Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate.
J Agric Food Chem
; 49(6): 2992-7, 2001 Jun.
Article
en En
| MEDLINE
| ID: mdl-11409999
Bovine skin gelatin was hydrolyzed with sequential protease treatments in the order of Alcalase, Pronase E, and collagenase using a three-step ultrafiltration membrane reactor. The molecular weight distributions of the first, second, and third hydrolysates were 4.8-6.6, 3.4-6.6, and 0.9-1.9 kDa, respectively. The angiotensin I converting enzyme (ACE) inhibitory activity of the third hydrolysate (IC(50) = 0.689 mg/mL) was higher than that of the first and second hydrolysates. Two different peptides showing strong ACE inhibitory activity were isolated from the hydrolysate using consecutive chromatographic methods including gel filtration chromatography, ion-exchange chromatography, and reversed-phase high-performance liquid chromatography. The isolated peptides were composed of Gly-Pro-Leu and Gly-Pro-Val and showed IC(50) values of 2.55 and 4.67 microM, respectively.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Hidrolisados de Proteína
/
Piel
/
Inhibidores de la Enzima Convertidora de Angiotensina
Límite:
Animals
Idioma:
En
Revista:
J Agric Food Chem
Año:
2001
Tipo del documento:
Article
Pais de publicación:
Estados Unidos