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The Protein Structure Determines The Sensitizing Capacity Of Brazil Nut 2s Albumin (Ber E1) In A Rat Food Allergy Model, Jolanda Hm Van Bilsen, Léon Mj Knippels, André H. Penninks, Willem F. Nieuwenhuizen, Harmen Hj De Jongh, Stef J. Koppelman
The Protein Structure Determines The Sensitizing Capacity Of Brazil Nut 2s Albumin (Ber E1) In A Rat Food Allergy Model, Jolanda Hm Van Bilsen, Léon Mj Knippels, André H. Penninks, Willem F. Nieuwenhuizen, Harmen Hj De Jongh, Stef J. Koppelman
Department of Food Science and Technology: Faculty Publications
It is not exactly known why certain food proteins are more likely to sensitize. One of the characteristics of most food allergens is that they are stable to the acidic and proteolytic conditions in the digestive tract. This property is thought to be a risk factor in allergic sensitization. The purpose of the present study was to investigate the contribution of the protein structure of 2S albumin (Ber e1), a major allergen from Brazil nut, on the sensitizing capacity in vivo using an oral Brown Norway rat food allergy model. Disulphide bridges of 2S albumin were reduced and …
The Protein Structure Determines The Sensitizing Capacity Of Brazil Nut 2s Albumin (Ber E1) In A Rat Food Allergy Model, Jolanda H. M. Van Bilsen, Leon M.J. Knippels, Andre H. Penninks, Willem F. Nieuwenhuizen, Harmen H.J. De Jongh, Stef J. Koppelman
The Protein Structure Determines The Sensitizing Capacity Of Brazil Nut 2s Albumin (Ber E1) In A Rat Food Allergy Model, Jolanda H. M. Van Bilsen, Leon M.J. Knippels, Andre H. Penninks, Willem F. Nieuwenhuizen, Harmen H.J. De Jongh, Stef J. Koppelman
Department of Food Science and Technology: Faculty Publications
It is not exactly known why certain food proteins are more likely to sensitize. One of the characteristics of most food allergens is that they are stable to the acidic and proteolytic conditions in the digestive tract. This property is thought to be a risk factor in allergic sensitization. The purpose of the present study was to investigate the contribution of the protein structure of 2S albumin (Ber e1), a major allergen from Brazil nut, on the sensitizing capacity in vivo using an oral Brown Norway rat food allergy model. Disulphide bridges of 2S albumin were reduced and …
Allergenicity Assessment Of A Genetically Modified Protein-Recombinant Human Lactoferrin, Cui Zhou, Na Sun, Jing Wang, Jing Lu, Jing Tian, Richard E. Goodman, Ning Li, Huilian Che, Kunlun Huang
Allergenicity Assessment Of A Genetically Modified Protein-Recombinant Human Lactoferrin, Cui Zhou, Na Sun, Jing Wang, Jing Lu, Jing Tian, Richard E. Goodman, Ning Li, Huilian Che, Kunlun Huang
Department of Food Science and Technology: Faculty Publications
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 …