Identification and formation of angiotensin-converting enzyme-inhibitory peptides in Manchego cheese by high-performance liquid chromatography-tandem mass spectrometry

被引：61

作者：

Gómez-Ruiz, JA ^{[1
]}

Ramos, M ^{[1
]}

Recio, I ^{[1
]}

机构：

[1] CSIC, Inst Fermentac Ind, E-28006 Madrid, Spain

来源：

JOURNAL OF CHROMATOGRAPHY A | 2004年 / 1054卷 / 1-2期

关键词：

cheese; food analysis; peptides; enzyme inhibitors;

D O I：

10.1016/j.chroma.2004.05.022

中图分类号：

Q5 [生物化学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

A total of 75 peptides included in the fraction with molecular mass below 3000 from an 8-month-old Manchego cheese could be identified using HPLC coupled on line to an ion trap mass spectrometer. Some previously described peptides with antihypertensive and/or angiotensin-converting enzyme (ACE)-inhibitory activity were detected. The formation of five active sequences was followed during cheese ripening in four different batches of Manchego cheese. Two experimental batches of Manchego cheese elaborated with selected bacterial strains with the aim of improve the organoleptic characteristics demonstrated also a good performance in the formation of peptides with ACE-inhibitory activity during cheese ripening. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：269 / 277

页数：9

共 43 条

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Characterization of multiply phosphorylated peptides selectively precipitated from a pancreatic casein digest [J].