Antioxidant activities of enzymatic rapeseed protein hydrolysates and the membrane ultrafiltration fractions

Abstract

In this study, rapeseed protein isolate was hydrolyzed with various proteases to obtain hydrolysates that were separated by membrane ultrafiltration into four molecular size fractions (<1, 1–3, 3–5, and 5–10kDa). Alcalase hydrolysis significantly (p<0.05) produced the highest yield of protein hydrolysate while Flavourzyme produced the least. The <1kDa fraction was the most abundant after the membrane ultrafiltration of the protein hydrolysates, which indicates that the proteases were efficient at reducing the native rapeseed proteins into low molecular weight peptides. Antioxidant properties of the resulting hydrolysates and membrane fractions were characterized and results showed the Pepsin+Pancreatin (P+P) protein hydrolysate had significantly highest (p<0.05) scavenging activity against DPPH radical among the unfractionated enzymatic hydrolysates. But the P+P hydrolysate was not as effective as other hydrolysates during long-term inhibition of linoleic acid oxidation. For most of the samples, fractionation into the <1kDa peptides significantly (p<0.05) improved DPPH and superoxide scavenging properties when compared to the unfractionated protein hydrolysates. Only the <1kDa fraction showed ferric reducing antioxidant power and the effect was dose-dependent. Overall, Alcalase and Proteinase K seem to be more efficient proteases to release antioxidant peptides from rapeseed proteins when compared to P+P, Flavourzyme and Thermolysin.