egg; Peptide; Secondary structure; RADICAL-SCAVENGING PEPTIDE; PROTEIN HYDROLYSATE; ENZYMES; OVOTRANSFERRIN; SYSTEM; YOLK; SKIN;
D O I
10.1016/j.foodres.2013.12.016
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Fertilized hen eggs are traditionally considered as dietary supplements in many Asian countries. This work aimed to obtain information on antioxidant peptides derived from fertilized eggs. Antioxidant activities were evaluated by measuring reducing power, DPPH radical scavenging activity and inhibition of pyrogallol autoxidation. During 15 days of incubation, the antioxidant activity of peptides increased with increasing incubation time. The peptides on day 15 were employed for isolation of antioxidant peptide. An antioxidant peptide, HLFGPPGKKDPV (MW: 1291.51 Da), was purified by consecutive chromatographic methods. The purified peptide was a novel peptide corresponding to the fragment 302-313 of ovotransferrin. The conformational prediction and Fourier transform infrared spectroscopy suggested that the peptide existed in beta-sheet. Furthermore, the peptide showed an inhibition ratio of 60.20% on linoleic acid autoxidation and an inhibitory effect on ABTS radicals (IC50: 312 mu M). These results suggested that fertilized eggs could be explored as a source of antioxidant peptides. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:18 / 24
页数:7
相关论文
共 37 条
[1]   Purification and antioxidant properties of octapeptide from salmon byproduct protein hydrolysate by gastrointestinal digestion [J].
Ahn, Chang-Bum ;
Kim, Jeong-Gyun ;
Je, Jae-Young .
FOOD CHEMISTRY, 2014, 147 :78-83
[2]   Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis [J].
Dávalos, A ;
Miguel, M ;
Bartolomé, B ;
López-Fandiño, R .
JOURNAL OF FOOD PROTECTION, 2004, 67 (09) :1939-1944
[3]   Development of antioxidant capacity in tissues of the chick embryo [J].
Gaal, T ;
Mezes, M ;
Noble, RC ;
Dixon, J ;
Speake, BK .
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 1995, 112 (04) :711-716
[4]  
HATEFI Y, 1962, J BIOL CHEM, V237, P1676
[5]   Oxygen radical absorbance capacity of peptides from egg white protein ovotransferrin and their interaction with phytochemicals [J].
Huang, Wu-Yang ;
Majumder, Kaustav ;
Wu, Jianping .
FOOD CHEMISTRY, 2010, 123 (03) :635-641
[6]   Ovotransferrin possesses SOD-like superoxide anion scavenging activity that is promoted by copper and manganese binding [J].
Ibrahim, Hisham R. ;
Hoq, Md. Imiranul ;
Aoki, Takayoshi .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2007, 41 (05) :631-640
[7]   Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis [J].
Je, Jae-Young ;
Qian, Zhong-Ji ;
Byun, Hee-Guk ;
Kim, Se-Kwon .
PROCESS BIOCHEMISTRY, 2007, 42 (05) :840-846
[8]   Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type [J].
Klompong, Vilailak ;
Benjakul, Soottawat ;
Kantachote, Duangporn ;
Shahidi, Fereldoon .
FOOD CHEMISTRY, 2007, 102 (04) :1317-1327
[9]   Fourier transform infrared spectroscopic analysis of protein secondary structures [J].
Kong, Jilie ;
Yu, Shaoning .
ACTA BIOCHIMICA ET BIOPHYSICA SINICA, 2007, 39 (08) :549-559
[10]   Characterization of a novel antioxidative peptide from the sand eel Hypoptychus dybowskii [J].
Lee, Woo-Shin ;
Jeon, Joong-Kyun ;
Byun, Hee-Guk .
PROCESS BIOCHEMISTRY, 2011, 46 (05) :1207-1211