Purification and identification of novel antioxidant peptides from enzymatic hydrolysate of chickpea (Cicer arietinum L.) protein concentrate

• Main Authors: Abir Mokni Ghribi, Assaâd Sila, Rémi Przybylski, Naima Nedjar-Arroume, Ines Makhlouf, Christophe Blecker, Hamadi Attia, Pascal Dhulster, Ali Bougatef, Souhail Besbes
• Format: Article
• Language: English
• Published: Elsevier 2015-01-01
• Series: Journal of Functional Foods
• Subjects: Chickpea; Protein concentrate; Antioxidant activity; Peptide; Mass spectrometry
• Online Access: http://www.sciencedirect.com/science/article/pii/S1756464614003909
• ISSN: 1756-4646

Enzymatic hydrolysis of chickpea protein concentrate (CP) by Alcalase® and some physiochemical and antioxidant properties of the resulting hydrolysate (CPH) were characterised. CPH displayed higher antioxidant activity than CP. This hydrolysate was fractionated by size exclusion chromatography on a Sephadex G-25 into four major fractions (Fra.I, Fra.II, Fra.III, and Fra.IV). Fraction III, which exhibited the highest DPPH scavenging activity (54% at 1 mg/ml), was then fractionated by reversed-phase high performance liquid chromatography (RP-HPLC). Eleven antioxidant fractions were isolated and two peptide sub-fractions show antioxidant activity (P3 and P8). The P8 displayed the highest DPPH radical-scavenging activity (67%; at 200 µg/ml) among these peptides subfractions. The molecular masses and amino acids sequences of the purified peptides were determined using ESI-MS and ESIMS/MS, respectively. Their structures were identified as Asp-His-Gly and Val-Gly-Asp-Ile. These peptides did not show haemolytic activity towards bovine erythrocytes. The results suggest that CPH are good source of natural antioxidants.