Chickpea, Protein concentrate; Antioxidant activity, Peptide; Mass spectrometry
Abstract :
[en] 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 subfractions
show antioxidant activity (P3 and P8). The P8 displayed the highest DPPH radicalscavenging
activity (67%; at 200 g/ml) among these peptides subfractions. The molecular
masses and amino acids sequences of the purified peptides were determined using ESIMS
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.
Disciplines :
Food science
Author, co-author :
Ghribi, Abir Mokni
Sila, Assaâd
Przybylski, Rémi
Nedjar-Arroume, Naima
Makhlouf, Ines
Blecker, Christophe ; Université de Liège - ULiège > Chimie et bio-industries > Science des alim. et formul.
Attia, Hamadi
Dhulster, Pascal
Bougatef, Ali
Besbes, Souhail
Language :
English
Title :
Purification and identification of novel antioxidant peptides from enzymatic hydrolysate of chickpea (Cicer arietinum L.) protein concentrate
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