Plant Food-Derived Angiotensin I Converting Enzyme Inhibitory Peptides

被引：138

作者：

Guang, Cuie ^{[1
]}

Phillips, Robert D. ^{[1
]}

机构：

[1] Univ Georgia, Dept Food Sci & Technol, Griffin, GA 30223 USA

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2009年 / 57卷 / 12期

关键词：

Hypertension; angiotensin I converting enzyme; plant proteins; bioactive peptides; BIOACTIVE PEPTIDES; CRYSTAL-STRUCTURE; N-DOMAIN; PROTEIN; PURIFICATION; HYDROLYSATE; IDENTIFICATION; SUBSTRATE; DIGESTION; OPTIMIZATION;

D O I：

10.1021/jf900494d

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Hypertension is one of the most common worldwide diseases that afflict humans. Angiotensin I converting enzyme (ACE) catalyzes the formation of vasoconstrictor, angiotensin II, and the inactivation of vasodilator, bradykinin. The influences of ACE on blood pressure make it an ideal target clinically and nutritionally in the treatment of hypertension. A number of animal food-derived peptides have been reviewed about their in vitro and in vivo ACE inhibitory activities. The aim of this review is to discuss the plant food-derived angiotensin I converting enzyme (ACE) inhibitory peptides from sources, production, purification, and structure to in vitro and in vivo activities.

引用

页码：5113 / 5120

页数：8

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