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