| dc.creator | Gómez Sampedro, Leidy Johanna | |
| dc.creator | Zapata Montoya, José Edgar | |
| dc.date | 2022-01-12T15:23:38Z | |
| dc.date | 2022-01-12T15:23:38Z | |
| dc.date | 2014 | |
| dc.date.accessioned | 2023-08-28T20:15:54Z | |
| dc.date.available | 2023-08-28T20:15:54Z | |
| dc.identifier | 1516-8913 | |
| dc.identifier | http://hdl.handle.net/10495/25224 | |
| dc.identifier | 10.1590/S1516-89132014005000004 | |
| dc.identifier | 1678-4324 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/8476403 | |
| dc.description | 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), HippurylHis-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. | |
| dc.description | COL0010771 | |
| dc.format | 8 | |
| dc.format | application/pdf | |
| dc.format | application/pdf | |
| dc.language | eng | |
| dc.publisher | Instituto de Tecnologia do Paraná - Tecpar | |
| dc.publisher | Grupo de Nutrición y Tecnología de Alimentos | |
| dc.publisher | Curitiba, Brasil | |
| dc.relation | Braz. Arch. Biol. Technol. | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.rights | http://creativecommons.org/licenses/by-nc-sa/2.5/co/ | |
| dc.rights | http://purl.org/coar/access_right/c_abf2 | |
| dc.rights | https://creativecommons.org/licenses/by-nc/4.0/ | |
| dc.subject | Inhibidores de la Enzima Convertidora de Angiotensina | |
| dc.subject | Angiotensin-Converting Enzyme Inhibitors | |
| dc.subject | Hidrólisis enzimática | |
| dc.subject | Enzymatic hydrolysis | |
| dc.subject | Péptidos | |
| dc.subject | Peptides | |
| dc.title | Effects of Hydrolysis and Digestion in Vitro on the Activity of Bovine Plasma Hydrolysates as Inhibitors of the Angiotensin I Converting Enzyme | |
| dc.type | info:eu-repo/semantics/article | |
| dc.type | info:eu-repo/semantics/publishedVersion | |
| dc.type | http://purl.org/coar/resource_type/c_2df8fbb1 | |
| dc.type | https://purl.org/redcol/resource_type/ART | |
| dc.type | Artículo de investigación | |
