| Summary: | © 2017 Elsevier Ltd The development of functional food ingredients using legume seed proteins has potential for nutraceutical use. We purified recombinant ß-conglutin proteins (rß1 to rß4, and rß6) from narrow-leafed lupin using affinity–chromatography, and evaluated their anti-inflammatory activity using ex vivo and in vitro systems. rß1, rß3, and rß6 produced lower levels of pro-inflammatory mediators such as nitric oxide (about –34.0–fold in all cases), iNOS m RNA (-7.15, -7.97, -7.41–fold), interleukin 1ß (-12.05, -11.64, -12.16–fold), chemokine CCL5 (-16.0, -18.0, -19.0–fold), and cytokines including TNF-a INF-? IL-1ß IL-2, IL-6, IL-8, and IL-12 (ß1: -28, -100, -8, -2, -49, -45, -127–fold; ß3: -22, -400, -9, -3, -33, -10, -2.54–fold; ß6: -72, -122, -11, -3, -2000, -13, -338–fold). These results suggest that the ß1, ß3, and ß6 conglutins have potential as functional food components in nutraceuticals and that can provide alternative therapies for the prevention and treatment of inflammatory-related diseases.
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