Angiotensin-converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starter cultures

Angiotensin-converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different... The angiotensin-converting enzyme (ACE)-inhibitory activity of water-soluble extracts from Manchego cheeses, which were manufactured with different starter cultures, was monitored during cheese ripening. On activity basis, the 3000 Da permeate from an 8-months-aged cheese, which was prepared with a defined-strain bacterial inoculum, was selected and fractionated by following several chromatographic steps. A total of 22 peptide fragments were identified in nine fractions by electrospray-ionisation-tandem mass spectrometry. Five of them corresponded to α s2 -CN-fragments, six to β -CN fragments, and 10 of them were peptides derived from the α s1 -CN sequence. The di-peptide, FP, could be originated from hydrolysis of various casein fractions. The complexity of the collected fractions after three chromatographic steps precluded the assignment of a single peptide responsible of the ACE-inhibitory activity. Fragment (199–204) from ovine β -CN, which was included in one of the most active fractions, was chemically synthesised and it was found to have an IC 50 value of 592 μ m . http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png International Dairy Journal Elsevier

Angiotensin-converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starter cultures

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Publisher
Elsevier
Copyright
Copyright © 2002 Elsevier Science Ltd
ISSN
0958-6946
eISSN
1879-0143
D.O.I.
10.1016/S0958-6946(02)00059-6
Publisher site
See Article on Publisher Site

Abstract

The angiotensin-converting enzyme (ACE)-inhibitory activity of water-soluble extracts from Manchego cheeses, which were manufactured with different starter cultures, was monitored during cheese ripening. On activity basis, the 3000 Da permeate from an 8-months-aged cheese, which was prepared with a defined-strain bacterial inoculum, was selected and fractionated by following several chromatographic steps. A total of 22 peptide fragments were identified in nine fractions by electrospray-ionisation-tandem mass spectrometry. Five of them corresponded to α s2 -CN-fragments, six to β -CN fragments, and 10 of them were peptides derived from the α s1 -CN sequence. The di-peptide, FP, could be originated from hydrolysis of various casein fractions. The complexity of the collected fractions after three chromatographic steps precluded the assignment of a single peptide responsible of the ACE-inhibitory activity. Fragment (199–204) from ovine β -CN, which was included in one of the most active fractions, was chemically synthesised and it was found to have an IC 50 value of 592 μ m .

Journal

International Dairy JournalElsevier

Published: Jan 1, 2002

References

  • Overview on milk protein-derived peptides
    Meisel, H.
  • The interpretation of collision-induced dissociation tandem mass spectra of peptides
    Papayannopoulos, A.I.
  • A new type of ripened, low-fat cheese with bioactive properties
    Ryhänen, E.-L.; Pihlanto-Leppälä, A.; Pahkala, E.
  • Peptides from several Italian cheeses inhibitory to proteolytic enzymes of lactic acid bacteria, Pseudomonas fluorescens ATCC 948 and to the angiotensin I-converting enzyme
    Smacchi, E.; Gobbeti, M.

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