Food allergen detection by mass spectrometry: From common to novel protein ingredients

Abstract

Food allergens are molecules, mainly proteins, that trigger immune responses in susceptible individuals upon consumption even when they would otherwise be harmless. Symptoms of a food allergy can range from mild to acute; this last effect is a severe and potentially life‐threatening reaction. The European Union (EU) has identified 14 common food allergens, but new allergens are likely to emerge with constantly changing food habits. Mass spectrometry (MS) is a promising alternative to traditional antibody‐based assays for quantifying multiple allergenic proteins in complex matrices with high sensitivity and selectivity. Here, the main allergenic proteins and the advantages and drawbacks of some MS acquisition protocols, such as multiple reaction monitoring (MRM) and data‐dependent analysis (DDA) for identifying and quantifying common allergenic proteins in processed foodstuffs are summarized. Sections dedicated to novel foods like microalgae and insects as new sources of allergenic proteins are included, emphasizing the significance of establishing stable marker peptides and validated methods using database searches. The discussion involves the in‐silico digestion of allergenic proteins, providing insights into their potential impact on immunogenicity. Finally, case studies focussing on microalgae highlight the value of MS as an effective analytical tool for ensuring regulatory compliance throughout the food control chain.

Utilizing the Banana S-Adenosyl-L-Homocysteine Hydrolase Allergen to Identify Cross-Reactive IgE in Ryegrass-, Latex-, and Kiwifruit-Allergic Individuals

“…Mass spectrometry (MS) is a widely used technique for the characterization of novel allergens. Analyzing the amino acid sequences of proteins after enzymatic digestion followed by MS in novel foods, such as insect and microalgae flours, can help in establishing their similarity to known allergens and forecasting the likelihood of cross-reactivity [ 15 ]. The digestion of food involves numerous human proteolytic enzymes, where certain allergenic epitopes may persist unaffected [ 15 ].…”

“…Analyzing the amino acid sequences of proteins after enzymatic digestion followed by MS in novel foods, such as insect and microalgae flours, can help in establishing their similarity to known allergens and forecasting the likelihood of cross-reactivity [ 15 ]. The digestion of food involves numerous human proteolytic enzymes, where certain allergenic epitopes may persist unaffected [ 15 ]. For instance, αS1-casein, a milk protein allergen, exhibits over three hundred linear epitopes, some of which remain intact even after in silico digestion with key enzymes like trypsin, chymotrypsin, and pepsin [ 15 ].…”

“…The digestion of food involves numerous human proteolytic enzymes, where certain allergenic epitopes may persist unaffected [ 15 ]. For instance, αS1-casein, a milk protein allergen, exhibits over three hundred linear epitopes, some of which remain intact even after in silico digestion with key enzymes like trypsin, chymotrypsin, and pepsin [ 15 ]. Intact epitopes identified after enzymatic processing can be used as marker peptides serving as indicators for the presence of allergenic proteins in novel foods, which would aid in the prediction and management of potential allergic reactions [ 14 , 15 ].…”