期刊
PROCESS BIOCHEMISTRY
卷 44, 期 4, 页码 490-493出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2008.12.017
关键词
Soybean extract; Fermentation; ACE-inhibitory peptide; Bioactive peptide; Antihypertensive
资金
- Korean government (ITEP) [10013796]
- Korea Institute of Industrial Technology(KITECH) [10013796] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Angiotensin I-converting enzyme (ACE), a dipeptidyl carboxypeptidase, plays an important physiological role in regulating blood pressure. ACE-inhibitory peptides derived from food proteins have potential pharmaceutical and human health uses. In this Study, we prepared a fermented soybean extract (FSE) through a rapid fermentation at an elevated temperature to accelerate proteolytic hydrolysis and described purification procedures to discover potent ACE-inhibitory peptides from FSE. After 3 days of aging, FSE exhibited ACE-inhibitory activity with an IC50 value of 1.46 mg/mL. Purification of novel ACE-inhibitory peptides was carried Out using ultra filtration and consecutive chromatographic methods. A novel ACE-inhibitory peptide, with 66-fold increase in ACE-inhibitory activity compared to that of FSE, was isolated from FSE through a five-step purification procedure. The amino acid sequence of the purified ACE-inhibitory peptides was determined to be Leu-Val-Gln-Gly-Ser by Edman degradation method, and its IC50 value was 22 mu g/mL (43.7 mu M). (C) 2009 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据