Determining the effect of malondialdehyde on the IgE‐binding capacity of shrimp tropomyosin upon in vitro digestion

BACKGROUND Stability in simulated gastric fluids is considered an important parameter for the estimation of food allergenicity. Moreover, proteins in food are highly susceptible to lipid oxidation during processing and preservation. In this study, the change in the IgE‐binding capacity of malondiald...

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Bibliographic Details
Published in:Journal of the science of food and agriculture 2017-10, Vol.97 (13), p.4588-4594
Main Authors: Lv, Liangtao, Lin, Hong, Li, Zhenxing, Ahmed, Ishfaq, Chen, Guanzhi
Format: Article
Language:English
Subjects:
Allergenicity
Allergens - chemistry
Allergens - immunology
Animals
Binding
Blotting, Western
Degradation
digestibility
Digestion
Electrophoresis, Polyacrylamide Gel
Food allergies
Gel electrophoresis
Immunoblotting
Immunoglobulin E
Immunoglobulin E - chemistry
Immunoglobulin E - immunology
Immunoglobulin G
In vitro methods and tests
Lipid peroxidation
Malondialdehyde
Malondialdehyde - chemistry
Oxidation
Oxidation resistance
Penaeidae - chemistry
Penaeidae - immunology
Pepsin
Preservation
Proteins
Seafood
Shellfish - adverse effects
Shellfish - analysis
shrimp
simulated gastric fluid
simulated intestinal fluid
Sodium lauryl sulfate
Tropomyosin
Tropomyosin - chemistry
Tropomyosin - immunology
Trypsin
western blot
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Summary:BACKGROUND Stability in simulated gastric fluids is considered an important parameter for the estimation of food allergenicity. Moreover, proteins in food are highly susceptible to lipid oxidation during processing and preservation. In this study, the change in the IgE‐binding capacity of malondialdehyde (MDA)‐treated shrimp tropomyosin (TM) following in vitro digestion was investigated by SDS‐PAGE and western blot. RESULTS Shrimp TM treated with different concentrations of MDA was slightly degraded and became increasingly resistant to pepsin digestion over time. While untreated TM was rapidly degraded, MDA‐treated TM showed some resistance and was degraded by trypsin only after increasing the digestion time. Results of immunoblotting studies on IgE using sera from patients allergic to shrimp indicated that the IgE‐binding capacity of TM and MDA (50 mmol L−1)‐treated TM decreased slightly after pepsin digestion and significantly decreased after trypsin digestion. CONCLUSION The study indicated that the resistance of TM to degradation increased after oxidation. The treatment with proteases, especially trypsin, is quite effective in decreasing the IgG/IgE‐binding capacity of shrimp TM. © 2017 Society of Chemical Industry
ISSN:0022-5142
1097-0010
DOI:10.1002/jsfa.8328