Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate

被引:184
作者
Zhao, Yuanhui [1 ]
Li, Bafang [1 ]
Liu, Zunying [1 ]
Dong, Shiyuan [1 ]
Zhao, Xue [1 ]
Zeng, Mingyong [1 ]
机构
[1] Ocean Univ China, Coll Food Sci, Qingdao 266003, Peoples R China
关键词
sea cucumber; gelatin; hydrolysate; ACE inhibitory peptide; renal hypertensive rat; antihypertensive effect;
D O I
10.1016/j.procbio.2007.08.011
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Gelatin from the sea cucumber (Acaudina molpadioidea) was hydrolyzed sequentially with bromelain and alcalase. The hydrolysate was fractionated into three ranges of molecular weight (GH-I, <10 kDa; GH-II, <5 kDa; GH-III, <1 kDa) using an ultrafiltration membrane bioreactor system. The GH-III brought about a high angiotensin-l-converting enzyme (ACE) inhibitory activity, with IC50 value of 0.35 mg/ml. An ACE inhibitory peptide was isolated from the GH-III, using the chromatographic methods including ion-exchange chromatography, gel filtration and reversed phase high-performance liquid chromatography. The purified ACE inhibitory peptide with a molecular weight of 840 Da consisted of five main amino acids (Glu, Asp, Pro, Gly and Ala), and its IC50 value was 0.0142 mg/ml. This sea cucumber gelatin hydrolysate (GH-III) was used as drinks administered to renal hypertensive rats (RHR) for 1 month. The systolic blood pressure and diastolic blood pressure of the RHR were significantly reduced, which indicates an antihypertensive effect by oral administration. (c) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1586 / 1591
页数:6
相关论文
共 29 条
[11]   Properties of gelatins from skins of fish -: black tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica) [J].
Jamilah, B ;
Harvinder, KG .
FOOD CHEMISTRY, 2002, 77 (01) :81-84
[12]   Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats [J].
Jung, WK ;
Mendis, E ;
Je, JY ;
Park, PJ ;
Son, BW ;
Kim, HC ;
Choi, YK ;
Kim, SK .
FOOD CHEMISTRY, 2006, 94 (01) :26-32
[13]  
Kim S., 1994, J KOREAN IND ENG CHE, V5, P547
[14]   PURIFICATION AND IDENTIFICATION OF AN ANGIOTENSIN I-CONVERTING ENZYME-INHIBITOR FROM SOY-SAUCE [J].
KINOSHITA, E ;
YAMAKOSHI, J ;
KIKUCHI, M .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 1993, 57 (07) :1107-1110
[15]   ISOLATION OF ANGIOTENSIN-CONVERTING ENZYME-INHIBITOR FROM TUNA MUSCLE [J].
KOHAMA, Y ;
MATSUMOTO, S ;
OKA, H ;
TERAMOTO, T ;
OKABE, M ;
MIMURA, T .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1988, 155 (01) :332-337
[16]   Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase [J].
Kuba, M ;
Tana, C ;
Tawata, S ;
Yasuda, M .
PROCESS BIOCHEMISTRY, 2005, 40 (06) :2191-2196
[17]   Purification and identification of angiotensin I-converting enzyme inhibitory peptide from buckwheat (Fagopyrum esculentum Moench) [J].
Ma, MS ;
Bae, IY ;
Lee, HG ;
Yang, CB .
FOOD CHEMISTRY, 2006, 96 (01) :36-42
[18]   Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790 [J].
Maeno, M ;
Yamamoto, N ;
Takano, T .
JOURNAL OF DAIRY SCIENCE, 1996, 79 (08) :1316-1321
[19]   INHIBITION OF ANGIOTENSIN I-CONVERTING ENZYME BY BACILLUS-LICHENIFORMIS ALKALINE PROTEASE HYDROLYZATES DERIVED FROM SARDINE MUSCLE [J].
MATSUI, T ;
MATSUFUJI, H ;
SEKI, E ;
OSAJIMA, K ;
NAKASHIMA, M ;
OSAJIMA, Y .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 1993, 57 (06) :922-925
[20]   ANGIOTENSIN I-CONVERTING ENZYME INHIBITORY PEPTIDES DERIVED FROM BONITO BOWELS AUTOLYSATE [J].
MATSUMURA, N ;
FUJII, M ;
TAKEDA, Y ;
SUGITA, K ;
SHIMIZU, T .
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 1993, 57 (05) :695-697