Optimization, identification, and comparison of peptides from germinated chickpea (Cicer arietinum) protein hydrolysates using either papain or ficin and their relationship with markers of type 2 diabetes

Food Chem. 2022 Apr 16:374:131717. doi: 10.1016/j.foodchem.2021.131717. Epub 2021 Dec 1.

Abstract

The objective was to optimize and compare the production of antidiabetic peptides from germinated chickpea isolated protein using either papain or ficin. Kabuli chickpeas were germinated for 2, 4 and 6 days. Proteins were isolated, and peptides were produced based on a central composite design selecting human dipeptidyl peptidase (DPP-IV) inhibition as a response. Peptide sequencing was performed to identify and evaluate the physiochemical, biochemical and bitterness properties. DPP-IV inhibition using papain was 84.66 ± 8.72%, with ficin being 72.05 ± 1.20%. The optimum hydrolysate conditions were 6 days germination, 1:10 E/S, and 30 min ficin hydrolysis; SPGAGKG, GLAR, and STSA were identified. Pure SPGAGKG had relatively high affinity for DPP-IV (-7.2 kcal/mol) and α-glucosidase inhibition (-5.9 kcal/mol), with an IC50 of 0.27 mg/mL for DPP-IV inhibition. Peptides in the chickpea hydrolysate inhibited markers of T2D, indicating that the optimal conditions could be used to prepare a functional food ingredient.

Keywords: Bitter receptors; Chickpea sprouts; Diabetes; Ficin; Germination; Optimization; Papain; Peptides.

MeSH terms

  • Cicer*
  • Diabetes Mellitus, Type 2*
  • Dipeptidyl Peptidase 4
  • Dipeptidyl-Peptidase IV Inhibitors*
  • Ficain
  • Humans
  • Papain
  • Peptides
  • Protein Hydrolysates

Substances

  • Dipeptidyl-Peptidase IV Inhibitors
  • Peptides
  • Protein Hydrolysates
  • Dipeptidyl Peptidase 4
  • Papain
  • Ficain