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 .
International Dairy Journal – Elsevier
Published: Jan 1, 2002
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