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Identification of ACE-inhibitory peptides in different Spanish cheeses by tandem mass spectrometry

Abstract

Different Spanish cheeses (Cabrales, Idiazábal, Roncal, Manchego, Mahón and a goat's milk cheese), made with diverse technologies and milk from different species, were studied for their angiotensin converting enzyme (ACE)-inhibitory activity. Among the water-soluble extract WSE<1000-Da of the different samples, Cabrales cheese was the most active with an inhibitory activity of 76.1%. On the contrary, Mahón cheese showed the lowest ACE-inhibitory index (56.6%). In order to identify the peptides involved in this activity, the WSE<1000-Da were analyzed by HPLC-MS/MS and off-line MS/MS. A total of 41 major peptides were identified in the different cheeses. Most of them derived from β-and αs1-casein. Several of these peptides were selected on the basis of the presence of proline as the C-terminal amino acid, and they were chemically synthesized. All peptides showed moderate or low ACE-inhibitory activity. Peptide DKIHP [β-CN f(47–51)], a sequence detected in all samples except Mahón cheese, showed the highest inhibitory activity with an IC50 value of 113.1 μM.

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Acknowledgements

This work has received financial support from project AGL-2004-06903-C02-01. J.A. Gómez-Ruiz was the recipient of a fellowship from the Comunidad Autónoma de Madrid, Spain. G. Taborda expresses his appreciation to Colciencias for a fellowship and to the Universidad de Caldas (Manizales, Colombia).

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Correspondence to Mercedes Ramos.

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Gómez-Ruiz, J.Á., Taborda, G., Amigo, L. et al. Identification of ACE-inhibitory peptides in different Spanish cheeses by tandem mass spectrometry. Eur Food Res Technol 223, 595–601 (2006). https://doi.org/10.1007/s00217-005-0238-0

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  • DOI: https://doi.org/10.1007/s00217-005-0238-0

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