Background: Recombinant human lactoferrin (rhLF) has previously suggested serving as food additive due to the natural iron binding properties that provide anti-microbial activity. Recombinant cows have been produced that express hLf in milk. However, the potential allergenicity of hLf has not been previously assessed. This research is conducted to evaluate the potential allergenicity of rhLF as a prerequisite for food use.
Methods: A comparison was made of the bioactivity, physicochemical properties and glycosylation profile between rhLF and natural hLF. The amino acid sequence of hLf was compared to known allergens. Additionally, the stability of hLf in pepsin and a human serum IgE test was conducted.
Results: The amino acid identity between rhLF and the minor allergen bovine lactoferrin was 71.4%. However, every human is exposed to hLf constantly without demonstrated allergies. The rhLF was digested rapidly by pepsin and was not specifically bound by IgE using serum from patients who are allergic to egg and milk.
Conclusion: Based on these results, the potential allergenicity of rhLF as produced in bovine milk is quite low. It may be added into formula powder or food to improve nutrition composition.