Peanut (Arachis hypogaea L.) as a source of antihypertensive and antimicrobial peptides

To optimize the production and yield of bioactive peptides, defatted raw and roasted peanut flours were subject to varied durations of hydrolysis. Alcalase and sequential hydrolysis with pepsin and pancreatin were the enzyme systems used. Alcalase provided a more extensive hydrolysis (pd0.05). The hydrolysates were shown to be a potent source of hypotensive peptides. HPLC fractions for each peanut treatment and enzyme system were assayed for ACE inhibitory activity. IC for inhibiting ACE activity from the potent hydrophobic end of the chromatograms 50ranged from 8.7g/ml to 235g/ml for the alcalase system and 7.9g/ml to 65.9g/ml for the pepsin-pancreatin system. The digests also exhibited lethality against pathogenic Listeria monocytogenes and Escherichia coli O157:H7 with the radii of inhibition ranging from 4 to 13mm and from 2 to 5mm respectively with digests protein concentration of 0.1 to 2mg.