Effects of enzyme type and process time on hydrolysis degree, electrophoresis bands and antioxidant properties of hydrolyzed proteins derived from defatted . press cake.

The present study aimed at investigating the effect of enzymatic hydrolysis times (40-240 min) with alcalase and pancreatin in enzyme-substrate ratio (2% w/w) on the hydrolysis degree, electrophoresis bands, antioxidant properties and chelating activities of iron and copper ions of bioactive peptides derived from defatted (black cumin) press cake. The hydrolysis degree was enhanced by increasing the process time using both enzymes. Both hydrolysis of the enzymes were led to producing peptides with low molecular weight (less of 10 kDa). The DPPH radical scavenging activity was more influenced by peptides hydrolyzed by alcalase. But, the products hydrolyzed by pancreatin had a higher inhibitory effect on the ABTS cationic radical than alcalase hydrolysis. The primary protein reducing power was reached the highest level after enzymatic hydrolysis by alcalase and pancreatin, respectively, for 200 and 240 min. Following the use of proteins hydrolyzed by alcalase and pancreatin, the production of thiobarbituric acid reactive substances was also diminished from 0.45 to 0.42 and 0.38 (mg MDA/L emulsion), respectively. After assessing the iron ion chelating, a higher level of activity was observed in the alkaline-derived enzyme hydrolysis samples. Furthermore, the highest amount of copper ion chelating was obtained after hydrolyzing the enzymes for 200 min.