Structure and function of plant protein-derived antihypertensive peptides

被引:98
作者
Aluko, Rotimi E. [1 ,2 ]
机构
[1] Univ Manitoba, Dept Human Nutr Sci, Winnipeg, MB R3T 2N2, Canada
[2] Univ Manitoba, Richardson Ctr Funct Foods & Nutraceut, Winnipeg, MB R3T 2N2, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
SPONTANEOUSLY HYPERTENSIVE-RATS; ENZYME-INHIBITORY PEPTIDES; IN-VITRO DIGESTION; BIOACTIVE PEPTIDES; BLOOD-PRESSURE; WALNUT PROTEIN; PEA PROTEIN; PURIFICATION; ANTIOXIDANT; IDENTIFICATION;
D O I
10.1016/j.cofs.2015.05.002
中图分类号
TS2 [食品工业];
学科分类号
100403 [营养与食品卫生学];
摘要
The main targets for antihypertensive peptides are renin and angiotensin converting enzyme (ACE). Plant protein-based inhibitory agents are first generated as enzymatic protein hydrolysates, which contain a pool of peptides with different sizes and effectiveness. Protein hydrolysate fractions that consist of mainly low molecular weight peptides (usually <3 kDa) are more effective inhibitors of renin and ACE than the bigger peptides. Purifications of protein hydrolysates have yielded several peptides that inhibit in vitro renin and ACE activities in addition to exerting in vivo blood pressure reductions. The structural basis for enhanced peptide activity varies but generally peptides that contain proline, branched-chain amino acids and aromatic amino acids have strong inhibitory activities against renin and ACE.
引用
收藏
页码:44 / 50
页数:7
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