Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate

•ACE-inhibitory peptides were purified from Ulva rigida protein enzymatic hydrolysate.•The purified active peptides were small, having amino acid sequences of IP and AFL.•The IP and AFL peptides were stable against temperature.•AFL is hydrolysed by intestinal mucosa peptidases to a strong ACE-inhibi...

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Bibliographic Details
Published in:Journal of functional foods 2016-10, Vol.26, p.65-76
Main Authors: Paiva, Lisete, Lima, Elisabete, Neto, Ana Isabel, Baptista, José
Format: Article
Language:English
Subjects:
ACE-inhibitory peptides
Enzymatic hydrolysis
Hypertension
Inhibition kinetic
Macroalgae
Simulated gastrointestinal digestion
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Summary:•ACE-inhibitory peptides were purified from Ulva rigida protein enzymatic hydrolysate.•The purified active peptides were small, having amino acid sequences of IP and AFL.•The IP and AFL peptides were stable against temperature.•AFL is hydrolysed by intestinal mucosa peptidases to a strong ACE-inhibitor dipeptide.•The IP and AFL may have potential use to develop anti-hypertension nutraceuticals. Ulva rigida protein was hydrolysed with pepsin plus bromelain after a screening of nine enzymes for optimal proteolysis. This hydrolysate, presenting ACE-inhibitory activity with an IC50 value of 0.483 mg/mL, was fractionated by ultrafiltration membranes into three molecular weight ranges (3 kDa). The
ISSN:1756-4646
2214-9414
DOI:10.1016/j.jff.2016.07.006