Germinated chickpea protein ficin hydrolysate and its peptides inhibited glucose uptake and affected the bitter receptor signaling pathway in vitro

Food Funct. 2023 Sep 19;14(18):8467-8486. doi: 10.1039/d3fo01408h.

Abstract

The objective of this study was to evaluate germinated chickpea protein hydrolysate (GCPH) in vitro for its effect on markers of type 2 diabetes (T2D) and bitter taste receptor expression in intestinal epithelial cells. Protein hydrolysate was obtained using ficin, and the resulting peptides were sequenced using LC-ESI-MS/MS. Caco-2 cells were used to determine glucose uptake and extra-oral bitter receptor activation. Three peptides, VVFW, GEAGR, and FDLPAL, were identified in legumin. FDLPAL was the most potent peptide in molecular docking studies with a DPP-IV energy of affinity of -9.8 kcal mol-1. GCPH significantly inhibited DPP-IV production by Caco-2 cells (IC50 = 2.1 mM). Glucose uptake was inhibited in a dose-dependent manner (IC25 = 2.0 mM). A negative correlation was found between glucose uptake and PLCβ2 expression in Caco-2 cells (R value, -0.62). Thus, GCPH has the potential to be commercialized as a functional ingredient.

MeSH terms

  • Caco-2 Cells
  • Cicer*
  • Diabetes Mellitus, Type 2*
  • Ficain
  • Glucose
  • Humans
  • Molecular Docking Simulation
  • Peptides / pharmacology
  • Protein Hydrolysates / pharmacology
  • Signal Transduction
  • Tandem Mass Spectrometry
  • Taste

Substances

  • Ficain
  • Protein Hydrolysates
  • Peptides
  • Glucose