Journal
JOURNAL OF FUNCTIONAL FOODS
Volume 26, Issue -, Pages 65-76Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jff.2016.07.006
Keywords
Macroalgae; Enzymatic hydrolysis; ACE-inhibitory peptides; Inhibition kinetic; Simulated gastrointestinal digestion; Hypertension
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Funding
- CIRN (Centro de Investigacao de Recursos Naturais, University of the Azores)
- cE3c funding [UID/BIN00329/2013]
- FRC (Fundo Regional da Gienca) [M3.1.2/F/014/2011]
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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 (<1 kDa, 1-3 kDa and >3 kDa). The <1 kDa fraction that exhibited the highest activity (IC50: 0.095 mg/mL) was purified using size-exclusion chromatography and reversed-phase high-performance liquid chromatography, yielding two active ACE inhibitory purified peptides. Edman degradation revealed its amino acid sequences to be IP and AFL with ICso values of 0.020 and 0.023 mg/mL, respectively. Both peptides were synthesized to confirm the structure and to validate their ACE-inhibitory activities. Lineweaver-Burk plots suggest that IP acts as a non-competitive and AFL as a competitive ACE-inhibitors. Stability assays showed that both peptides are heat-stable and AFL is hydrolysed by intestinal mucosa peptidases to FL with IC50 value of 0.004 mg/mL that acts as a non-competitive ACE-inhibitor. The results suggest that these peptides might have a potential use in the preparation of antihypertensive drugs or functional foods. (C) 2016 Elsevier Ltd. All rights reserved.
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