Millets are well-known for protein with high nutritional value and a range of health benefits. Milletderived proteins can thus be a rich source of bioactive peptides with multiple bioactive properties. In this study three proteolytic enzymes, i.e. alcalase, bromelain, and chymotrypsin were used to generate pearl millet protein hydrolysates (PMPHs) and explored for multifunctional bioactive properties. Degree of hydrolysis (DH) ranged between 28.69% and 59.21% with maximum DH observed for PMPs hydrolysed with bromelain for 9 h. The PMPs digested with alcalase exhibited enhanced in-vitro anti-diabetic potential with greater inhibition towards α-amylase and dipeptidyl peptidase-IV (DPP-IV) with IC 50 inhibitory concentration of 5.06 and 3.44 μg mL −1 , respectively. Alcalase PMPHs demonstrated the strongest ABTS radical scavenging activity (976 mM TEAC) while chymotrypsin-generated PMPHs showed significant scavenging of DPPH free radicals (222.3 mM TEAC). In addition, bromelain-treated hydrolysates displayed the highest α-glucosidase inhibitory activity (6.71 μg mL −1 ) and Ferric reducing anti-oxidant power (585.7 mM TEAC). Moreover, PMPHs generated by alcalase showed potential anti-lipidemic activity by inhibiting pancreatic lipase and cholesteryl esterase with maximum IC 50 values of 3.46 and 3.61 μg mL −1 , respectively. These findings suggest that PMPs could be used as a potential source for bioactive hydrolysates with improved anti-diabetic, anti-lipidemic, and anti-oxidant activities.

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