Data/hora: 01/06/2024 09:55:09

Provedor de dados: | 52
País: | Brazil
Título: | Effects of hydrolysis and digestion in vitro on the activity of bovine plasma hydrolysates as inhibitors of the angiotensin I converting enzyme
Autores: | Gómez Sampedro,Leidy Johanna; Zapata Montoya,José Edgar.
Data: | 2014-06-01
Ano: | 2014
Palavras-chave: | Enzymatic hydrolysis; Bioactive peptides; Angiotensin I-converting enzyme inhibitors; Peptide sequence.
Resumo: | 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.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000300012
Editor: | Instituto de Tecnologia do Paraná - Tecpar
Relação: | 10.1590/S1516-89132014005000004
Formato: | text/html
Fonte: | Brazilian Archives of Biology and Technology  v.57 n.3 2014
Fonte: | info:eu-repo/semantics/openAccess