中国科学院大连化学物理研究所机构知识库
Advanced  
DICP OpenIR  > 中国科学院大连化学物理研究所  > 期刊论文
题名: Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the anti hypertensive effect of hydrolysate in spontaneously hypertensive rats
作者: Wang, Jiapei1, 2;  Hu, Jianen3;  Cui, Jinzhe4;  Bai, Xuefang1;  Du, Yuguang1;  Miyaguchi, Yuji5;  Lin, Bingcheng1
关键词: oyster protein hydrolysate ;  ACE inhibitory peptides ;  spontaneously hypertensive rat ;  purification and identification ;  hypertension
刊名: FOOD CHEMISTRY
发表日期: 2008-11-15
DOI: 10.1016/j.foodchem.2008.03.059
卷: 111, 期:2, 页:302-308
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Physical Sciences ;  Life Sciences & Biomedicine
类目[WOS]: Chemistry, Applied ;  Food Science & Technology ;  Nutrition & Dietetics
研究领域[WOS]: Chemistry ;  Food Science & Technology ;  Nutrition & Dietetics
英文摘要: Oyster (Crassostrea talienwhanensis Crosse) proteins were produced from fresh oyster and subsequently digested with pepsin. The separations were performed with a Sephadex LH-20 gel filtration chromatography and a RP-HPLC. A purified peptide with sequence Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe (VVYPWTQRF) was firstly isolated and characterized from oyster protein hydrolysate and its ACE inhibitory activity was determined with IC50 value of 66 mu mol/L in vitro. Stability study for ACE inhibitory activity showed that the isolated nonapeptide had the good heat and pH stability and strong enzyme-resistant properties against gastrointestinal proteases. Kinetic experiments demonstrated that inhibitory kinetic mechanism of this peptide was non-competitive and its K-m and K-i values were calculated. The yield of this peptide from oyster proteins was 8.5%. Furthermore, the oyster protein hydrolysate (fraction II), prepared by pepsin treatment firstly exhibited antihypertensive activity when it was orally administered to spontaneously hypertensive rat (SHR) at a dose of 20 mg/kg. These results demonstrated that the hydrolysate from oyster proteins prepared by pepsin treatment could serve as a source of peptides with antihypertensive activity. (C) 2008 Elsevier Ltd. All rights reserved.
关键词[WOS]: ANGIOTENSIN-CONVERTING ENZYME ;  ANTIHYPERTENSIVE PEPTIDES ;  ENDOGENOUS INHIBITOR ;  BOVINE BRAIN ;  VV-HEMORPHIN-7 ;  HEMOGLOBIN ;  HEMORPHINS ;  SAUCE ;  ASSAY ;  MILK
语种: 英语
WOS记录号: WOS:000257979700005
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/141038
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

Files in This Item:

There are no files associated with this item.


作者单位: 1.Chinese Acad Sci, Dalian Inst Chem Phys, Grp 1805, Dalian 116023, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
3.Dalian Fisheries Univ, Dalian 116023, Peoples R China
4.Dalian Inst Light Ind, Sch Art & Design, Dalian 116034, Peoples R China
5.Ibaraki Univ, Coll Agr, Ibaraki 3000393, Japan

Recommended Citation:
Wang, Jiapei,Hu, Jianen,Cui, Jinzhe,et al. Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the anti hypertensive effect of hydrolysate in spontaneously hypertensive rats[J]. FOOD CHEMISTRY,2008,111(2):302-308.
Service
 Recommend this item
 Sava as my favorate item
 Show this item's statistics
 Export Endnote File
Google Scholar
 Similar articles in Google Scholar
 [Wang, Jiapei]'s Articles
 [Hu, Jianen]'s Articles
 [Cui, Jinzhe]'s Articles
CSDL cross search
 Similar articles in CSDL Cross Search
 [Wang, Jiapei]‘s Articles
 [Hu, Jianen]‘s Articles
 [Cui, Jinzhe]‘s Articles
Related Copyright Policies
Null
Social Bookmarking
  Add to CiteULike  Add to Connotea  Add to Del.icio.us  Add to Digg  Add to Reddit 
所有评论 (0)
暂无评论
 
评注功能仅针对注册用户开放,请您登录
您对该条目有什么异议,请填写以下表单,管理员会尽快联系您。
内 容:
Email:  *
单位:
验证码:   刷新
您在IR的使用过程中有什么好的想法或者建议可以反馈给我们。
标 题:
 *
内 容:
Email:  *
验证码:   刷新

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.

 

 

Valid XHTML 1.0!
Powered by CSpace