Purification of novel angiotensin converting enzyme inhibitory peptides from beef myofibrillar proteins and analysis of their effect in spontaneously hypertensive rat model

被引：38

作者：

Lee, Seung Yun ^{[1
]}

Hur, Sun Jin ^{[1
]}

机构：

[1] Chung Ang Univ, Dept Anim Sci & Technol, 4726 Seodong Daero, Anseong 17546, Gyeonggi, South Korea

来源：

BIOMEDICINE & PHARMACOTHERAPY | 2019年 / 116卷

关键词：

ACE inhibitory peptide; Beef; Myofibrillar protein; Antihypertensive effect; Spontaneously hypertensive rats; BLOOD-PRESSURE; ANTIHYPERTENSIVE PEPTIDES; BIOACTIVE PEPTIDES; OXIDATIVE STRESS; THIOL-GROUP; HYDROLYSIS; FRACTIONS; GENETICS; PROGRESS; MEAT;

D O I：

10.1016/j.biopha.2019.109046

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

100103 [病原生物学]; 100218 [急诊医学];

摘要：

This study was conducted to purify the angiotensin converting enzyme (ACE) inhibitory peptides from beef myofibrillar proteins by using inexpensive enzymes alkaline-AK and papain. Different molecular weight peptides (< 3 and < 10 kDa) were obtained using ultrafiltration. The < 3 kDa peptides obtained by alkaline-AK (AK3K) digestion showed the highest ACE inhibitory activity (74.29%) as compared to other alkaline-AK peptides, and a strong antihypertensive effect of AK3K was observed in the spontaneously hypertensive rat (SHR) model. The AK3K treatment groups (400 and 800 mg/kg body weight) exhibited a decrease in systolic blood pressure (SBP) by 28 and 35 mmHg, respectively in the SHR model. The study demonstrated that the ACE inhibitory peptide obtained from beef myofibrillar proteins had the sequence Leu-Ile-Val-Gly-Ile-Ile-Arg-Cys-Val, and could be possibly used for lowering the SBP.

引用

页数：7

共 56 条

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