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

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 αs2-CN-fragments, six to β-CN fragments, and 10 of them were peptides derived from the αs1-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 IC50 value of 592 μm.

Bibliographic Details

Main Authors:	Gómez-Ruiz, José Ángel, Ramos, Mercedes, Recio, Isidra
Other Authors:	Ministerio de Ciencia y Tecnología (España)
Format:	artículo biblioteca
Published:	Elsevier 2002
Subjects:	Bioactive peptides, Manchego cheese, ACE-inhibitory activity, Cheese starters, Functional foods,
Online Access:	http://hdl.handle.net/10261/256553 http://dx.doi.org/10.13039/100012818 http://dx.doi.org/10.13039/501100006280
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