Characterization of peptides with antioxidant activity and antidiabetic potential obtained from chickpea (Cicer arietinum L.) protein hydrolyzates

Abstract

Alcalase hydrolyzates were prepared from the albumin (AH) and globulin (GH) fractions of eight chickpea (Cicer arietinum L.) genotypes from Mexico and 10 from other countries. Protein content, antioxidant activity (AA) (ABTS, DPPH), and degree of hydrolysis were evaluated and the best genotype was selected by principal component analysis. The hydrolyzates of the chosen genotype were analyzed for its antidiabetic potential measured as inhibition of α‐amylase, α‐glucosidase, and dipeptidyl peptidase‐4 (DPP4). Peptide profiles were obtained by liquid chromatography‐mass spectrometry (UPLC‐DAD‐MS), and the most active peptides were analyzed by molecular docking. The average antioxidant activity of albumin hydrolyzates was higher than that of globulin hydrolyzates. ICC3761 was the selected genotype and peptides purified from the albumin hydrolyzate showed the best antioxidant activity and antidiabetic potential (FEI, FEL, FIE, FKN, FGKG, and MEE). FEI, FEL, and FIE were in the same chromatographic peak and this mixture showed the best ABTS scavenging (78.25%) and DPP4 inhibition (IC50 = 4.20 µg/ml). MEE showed the best DPPH scavenging (47%). FGKG showed the best inhibition of α‐amylase (54%) and α‐glucosidase (56%) and may be a competitive inhibitor based on in silico‐predicted interactions with catalytic amino acids in the active site of both enzymes. These peptides could be used as nutraceutical supplements against diseases related to oxidative stress and diabetes. Practical Application This study showed that chickpea protein hydrolyzates are good sources of peptides with antidiabetic potential, showing high antioxidant activity and inhibition of enzymes related to carbohydrate metabolism and type 2 diabetes. These hydrolyzates could be formulated in functional foods for diabetes.

In Silico Approaches to Identify Polyphenol Compounds as α-Glucosidase and α-Amylase Inhibitors against Type-II Diabetes

“…Pharmacophore modeling that can be classified as ligand and structure-based approaches has become a major tool in drug discovery [ 256 ] and has been extensively used in virtual screening [ 257 ]. The objective of pharmacophore modeling is to find chemical features responsible for a specific biological activity among potent ligands [ 258 ]. Therefore, the use of appropriate modeling for screening drugs for T2DM is important in evaluating the interaction between the receptor and ligand, defined as essential geometric arrangement of atoms or functional groups necessary to produce a given biological response [ 259 ].…”

Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides

“…Thus, protein from Vigna unguiculata was partially hydrolyzed by this microbial enzyme, reaching a DH value of 53.0% after 90 min of incubation [ 35 ]. Similarly, globulins and albumins from eight chickpea ( Cicer arietinum L.) genotypes were found to be susceptible to Alcalase, and hydrolyzates obtained after 90 min showed DH values between 33.8 and 42.6% [ 36 ]. The susceptibility of albumin to enzymatic hydrolysis was confirmed using a SDS-PAGE analysis.…”

Molecular cloning and characterization of an alpha-amylase inhibitor (TkAAI) gene from Trichosanthes kirilowii Maxim.

“…Generally, alpha-amylase inhibitors naturally-derived from the plants had few negative effects on humans, so the prospect of alpha-amylase inhibitors peptides could be developed as a treatment for diabetes mellitus type II by alleviating abnormal absorption of carbohydrates. [33] To our knowledge, TkAAI was the rst alpha-amylase inhibitor gene extracted from T. kirilowii. Inhibitory activity of TkAAI against PPA was preliminarily measured.…”