Isolation and identification of angiotensin-converting enzyme inhibitory peptides from egg white protein hydrolysates

被引：125

作者：

Liu, JingBo ^{[1
]}

Yu, ZhiPeng ^{[1
]}

Zhao, WenZhu ^{[1
]}

Lin, SongYi ^{[1
]}

Wang, ErLei ^{[1
]}

Zhang, Yan ^{[1
]}

Hao, Hui ^{[1
]}

Wang, ZuoZhao ^{[1
]}

Chen, Feng ^{[2
]}

机构：

[1] Jilin Univ, Lab Nutr & Funct Food, Changchun 130062, Peoples R China

[2] Clemson Univ, Dept Food Sci & Human Nutr, Clemson, SC 29634 USA

来源：

FOOD CHEMISTRY | 2010年 / 122卷 / 04期

关键词：

ACE-inhibitory activity peptides; Egg white protein; Tandem mass spectrometry; SPONTANEOUSLY HYPERTENSIVE-RATS; MASS-SPECTROMETRY; PURIFICATION; MILK; CHROMATOGRAPHY; EXTRACT;

D O I：

10.1016/j.foodchem.2010.03.108

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The aim of this study was to identify potential angiotensin I-converting enzyme (ACE) inhibitory peptide from egg white protein. The protein was hydrolysed by Alcalase and the hydrolysates were isolated with Gel filtration to get the high activity fraction. The fraction was identified by LC tandem mass spectrometric 4000 Q Trap MS. In the current work, 19 peptides were discovered in the fractions, five of which sourced from ovotransferrin and were synthesised by Fmoc solid phase method. ACE-inhibitory activity was measured by HPLC assay. The 50% inhibitory concentrations of Arg-Val-Pro-Ser-Leu (RVPSL) was 20 mu M. Based on this remarkable ACE-inhibitory activity, it is suggested that RVPSL may have potential applications as a functional food, which could be used as nutraceutical compounds. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：1159 / 1163

页数：5

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