Revista: | Brazilian archives of biology and technology |
Base de datos: | PERIÓDICA |
Número de sistema: | 000373466 |
ISSN: | 1516-8913 |
Autors: | Gómez Sampedro, Leidy Johanna1 Zapata Montoya, José Edgar1 |
Institucions: | 1Universidad de Antioquia, Facultad de Química Farmacéutica, Medellín, Antioquia. Colombia |
Any: | 2014 |
Període: | May-Jun |
Volum: | 57 |
Número: | 3 |
Paginació: | 386-393 |
País: | Brasil |
Idioma: | Inglés |
Tipo de documento: | Artículo |
Enfoque: | Analítico, descriptivo |
Resumen en inglés | The angiotensin I-converting enzyme (ACE) inhibiting activity of bovine plasma hydrolyzates obtained by Alcalase 2.4 L at different degrees of hydrolysis (DH) was evaluated. For the evaluation of ACE inhibition (ACEI), Hippuryl-His-Leu was used as substrate and the amount of hippuric acid liberated by non-inhibiting ACE was determined by spectrophotometry at 228 nm. The results showed that the enzymatic hydrolysis increased the ACEI activity as compared with the un-hydrolyzed plasma. The highest activity was onbtained with a DH of 6.7%. The peptide fractions with the maximum activity were isolated using ultrafiltration membranes, ion exchange chromatography and high performance liquid chromatography on reverse phase (RP-HPLC). The fraction with highest ACEI activity, showed an IC50 of 0.18 mg/mL and contained peptides with sequences AGATGVTISGAG, YSRRHPEYAVS, Q(K)AW and L(l)I(I)VR, which were determined by MALDI-TOF-TOF. It was also found that after submitting such fraction to digestive conditions in vitro, the ACEI activity remained constant |
Disciplines | Biología, Química |
Paraules clau: | Bioquímica, Química farmacéutica, Péptidos bioactivos, Hidrólisis enzimática, Enzima convertidora de angiotensina, Inhibición enzimática, Plasma bovino |
Keyword: | Biology, Chemistry, Biochemistry, Medicinal chemistry, Bioactive peptides, Enzymatic hydrolysis, Angiotensin converting enzyme, Enzymatic inhibition, Bovine plasma |
Text complet: | Texto completo (Ver HTML) |