Functional properties and biological activities of perilla seed meal protein hydrolysates obtained by using different proteolytic enzymes

In this study, we aimed to determine the potential functional properties and biological activities of the hydrolysates of perilla seed meal (PSM), which is a by-product of perilla seed oil extraction. PSM protein was hydrolyzed independently by using five proteases, and their functional and biological properties were analyzed. PSM protein hydrolysate exhibited high solubility at most of the tested pH values, and the trypsin-treated hydrolysate exhibited the highest water and oil absorption capacity. The neutrase-treated hydrolysate was most effective in scavenging the 1,1-diphenyl-2-picrylhydrazine radicals, whereas the pepsin-treated hydrolysate showed the highest angiotensin I-converting enzyme inhibitory effect, and anti-inflammatory activity. Trypsin-treated hydrolysate exhibited the highest scavenging activity against of 2,2 '-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid radicals with the IC(50)of 109.72 mu g/mL. The results of the present study suggest that the type of protease used for the treatment significantly influences the functional properties and biological activities of the resulting PSM protein hydrolysates.