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Food allergies are a common health problem worldwide, triggering an abnormal immune response. Fish belongs to the top nine of most allergenic foods, among milk, eggs, shellfish, tree nuts, peanuts, wheat, soybeans and the most recently added sesame. The continuing increase of aquaculture production and the relatively easy access to fish worldwide, contribute to increased fish consumption which result in higher prevalence of allergies. The main allergen in fish, responsible for up to 70-95% of the allergic reactions, is a small and stable calcium-binding muscle protein named parvalbumin. This thesis was focused on parvalbumin in two economically important fish species for Southern Europe aquaculture, namely gilthead seabream (Sparus aurata) and European seabass (Dicentrarchus labrax). Chapter 2 characterized this allergen, determining its structure by circular dichroism, sequencing its amino acids by mass spectrometry and analyzing its stability after fish digestion or processing. Results showed that parvalbumin represents a higher content of α-helices and some β-sheets in its secondary structure, at room temperature. Parvalbumins detection reduced throughout gastrointestinal digestion, and also several processing techniques, like salting, steaming and autoclaving showed a significant reduction (p |
