| Journal: | Brazilian archives of biology and technology |
| Database: | PERIÓDICA |
| System number: | 000373466 |
| ISSN: | 1516-8913 |
| Authors: | Gómez Sampedro, Leidy Johanna1 Zapata Montoya, José Edgar1 |
| Institutions: | 1Universidad de Antioquia, Facultad de Química Farmacéutica, Medellín, Antioquia. Colombia |
| Year: | 2014 |
| Season: | May-Jun |
| Volumen: | 57 |
| Number: | 3 |
| Pages: | 386-393 |
| Country: | Brasil |
| Language: | Inglés |
| Document type: | Artículo |
| Approach: | Analítico, descriptivo |
| English abstract | 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 |
| Keyword: | 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 |
| Full text: | Texto completo (Ver HTML) |
