J. Dairy Sci. 89:3336–3344 © American Dairy Science Association, 2006. 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 wa-ter-soluble extracts, obtained from raw and sterilized ovine and caprine cheeselike systems coagulated with enzymes from the plant Cynara cardunculus, were as-sessed. Prior to the assay, the 3,000-Da permeate from 45-d-old cheeselike systems was fractionated by tan-dem 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-ca-sein, 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-ca-sein), and corresponding to the β-casein sequence Tyr-Gln-Glu-Pro-*, possessed antioxidant activity. Key words: plant protease, ovine cheese, caprine cheese, angiotensin-converting enzyme inhibitio