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Allergenicity assessment of genetically engineered (GE) soybean and processed shellfish using immunological and proteomics methods
Soybean allergy affects approximately 0.1 - 0.2% of general population worldwide. Published studies have reported between 16 to 21 proteins in soybean are allergens or putative allergens. Any new genetically engineered (GE) soybean is subjected to allergenicity evaluation to minimize the risk of food allergies. This study included comparison of IgE binding from individual soybean allergic subjects to proteins in two GE soybean lines, their respective genetically similar controls, and other commercial non-GE lines. The results indicated that the two GE soybeans did not present an increased risk for soybean allergic subjects especially because those with soybean allergy should avoid all soybeans. Based on the variation of endogenous allergens among non-GE commercial lines, it is not clear that similar tests are useful to evaluate food safety for GM crops. Subunits of either β-conglycinin or glycinin were the major IgE binding proteins identified in the study population. A number of proteins reported as allergens or putative allergens and required to be evaluated by agencies were not identified, thus demanding quantification analysis of all putative allergens is irrelevant to food allergy risk. ^ Shellfish are one of the most frequent causes for food hypersensitivity. The allergens and allergenicity of molluscan shellfish have been poorly studied compared to that of crustacean shellfish. The frequency of the cross-reactions between molluscan and crustacean shellfish and the involved allergens are also not well characterized. For the second objective of this research, tropomyosin, troponin T, troponin I, myosin heavy chain, actin, heat shock protein 70, α-actin, and paramyosin were identified as IgE binding proteins expressed in bay scallop. Cross-reactive IgE binding between shrimp and scallop was common but not constant among the study population. Tropomyosin was the major cross-reactive IgE binding protein, but distinct epitopes existed in scallop tropomyosin. Our work demonstrated a decrease in protein solubility, an increase in IgE binding reactivity, and a decrease in clinically relevant eliciting capacity from the extractable shrimp and scallop proteins after boiling and roasting. Considering that shellfish are normally consumed after cooking, the results indicated that future studies to understand allergic reactions to shrimp and scallop should use cooked samples.^
Food science|Plant sciences
Lu, Mei, "Allergenicity assessment of genetically engineered (GE) soybean and processed shellfish using immunological and proteomics methods" (2016). ETD collection for University of Nebraska - Lincoln. AAI10142100.