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Purification, identification and characterization of two novel antioxidant peptides from finger millet (Eleusine coracana) protein hydrolysate

Agrawal, Himani, Joshi, Robin, Gupta, Mahesh
Food research international 2019 v.120 pp. 697-707
Eleusine coracana, antioxidant activity, antioxidants, computer simulation, free radicals, functional foods, gel chromatography, hydrolysates, hydrolysis, ingredients, pepsin, protein hydrolysates, serine, synthetic peptides, threonine, trypsin, ultrafiltration
Antioxidant peptides were successfully identified from a finger millet protein hydrolysate. The trypsin hydrolysate showed a higher degree of hydrolysis (17.47 ± 0.63%) than the pepsin hydrolysate, was further fractionated by ultrafiltration membrane [<3 kDa (UF3), 3-10 kDa (UF2) and > 10 kDa (UF1)]. UF3 with higher antioxidant activity (48.41 ± 0.21%) was further fractionated into five fractions (GFA, GFB, GFC, GFD and GFE) using gel filtration. Fraction GFB possessed the highest antioxidant activity (61.79 ± 0.08%) and was purified by reverse-phase ultra-flow liquid chromatography. Two potential antioxidant peptides were identified as TSSSLNMAVRGGLTR and STTVGLGISMRSASVR. Synthetic peptides with the same sequence were synthesized and characterized for their antioxidant activity. Molecular docking studies revealed that potential antioxidant activity from both peptides resulted from the interaction of serine and threonine residues with free radicals. The current study suggested that natural peptides identified from finger millet have potent antioxidant activity and regarded as a promising source for a functional food ingredient.