Conformation affects the potential allergenicity of ovalbumin after heating and glycation

Ovalbumin (OVA), one of the major allergens in hen egg white, and has widespread use in experimental models of allergy. The aim of this research was to assess the effect of glycation and heat treatment on the potential allergenicity of OVA prepared from hen egg white. Secondary and tertiary structur...

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Bibliographic Details
Published in:Food additives & contaminants. Part A, Chemistry, analysis, control, exposure & risk assessment Chemistry, analysis, control, exposure & risk assessment, 2013-10, Vol.30 (10), p.1684-1692
Main Authors: Ma, X.J., Chen, H.B., Gao, J.Y., Hu, C.Q., Li, X.
Format: Article
Language:English
Subjects:
allergenicity
Allergens - adverse effects
Allergens - chemistry
Allergens - immunology
Allergies
Animals
Antibody Specificity
antigenicity
Avian Proteins - adverse effects
Avian Proteins - chemistry
Avian Proteins - immunology
Biological and medical sciences
Chickens
egg allergy
Egg and egg product industries
Egg Hypersensitivity - immunology
Eggs
Food industries
Fundamental and applied biological sciences. Psychology
glycation
Glycosylation
Heating
Hot Temperature
Humans
Immunoglobulin E - blood
ovalbumin
Ovalbumin - adverse effects
Ovalbumin - chemistry
Ovalbumin - immunology
Protein Conformation
protein structure
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Rabbits
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Summary:Ovalbumin (OVA), one of the major allergens in hen egg white, and has widespread use in experimental models of allergy. The aim of this research was to assess the effect of glycation and heat treatment on the potential allergenicity of OVA prepared from hen egg white. Secondary and tertiary structures of OVA were also characterised to show the relationship between potential allergenicity and the conformation of OVA after heating and glycation. Glycation significantly reduced the potential allergenicity of OVA tested with egg allergy patients' sera, which was caused by conformation changes. An increased IgG reactivity was measured using rabbit anti-OVA and was supposed to be caused by protein unfolding which exposed hidden epitopes. Heating reduced the potential allergenicity of OVA at the expense of increased IgG reactivity. It is suggested that conformational changes of OVA induced by glycation and controlled heating significantly reduced its potential allergenicity.
ISSN:1944-0049
1944-0057
DOI:10.1080/19440049.2013.822105