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Orientador(es)
Resumo(s)
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.
Descrição
Palavras-chave
Plant protease Ovine cheese Caprine Angiotensin-converting enzyme inhibition
Contexto Educativo
Citação
"Journal of Dairy Science" . ISSN 0022-0302. 89 (2006) 3336–3344