Purification of angiotensin converting enzyme inhibitory peptides from sunflower protein hydrolysates by reverse-phase chromatography following affinity purification

被引：36

作者：

Megias, Cristina ^{[1
]}

Pedroche, Justo ^{[1
]}

del Mar Yust, Maria ^{[1
]}

Alaiz, Manuel ^{[1
]}

Giron-Calle, Julio ^{[1
]}

Millan, Francisco ^{[1
]}

Vioque, Javier ^{[1
]}

机构：

[1] CSIC, Inst Grasa, Seville 41012, Spain

来源：

LWT-FOOD SCIENCE AND TECHNOLOGY | 2009年 / 42卷 / 01期

关键词：

Sunflower protein hydrolysate; Affinity purification; Angiotensin converting enzyme; Inhibitory peptides; COPPER-CHELATING PEPTIDES; BIOACTIVE PEPTIDES; (ACE)-INHIBITORY ACTIVITY; ACE; IMMOBILIZATION; ISOLATE; AGAROSE; ACID;

D O I：

10.1016/j.lwt.2008.05.003

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The purification of a peptidic fraction with angiotensin converting enzyme (ACE) inhibitory activity from sunflower protein hydrolysates by affinity chromatography was recently described. We now describe that reverse-phase HPLC fractionation of this product yields several fractions with IC50 one order of magnitude higher than those previously purified by reverse-phase HPLC following gel filtration chromatography, showing that affinity chromatography is much more effective than gel filtration chromatography as a first step for purification of ACE inhibitory peptides. The amino acid composition of these fractions is presented, but attempts to determine their amino acid sequence failed, showing that these fractions contained more than one peptide. (C) 2008 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved.

引用

页码：228 / 232

页数：5

共 24 条

[1] DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID [J].