RESUMO
New plant proteins with high nutritional quality and biological properties are actively searched worldwide. Moringa oleifera seed protein isolate was prepared from defatted flour and hydrolyzed using four proteases namely trypsin, pepsin, Alcalase, and thermolysin. Then, antioxidant activity and cellular glucose uptake properties of the hydrolysates were assessed. A high degree of hydrolysis was obtained for hydrolysate prepared using trypsin (60.07%), followed by pepsin (57.14%), Alcalase (50.68%), and thermolysin (45.45%). Thermolysin hydrolysate was the most antioxidant efficient (IC50 0.15 and 0.74 mg/mL for 2,2'-azino-bis(acide 3-ethylbenzothiazoline-6-sulfonique) diammonium salt (ABTS) and 2,2-Diphenyl-1-picrylhydrazyl (DPPH) scavenging activity, respectively). Trypsin hydrolysate stimulated high glucose uptake by yeast cells (12.34-35.28%). In the absence of insulin, Alcalase hydrolysate was the most efficient for glucose uptake by the muscle, with the rate ranging from 22.03% to 29.93% after 30 min, then from 29.55% to 34.6% after 60 min. The four hydrolysates improved glucose uptake by the muscle in the presence of insulin with the rate ranging from 46.88% to 58.03% after 30 min, and from 50% to 58.18% after 60 min. Therefore, Moringa oleifera seed proteins could be used to prepare peptides as components of functional foods for the management of type-2 diabetes.
