Isolation and Identification of a Novel Antioxidant Peptide from Chickpea (Cicer arietinum L.) Sprout Protein Hydrolysates

Abstract

Chickpea (Cicer arietinum L.) is the second most widely cultivated leguminous plant in the world. In this study, the chickpea sprout protein (CSP) was hydrolyzed by various enzymes (trypsin, neutrase, alcalase and papain). The neutrase fraction (NF) which exhibits the best antioxidant activity with a high degree of hydrolysis (DH) was purified by ion-exchange chromatography (IEC), gel filtration chromatography (GFC), and reverse phase high-performance liquid chromatography (RP-HPLC). A novel antioxidant peptide (NF2-4-1) was identified to be Leu-Thr-Glu-IIe-IIe-Pro with 685.41 Da molecular weight utilized matrix-assisted laser desorption/ionization-time of flight mass spectrometry. The IC50 values of NF2-4-1 was 0.24 ± 0.06 mg/mL on 1, 1-diphenyl-2-picrylhydrazyl (DPPH˙) and 0.57 ± 0.04 mg/mL on hydroxyl radicals (·OH) scavenging activity, respectively. Therefore, the results of this study demonstrate that chickpea sprouts can be used as a source of natural antioxidant peptides for food and nutraceutical applications.