Isolation of angiotensin I converting enzyme (ACE) inhibitor from fermented oyster sauce, Crassostrea gigas

被引：107

作者：

Je, JY ^{[1
]}

Park, JY ^{[1
]}

Jung, WK ^{[1
]}

Park, PJ ^{[1
]}

Kim, SK ^{[1
]}

机构：

[1] Pukyong Natl Univ, Dept Chem, Pusan 608737, South Korea

来源：

FOOD CHEMISTRY | 2005年 / 90卷 / 04期

关键词：

fermented oyster; ACE inhibitor; antihypertensive effect; competitive inhibition;

D O I：

10.1016/j.foodchem.2004.05.028

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Angiotensin I converting enzyme (ACE) inhibitor was isolated from fermented oyster sauce (FOS) and purified. Oyster was fermented with 25% NaCl (w/w) at 20 degreesC for 6 months. FOS was passed through a 40-mesh sieve, desalted using an electrodialyzer and then lyophilized. ACE inhibitory activity of FOS was investigated, and the IC50 value was determined to be 2.45 mg/ml. ACE inhibitor from FOS was purified using SP-Sephadex C-25 ion exchange chromatography, Sephadex G-50 gel chromatography, high-performance liquid chromatography (HPLC) on a gel permeation chromatography (GPC) column and reversed-phase HPLC on a C-18 column. The purified inhibitor had an IC50 value of 0.0874 mg/ml, and it exhibited competitive inhibition against ACE. The purified peptide was evaluated for its antihypertensive effect in spontaneously hypertensive rats (SHRs) following oral administration. Rat blood pressure significantly decreased after inhibitor injection. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：809 / 814

页数：6

共 24 条

[1] Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion [J].