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-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 beta-casein, as well as Arg-Pro-Lys and Arg-Pro-Lys-His-Pro-Ile-Lys-His-* from alpha(s1)-casein exhibited ACE-inhibitory activity. Peptides released upon cleavage of the peptide bond Leu190-Tyr191 (either in ovine or caprine beta-casein), and corresponding to the beta-casein sequence Tyr-Gln-Glu-Pro-*, possessed antioxidant activity.
Silva
S V
SV
Escola Superior de Biotecnologia, Universidade Católica Portuguesa, Rua Dr. António Bernardino de Almeida, P-4200-072 Porto, Portugal.
Pihlanto
A
A
Malcata
F X
FX
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000032:analysis* / Q000378:metabolism; D000818:Animals; D000975:Antioxidants / Q000032:analysis* / Q000378:metabolism; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism; D002611:Cheese / Q000032:analysis*; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D031942:Cynara / Q000201:enzymology*; D006041:Goats; D020128:Inhibitory Concentration 50; D008892:Milk / Q000378:metabolism; D010455:Peptides / Q000737:chemistry*; D010940:Plant Proteins / Q000378:metabolism; D012756:Sheep
D000806:Angiotensin-Converting Enzyme Inhibitors; D000975:Antioxidants; D010455:Peptides; D010940:Plant Proteins; D016282:Aspartic Acid Endopeptidases; C097455:aspartic proteinases, Cynara cardunculus