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Absorption of iron from recombinant human lactoferrin in young US women^1,2,3

¹ From the Department of Nutrition, University of California, Davis, CA

Background: Lactoferrin is a major protein component of human milk, and it binds iron with high affinity. Because the human small intestine has receptors for lactoferrin, a role for it in iron absorption has been suggested.

Objective: The objective was to study the absorption of iron from extrinsically labeled purified recombinant human lactoferrin produced in rice and to compare it with the absorption of iron from ferrous sulfate.

Design: On 2 occasions 4 wk apart, healthy young women (n = 20) were fed a standardized meal supplemented in randomized order with ⁵⁹Fe as lactoferrin or as ferrous sulfate. Ten subjects received lactoferrin that had been heat-treated, and 10 subjects received untreated lactoferrin. Iron absorption was measured in a whole-body counter after 14 and 28 d and also was measured by red blood cell incorporation after 28 d.

Results: The difference in whole-body iron absorption between heat-treated (24.6 ± 20.8%; n = 10) and untreated (16.2 ± 4.4%; n = 10) lactoferrin was not significant. The difference in whole-body iron absorption between the groups given lactoferrin (20.4 ± 15.3%; n = 20) or ferrous sulfate (18.8 ± 13.2%; n = 20) also was not significant. Serum ferritin and iron absorption were inversely correlated in subjects when they received either lactoferrin or ferrous sulfate, which suggested that iron is absorbed from the 2 sources by a similar mechanism.

Conclusions: Iron is equally well absorbed from lactoferrin (whether heat-treated or untreated) and ferrous sulfate. Thus, iron provided by dietary lactoferrin is likely to be well utilized in human adults.

Key Words: Lactoferrin • human lactoferrin • recombinant human lactoferrin • iron • iron absorption • human milk proteins

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