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Iron absorption from concentrated hemoglobin hydrolysate by rat.
Nikta Vaghefi1, Fuzia Nedjaoum, Didier Guillochon
1Laboratoire de Physiologie Digestive et Nutritionnelle, CHU, F-14033 Caen, France.
The Journal of Nutritional Biochemistry
|June 7, 2005
Summary
Heme iron absorption is improved by peptides from hemoglobin hydrolysis, especially when cysteine is added. Enzyme type and peptide interactions significantly influence iron uptake efficiency.
Area of Science:
- Biochemistry
- Nutritional Science
- Gastroenterology
Background:
- Heme iron from hemoglobin is highly bioavailable but challenging for dietary fortification due to low iron content and poor solubility of purified heme.
- Understanding heme iron absorption requires investigating interactions between heme, peptides, and other factors like cysteine.
Purpose of the Study:
- To assess the impact of concentrated heme iron, peptides from globin hydrolysis, and cysteine on iron absorption.
- To elucidate the relationship between heme-peptide interactions and iron bioavailability.
Main Methods:
- Hemoglobin hydrolysis using pepsin or subtilisin, followed by heme iron concentration via ultrafiltration.
- Iron absorption assessment using an Ussing chamber model, with gluconate as a control.
- Investigating the effect of cysteine supplementation on iron uptake.
Main Results:
- Iron uptake was lower from non-concentrated pepsin hydrolysate and gluconate compared to other groups.
- Cysteine significantly enhanced iron uptake, except in the concentrated subtilisin hydrolysate group.
- No significant differences in iron uptake were observed between different cysteine-supplemented groups.
Conclusions:
- Hydrophobic peptides and the strength of heme-peptide interactions are key determinants of heme iron absorption.
- These interactions primarily occur before iron uptake, as evidenced by cysteine's effect.
- Enzymatic hydrolysis pathways influence the composition of peptides and subsequent heme iron bioavailability.