Angiotensin-Converting Enzyme Inhibition In Vitro by Protein Hydrolysates and Peptide Fractions from Mojarra of Nile Tilapia (Oreochromis niloticus) Skeleton.
J Med Food
; 22(3): 286-293, 2019 Mar.
Article
em En
| MEDLINE
| ID: mdl-30835154
ABSTRACT
Mojarra of Nile tilapia (Oreochromis niloticus) skeleton was used as protein source for the preparation of protein hydrolysates and peptide fractions with angiotensin-converting enzyme (ACE) inhibitory activity. The flour presented a content of 34.92% protein and a brightness (luminosity, L*) of 82.29. Protein hydrolysates were obtained from the protein-rich flour with the enzymes Flavourzyme® and Alcalase® reaching degree of hydrolysis (%DH) of 52% and 67% at 100 min of reaction, respectively. Both hydrolysates showed low-molecular-weight (MW) peptides estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The hydrolysates obtained with Flavourzyme at 60 min and at 80 min with Alcalase showed greater ACE inhibitory activity with IC50 values of 0.238 and 0.344 mg/mL, respectively. The peptide fraction A (MW >10 kDa) with Flavourzyme and fraction B (MW = 10-5 kDa) with Alcalase obtained by ultrafiltration of hydrolysates with higher DH presented IC50 of 0.728 and 0.354 mg/mL, respectively, whereas peptide fraction C (MW = 5-3 kDa) with both enzymes hydrolysates with greater ACE inhibitory activity showed IC50 values of 0.470 and 0.634 mg/mL. The components obtained in this study could be used as functional ingredients in the design and development of functional foods.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Inibidores da Enzima Conversora de Angiotensina
/
Ciclídeos
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Proteínas de Peixes
/
Anti-Hipertensivos
Limite:
Animals
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article