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Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate
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Advisor(s)
Abstract(s)
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 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.
Description
Keywords
ACE-inhibitory Peptides Enzymatic Hydrolysis Hypertension Inhibition Kinetic Macroalgae Simulated Gastrointestinal Digestion
Citation
Paiva, L., Lima, E., Baptista, J., & Neto, A. I.. (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. https://doi.org/10.1016/j.jff.2016.07.006
Publisher
Elsevier