Title: Effects of Structural Modifications on Immunogenicity of Food Proteins
Project duration: Oct, 2015- Sep, 2019
Protein misfolding occurs occasionally in human metabolism. Such events can trigger the innate immune system, initiate chronic immune activation and improper immune response. These are etiologically involved in e.g. neuro-inflammatory disorders like Alzheimers disease and Parkinson disease. Prevention of aggregation and processing-related misfolding, e.g. ß-sheet structure induction, is also relevant in pharmaceutical protein preparation and may lead to unwanted immune responses towards such proteins. For instance, glycation of peanut protein is involved in the development of allergy, and aggregation of milk proteins affects their intestinal uptake and shifts this from epithelial uptake to uptake via Peyers Patches.
The significance of food protein structure modifications as a result of processing is relatively underexposed. Heating, shearing and pH change are important parameters for possible structural changes in proteins, leading to misfolding, hydrophobicity changes, aggregation and glycation as a consequence of Maillard reaction. As an major allergen in cows milk, ß-lactoglobulin (BLG) is used as an example protein to study the connection between structure change and immune system stimulation.
Aim: Our research focuses on relating processing-induced structural modifications of food proteins to possible changes in their immunogenicity. Physico-chemical descriptions of such changes will be related to immune responses in in vitro systems and in animal models.