The oil processing industry generates significant quantities of lemon basil seed residue which is not currently used to any great extent. However, this by-product has important potential as a source...

Defatted rice bran (DRB) is a by-product of oil extraction from rice bran (Oryza sativa L.), and has health benefits. This in vitro study investigated the antioxidant and anti-inflammatory effects of four crude DRB protein hydrolysate fractions prepared by pepsin-pancreatin digestion and fractionated by ultrafiltration on a transformed macrophage cell line, RAW264.7. Protein hydrolysates with MW <3 kDa (F4 fraction) had the lowest IC 50 for NO -, DPPH_ and ABTS radical scavenging activities (0.38 6 0.01, 1.24 6 0.03 and 0.17 6 0.01 mg/mL, respectively). The pooled fraction formed after Reverse phase-High-performance liquid chromatography (HPLC) (F 4-5 ) had the highest percentage inhibition of radical scavenging for DPPH_, and NO -(25.04 6 0.88, and 6.50 6 0.39%, respectively). LC-MS of F 4-5 revealed peptides exhibiting antioxidant activity were composed of His (H), Trp (W) and Tyr (Y) that known to enhance the scavenging activities of peptides. The F4 fraction suppressed lipopolysaccharide and rmIFN-g mediated increase in iNOS, IL-6 and TNF-a mRNA levels in RAW264.7 cells, suggesting the interference was mediated at the transcriptional level. PRACTICAL APPLICATIONDefatted rice bran (DRB) is a good source of nutritional proteins. In this study, DRB protein was hydrolyzed using proteases and further fractionated by ultrafiltration. The results demonstrated that DRB hydrolysates and their fractions exhibited antioxidant and anti-inflammatory activities indicating these as a potential source of functional food and medicines.

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BACKGROUND Salmon bones, a waste by‐product from the salmon industry, were used as a protein hydrolysate source for the production of bioactive peptides. The aim of this work was to evaluate the potential antioxidant and anti‐inflammatory properties of salmon bone protein hydrolysate (SBPH). RESULTS Salmon bones were hydrolyzed by separately using one of four proteases (Alcalase, Favourzyme, Neutrase and papain) at various concentrations (10, 25 and 50 mg mL−1), where the SBPH derived from 10 mg mL−1 papain hydrolysis exhibited the highest nitric oxide (NO) radical scavenging activity. After ultrafiltration, the MW < 0.65 kDa fraction showed the strongest NO inhibitory activity and was further fractionated by gel filtration chromatography (G1 and G2 fractions) and reverse‐phase high‐performance liquid chromatographic fractionation of the G1 fraction, from which the three main peaks (H1, H2 and H3) were found to have a marked NO‐inhibitory activity and their peptide sequences were determined. Moreover, the G1 fraction was shown to inhibit both the lipopolysaccharide (LPS)‐induced NO production and the LPS‐induced inducible NO synthase , interleukin‐6, tumor necrosis factor‐α and induced NO production and the LPSCOX‐2 mRNA levels in RAW 264.7 cells. CONCLUSIONS Salmon bones from the salmon fisheries and farming industry were utilized by enzymatic hydrolysis for the production of valuable peptides. The results of this study suggested that bioactive peptides derived from salmon bones would be alternative anti‐inflammation materials in functional resources. © 2019 Society of Chemical Industry

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