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Can Glycation Reduce Food Allergenicity?
Qinchun Rao1, Xingyi Jiang1, Yida Li2
1Department of Nutrition, Food and Exercise Sciences , Florida State University , Tallahassee , Florida 32306 , United States.
Journal of Agricultural and Food Chemistry
|April 17, 2018
Summary
Food glycation, a natural process, alters protein properties and immunoreactivity. Its impact on allergen binding doesn't always predict patient allergic reactions.
Area of Science:
- Food science
- Protein chemistry
- Immunology
Background:
- Glycation, also known as the Maillard reaction, is a natural process during food production.
- This reaction can modify the physiochemical properties and functionality of food proteins.
- Understanding glycation is crucial for food processing and safety.
Purpose of the Study:
- To clarify terminology confusion between glycation and glycosylation.
- To review current applications of glycation in food science.
- To analyze the impact of glycation on protein immunoreactivity and allergenicity.
Main Methods:
- Literature review and perspective synthesis.
- Analysis of glycation's effects on protein structure and function.
- Evaluation of glycation's influence on immunoglobulin binding.
Main Results:
- Glycation can decrease, maintain, or increase protein immunoreactivity.
- Changes in immunoglobulin E (IgE) or G (IgG) binding do not reliably predict clinical allergenicity.
- Distinguishing glycation from glycosylation is important for accurate interpretation.
Conclusions:
- Glycation significantly impacts food protein immunoreactivity.
- Allergenicity assessment requires careful consideration beyond in vitro binding assays.
- Further research is needed to fully understand glycation's role in food allergy.
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