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

  • Articles in SCI Journals
  • Nov, 2016

Paiva, L., Lima, E., Neto, A.I. & Baptista, J. (2016) Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate.

Journal of Functional Foods, 26, 65-76. DOI:10.1016/j.jff.2016.07.006 (IF2016 3,144; Q1 Food Science & Thechnology)
Summary:

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 50: 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 IC50 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.


http://www.sciencedirect.com/science/article/pii/S1756464616301840