BACKGROUND
Salmon bones, a waste byâproduct 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 antiâinflammatory 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 50âmgâmLâ1), where the SBPH derived from 10âmgâmLâ1 papain hydrolysis exhibited the highest nitric oxide (NO) radical scavenging activity. After ultrafiltration, the MWâ<â0.65âkDa fraction showed the strongest NO inhibitory activity and was further fractionated by gel filtration chromatography (G1 and G2 fractions) and reverseâphase highâperformance liquid chromatographic fractionation of the G1 fraction, from which the three main peaks (H1, H2 and H3) were found to have a marked NOâinhibitory activity and their peptide sequences were determined. Moreover, the G1 fraction was shown to inhibit both the lipopolysaccharide (LPS)âinduced NO production and the LPSâinduced inducible NO synthase , interleukinâ6, tumor necrosis factorâα and induced NO production and the LPSCOXâ2 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 antiâinflammation materials in functional resources. © 2019 Society of Chemical Industry