Production of functional peptides with inhibition ability against angiotensin I-Converting enzyme using P. pastoris expression system.
J Food Drug Anal
; 26(3): 1097-1104, 2018 07.
Article
en En
| MEDLINE
| ID: mdl-29976402
ABSTRACT
To obtain the angiotension-I converting enzyme inhibitor (ACEI), a fusion ACEI polypeptide encoded with 8 DNA sequences of GPL, GPM, IKW, IVY, IRPVQ, IWHHT, IYPRY and IAPG, which were selected and designed and cloned into pGAPZαC and then transformed into Pichia pastoris SMD1168H. After 3 days induction, the fraction with highest ACEI activity was expressed and purified using a Ni Sepharose™ 6 Fast Flow. The IC50 of recombinant ACEI polypeptide was 88.2 µM. A 128-fold increase of ACEI activity (0.69 µM) was obtained after pepsin digestion, which was equivalent to 0.022 µM of captopril. Reverse phase HPLC indicated all the 8 peptides contained in ACEI-hydrolysate after pepsin digestion.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Pichia
/
Inhibidores de la Enzima Convertidora de Angiotensina
/
Expresión Génica
Límite:
Humans
Idioma:
En
Revista:
J Food Drug Anal
Año:
2018
Tipo del documento:
Article
País de afiliación:
Taiwán