Application of at-line two-dimensional liquid chromatography–mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysatesReportar como inadecuado




Application of at-line two-dimensional liquid chromatography–mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates - Descarga este documento en PDF. Documentación en PDF para descargar gratis. Disponible también para leer online.

Analytical and Bioanalytical Chemistry

, Volume 391, Issue 1, pp 299–307

First Online: 09 April 2008Received: 17 October 2007Revised: 18 February 2008Accepted: 18 February 2008

Abstract

A two-dimensional chromatographic method with mass spectrometric detection has been developed for identification of small, hydrophilic angiotensin I-inhibiting peptides in enzymatically hydrolysed milk proteins. The method involves the further separation of the poorly retained hydrophilic fraction from a standard C18 reversed-phase column on a hydrophilic interaction liquid chromatography HILIC column. The latter column is specifically designed for the separation of hydrophilic compounds. Narrow fractions collected from the HILIC column were analysed for their angiotensin I-converting enzyme ACE inhibiting potential in an at-line assay. Fractions showing significant inhibition of ACE were analysed by LC–MS for structure elucidation. With this method the main peptides responsible for ACE-inhibition in the hydrophilic part of a milk hydrolysate could be determined. The ACE-inhibiting peptides RP, AP, VK, EK, and EW explained more than 85% of ACE-inhibition by the hydrophilic fraction.

KeywordsAngiotensin-converting enzyme Blood pressure-lowering peptides HPLC MS Reversed-phase HILIC  Download fulltext PDF



Autor: Chris J. van Platerink - Hans-Gerd M. Janssen - Johan Haverkamp

Fuente: https://link.springer.com/







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