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.
| Main Authors: | , , |
|---|---|
| Other Authors: | |
| 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 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|