Identification and Comparison of Peptides from Chickpea Protein Hydrolysates Using Either Bromelain or Gastrointestinal Enzymes and Their Relationship with Markers of Type 2 Diabetes and Bitterness

Abstract

The chickpea (Cicer arietinum L.) is one of the most important pulses worldwide. The objective was to identify, compare and evaluate peptides from chickpea hydrolysates produced by two enzymatic treatments. The antidiabetic potential and bitterness of the peptides and induction of bitter receptors were identified in silico. Proteins were isolated from the Kabuli variety. Peptides were produced from the proteins using a simulated digestive system (pepsin/pancreatin, 1:50 Enzyme/Protein, E/P), and these peptides were compared with those produced via bromelain hydrolysis (1:50 E/P). The protein profiles, sequences and characteristics of the peptides were evaluated. The biochemical inhibition and molecular docking of dipeptidyl peptidase-IV (DPP-IV), α-amylase and α-glucosidase were also studied. The molecular docking identified peptides from enzymatic hydrolysis as inhibitors of DPP-IV. The high hydrophobicity of the peptides indicated the potential for bitterness. There was no correlation between peptide length and DPP-IV binding. Peptides sequenced from the pepsin/pancreatin hydrolysates, PHPATSGGGL and YVDGSGTPLT, had greater affinity for the DPP-IV catalytic site than the peptides from the bromelain hydrolysates. These results are in agreement with their biochemical inhibition, when considering the inhibition of sitagliptin (54.3 µg/mL) as a standard. The bitter receptors hTAS2R38, hTAS2R5, hTAS2R7 and hTAS2R14 were stimulated by most sequences, which could be beneficial in the treatment of type 2 diabetes. Chickpea hydrolysates could be utilized as functional ingredients to be included in the diet for the prevention of diabetes.

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

“…The α‐amylase inhibition value corresponded to those reported by Chandrasekaran et al. (2020) in pepsin‐pancreatin and bromelain chickpea hydrolyzates (11.0%–38.4%); however, those values were obtained using a much higher concentration of hydrolyzates (10 mg/ml).…”

“…The peptides inhibited DPP4 (Table 4) with IC 50 values (4.2–12.08 µg/ml) close to those reported for commercial inhibitors such as Diprotin A (ILE‐PRO‐ILE, IC 50 = 1.1 µg/ml) and Diprotin B (VAL‐PRO‐ILE, IC 50 = 5.5 µg/ml) (Umezawa et al., 1984), and lower than that reported for the commercial drug Sitagliptin (C 16 H 15 F 6 N 5 O, IC 50 = 54.3 µg/ml) (Chandrasekaran et al., 2020). The peak 1 peptides (FEI, FEL, and FIE) were the best inhibitors of DPP4 (IC 50 = 4.20 µg/ml).…”

Drug Carriers Based on Graphene Oxide and Hydrogel: Opportunities and Challenges in Infection Control Tested by Amoxicillin Release

“…The protein linker used in the attachment of the antibiotic molecules was selected to the substrate specificity of BROM. It is the enzyme with low substrate specificity; however, from the amino acid composition of peptides obtained after BROM treatment, some preferences of BROM can be found [48]. Dominate the peptides with glycine at the N' terminal while neutral amino acids (leucine, phenylalanine, alanine) at the C' terminal of peptide chains.…”

Bioactive Peptides as Potential Nutraceuticals for Diabetes Therapy: A Comprehensive Review

“…Peptides produced from chickpea (Cicer arietinum) using a simulated digestive system and bromelain (enzyme derived from pineapple plant) hydrolysis were compared for their antidiabetic activity. Inhibition assays and molecular docking analysis indicated that the peptides PHPATSGGGL and YVDGSGTPLT had greater affinity for the catalytic site of DPP IV compared to peptides isolated from bromelain hydrolysate [103]. Evidently, protein-rich beans are a good source of bioactive peptides, many of which are yet to be fully explored.…”