alexa Allergenicity Assessment of a Genetically Modified Protein-Recombinant Human Lactoferrin | OMICS International | Abstract
ISSN: 2155-6121

Journal of Allergy & Therapy
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Research Article

Allergenicity Assessment of a Genetically Modified Protein-Recombinant Human Lactoferrin

Cui Zhou1, Na Sun1, Jing Wang1, Jing Lu1, Jing Tian2, Richard E Goodman3, Ning Li4, Huilian Che1,5* and Kunlun Huang1,5*

1College of Food Science and Nutritional Engineering, China Agricultural University, China

2Department of Dermatology, the First Affliated Hospital of Herbin Medical University, China

3Department of Food Science & Technology, University of Nebraska, USA

4State Key Laboratory for Agro Biotechnology, China Agricultural University, China

5The Supervision, Inspection and Testing Center of Genetically Modified Organisms, Ministry of Agriculture, China

*Corresponding Author:
Huilian Che
College of Food Science and Nutritional Engineering
China Agricultural University
Beijing 100083, China
Tel: 86-10+62738552
Fax: 86-10+62323465
E-mail: [email protected]
Kunlun Huang
College of Food Science and Nutritional Engineering
China Agricultural University
Beijing 100083, China
Tel: 86-10+62738552
Fax: 86-10+62323465
E-mail: [email protected]

Received date: February 01, 2013; Accepted date: February 28, 2013; Published date: March 05, 2013

Citation: Zhou C, Sun N, Wang J, Lu J, Tian J, et al. (2013) Allergenicity Assessment of a Genetically Modified Protein-Recombinant Human Lactoferrin. J Aller Ther S3:002. doi: 10.4172/2155-6121.S3-002

Copyright: © 2013 Zhou C, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

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.

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