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Published on: February 10, 2018
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.
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.
Abstract:
Chickpea-chelating peptides were purified and analysed for their iron-chelating activity. These peptides were purified after affinity and gel filtration chromatography from a chickpea protein hydrolysate produced with pepsin and pancreatin. Iron-chelating activity was higher in purified peptide fractions than in the original hydrolysate. Histidine contents were positively correlated with the iron-chelating activity. Hence fractions with histidine contents above 20% showed the highest chelating activity. These results show that iron-chelating peptides are generated after chickpea protein hydrolysis with pepsin plus pancreatin. These peptides, through metal chelation, may increase iron solubility and bioavailability and improve iron absorption.
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