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Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the anti hypertensive effect of hydrolysate in spontaneously hypertensive rats
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
2008-11-15
DOI10.1016/j.foodchem.2008.03.059
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
关键词[WOS]ANGIOTENSIN-CONVERTING ENZYME ; ANTIHYPERTENSIVE PEPTIDES ; ENDOGENOUS INHIBITOR ; BOVINE BRAIN ; VV-HEMORPHIN-7 ; HEMOGLOBIN ; HEMORPHINS ; SAUCE ; ASSAY ; MILK
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.
语种英语
WOS记录号WOS:000257979700005
引用统计
被引频次:116[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/141038
专题中国科学院大连化学物理研究所
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
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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.
APA Wang, Jiapei.,Hu, Jianen.,Cui, Jinzhe.,Bai, Xuefang.,Du, Yuguang.,...&Lin, Bingcheng.(2008).Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the anti hypertensive effect of hydrolysate in spontaneously hypertensive rats.FOOD CHEMISTRY,111(2),302-308.
MLA Wang, Jiapei,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".FOOD CHEMISTRY 111.2(2008):302-308.
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