Bioactive Peptides in Ovine and Caprine Cheeselike Systems Prepared with Proteases from Cynara cardunculus

The potential angiotensin-converting enzyme (ACE)–inhibitory and antioxidant activities of peptides in water-soluble extracts, obtained from raw and sterilized ovine and caprine cheeselike systems coagulated with enzymes from the plant Cynara cardunculus, were assessed. Prior to the assay, the 3,000...

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Bibliographic Details
Published in:Journal of dairy science 2006-09, Vol.89 (9), p.3336-3344
Main Authors: Silva, S.V., Pihlanto, A., Malcata, F.X.
Format: Article
Language:English
Subjects:
alphaS1-casein
angiotensin-converting enzyme inhibition
Angiotensin-Converting Enzyme Inhibitors - analysis
Angiotensin-Converting Enzyme Inhibitors - metabolism
Animal productions
Animals
antihypertensive effect
antioxidant activity
Antioxidants - analysis
Antioxidants - metabolism
Aspartic Acid Endopeptidases - metabolism
beta-casein
bioactive properties
Biological and medical sciences
caprine cheese
Cheese - analysis
Chromatography, High Pressure Liquid - methods
Cynara - enzymology
Cynara cardunculus
enzyme inhibitors
ewe milk
Food industries
Fundamental and applied biological sciences. Psychology
goat cheese
goat milk
Goats
Inhibitory Concentration 50
Milk - metabolism
Milk and cheese industries. Ice creams
milk clotting
oligopeptides
ovine cheese
Peptides - chemistry
plant protease
Plant Proteins - metabolism
rennet substitutes
renneting
Sheep
Terrestrial animal productions
Vertebrates
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Summary:The potential angiotensin-converting enzyme (ACE)–inhibitory and antioxidant activities of peptides in water-soluble extracts, obtained from raw and sterilized ovine and caprine cheeselike systems coagulated with enzymes from the plant Cynara cardunculus, were assessed. Prior to the assay, the 3,000-Da permeate from 45-d-old cheeselike systems was fractionated by tandem chromatographic techniques. Several peaks were obtained in each chromatogram, but only some were associated with ACE-inhibitory or antioxidant activity or both. Peptides Tyr-Gln-Glu-Pro, Val-Pro-Lys-Val-Lys, and Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-* from β-casein, as well as Arg-Pro-Lys and Arg-Pro-Lys-His-Pro-Ile-Lys-His-* from αs1-casein exhibited ACE-inhibitory activity. Peptides released upon cleavage of the peptide bond Leu190-Tyr191 (either in ovine or caprine β-casein), and corresponding to the β-casein sequence Tyr-Gln-Glu-Pro-*, possessed antioxidant activity.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(06)72370-0