Antioxidant Activity of Peptide Fractions from Chickpea Globulin Obtained by Pulsed Ultrasound Pretreatment

Abstract

Protein hydrolysates and peptides can show biological activities, and pulsed ultrasound improves bioactivities. Among matrices from which protein hydrolysates can be obtain, chickpea is an excellent source. The objective of this research was to evaluate the effect of pulsed ultrasound on globulin concentrate to obtain chickpea hydrolysate (HGb) and peptide fractions and their bioactivity. Antioxidant activity by ABTS (2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt), FRAP (Ferric Reducing Antioxidant Power) and human erythrocyte assays was determined. The electrophoretic profile, amino acid profile, and antimicrobial activity of hydrolysates were also determined. Two hydrolysates had the highest antioxidant activity: HGb (91.44% ABTS inhibition, 73.04% hemolysis inhibition and 5185.57 µmol TE/g dried sample in FRAP assay) and HGb-20 (48.25% ABTS inhibition, 100% hemolysis inhibition and 2188.53 µmol TE/g dried sample in FRAP assay). Peptide fractions inhibited 100% of the hemolysis on human erythrocytes. The hydrolysates from chickpea proteins obtained with savinase have antioxidant activity through the SET and HAT mechanisms. The application of the obtained compounds for the development of functional foods or for food preservation should be considered.