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In vitro antihypertensive and antioxidative properties of trypsin‐derived Moringa oleifera seed globulin hydrolyzate and its membrane fractions

Moringa oleifera seed globulin was hydrolyzed with trypsin and fractionated to produce <1, 1–3, and 3–5 kDa peptide sizes. These were evaluated for antioxidant properties: DPPH, hydroxyl radical scavenging assays, FRAP, and metal chelation tests; and in vitro antihypertensive properties: ACE and...

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Detalles Bibliográficos
Autores principales: Aderinola, Taiwo Ayodele, Fagbemi, Tayo Nathaniel, Enujiugha, Victor Ndigwe, Alashi, Adeola Monisola, Aluko, Rotimi Emmanuel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6341156/
https://www.ncbi.nlm.nih.gov/pubmed/30680166
http://dx.doi.org/10.1002/fsn3.826
Descripción
Sumario:Moringa oleifera seed globulin was hydrolyzed with trypsin and fractionated to produce <1, 1–3, and 3–5 kDa peptide sizes. These were evaluated for antioxidant properties: DPPH, hydroxyl radical scavenging assays, FRAP, and metal chelation tests; and in vitro antihypertensive properties: ACE and renin inhibition. Membrane fractionation led to improved antioxidative properties of 29.13% (<1 kDa), 180% (<1 kDa), and 30.58% (1–3 kDa) for DPPH, FRAP, and metal iron chelation, respectively. There was however 48.77% reduction (1–3 kDa) in hydroxyl radical scavenging activity. There was also improvement in ACE inhibitory potentials of the peptides with the 1–3 kDa peptide showing significantly highest ACE inhibition (72.48%)but very low (17.64%, 1–3 kDa) inhibition against the renin. It was concluded that hydrolysis of M oleifera seed globulin with trypsin produced peptides and peptide fractions with potential antioxidant and antihypertensive properties.