Iron-chelating activity of chickpea protein hydrolysate peptides

Cristina Torres-Fuentes1, Manuel Alaiz, Javier Vioque

  • 1Instituto de la Grasa (CSIC), Avda. Padre García Tejero 4, 41012-Sevilla, Spain.

Food Chemistry
|July 10, 2014
PubMed

Insights

Iron-chelating peptides were purified from chickpea protein hydrolysates. Higher histidine content in these peptides correlated with increased iron-chelating activity, suggesting enhanced iron bioavailability.

Area of Science:

  • Food Science
  • Biochemistry
  • Nutritional Science

Background:

  • Iron deficiency is a global health concern.
  • Dietary iron bioavailability is often limited.
  • Chickpea proteins are a potential source of bioactive peptides.

Purpose of the Study:

  • To purify and characterize iron-chelating peptides from chickpea protein hydrolysates.
  • To investigate the relationship between peptide composition and iron-chelating activity.
  • To assess the potential of these peptides in improving iron absorption.

Main Methods:

  • Chickpea protein hydrolysis using pepsin and pancreatin.
  • Purification of peptides via affinity and gel filtration chromatography.
  • Analysis of iron-chelating activity and histidine content.

Main Results:

  • Purified peptide fractions exhibited higher iron-chelating activity than the original hydrolysate.
  • A positive correlation was found between histidine content and iron-chelating activity.
  • Fractions with histidine content exceeding 20% demonstrated the highest chelating efficacy.

Conclusions:

  • Iron-chelating peptides are effectively generated from chickpea protein hydrolysis.
  • These peptides hold potential for enhancing iron solubility, bioavailability, and absorption.
  • Histidine-rich peptides are key contributors to the observed iron-chelating properties.