Food allergy is a major public health concern that affects up to 8% of children and up to 2% of the adult population.  To protect the allergic consumer with accurate food allergen labeling, reliable analytical methods are required for allergen detection and quantification.  These methods must be effective in spite of food processing-induced changes in the biophysical and immunological properties of multiple allergen proteins in a sample food matrix.  In this work, a comprehensive liquid chromatography (LC)-mass spectrometry (MS) methodology is applied for simultaneous multi-allergen detection in thermally-processed food samples incurred with milk, egg, and peanut. Combining enhanced protein solubilization methodologies with high resolution MS enables a peptide-specific view of changes in allergen protein containing foods produced with variable compositions and processing conditions.  Compiled data from a global proteomics approach are utilized to identify differentially-abundant peptides resulting from thermally-induced protein modifications.  Furthermore, a comparative LC-MS/MS approach provides a platform by which to screen multiple allergens in varying food matrices for thermally-resistant or stable allergen peptide biomarkers.  Identified peptide targets are then paired with isotopically-labeled analogs in the development of a multiplexed quantitative MRM (multiple reaction monitoring) LC-MS/MS assay for simultaneous detection of milk, egg, and peanut allergens in baked goods.  Quantitative MS results are compared to those obtained with commercially-available ELISA kits.  A combined analytical approach incorporating global proteomic screening with quantitative MS analyses promotes an advanced understanding of fundamental changes in allergen proteins induced by food processing chemistry, thereby improving the performance of detection methods for allergens in complex food systems.

Multi-allergen detection in thermally-processed baked goods by mass spectrometry

248th National Meeting (2014)

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