Vito Nettisa, Mariachiara Biancoa,b, Cosima Damiana Calvanoa,b, Rosaria Anna Piccaa,b, Margherita Izzia, Tommaso Cataldia,b

aDipartimento di Chimica,
bCentro interdipartimentale SMART, Università degli Studi di Bari Aldo Moro, via Orabona 4, 70126, Bari.

The growing interest in recent years in the ecological transition has led to the development of new materials including new food packaging made as biocompatible through the use of natural substances such as alginate, soy or a mixture of different components [1].  The use of these materials can raise concerns about the potential release of allergenic proteins from packaging derived from food-allergenic ingredients to the food during storage. Allergens are defined as proteins that can trigger, in sensitive people, mild to severe reactions such as anaphylaxis, [2]. The European Union has identified 14 food allergenic ingredients, including milk, soybean, eggs, peanuts, crustaceans, nuts, fish, wheat, molluscs, celery, mustard, sesame, lupin, and sulfur dioxide. Additionally, new classes of food allergens, classified as ‘novel foods,’ are emerging, including allergenic proteins from algae and insects [3]. This study focuses on innovative food packaging based on a zein-casein film. 

The inclusion of 3% (w/v) caseins was found essential to enhance the morphology of the zein-based film. Caseins, known allergenic proteins from milk, could potentially migrate to foods, thus their release must be assessed to protect the health of sensitive individuals. In this work we present preliminary results from aqueous solution extractions of zein-casein films, specifically identifying allergens. In detail, the aqueous extracts were digested by trypsin overnight at 37°C and, the digests were analysed by both matrix-assisted laser desorption/ionization (MALDI)-time of flight (TOF)/TOF mass spectrometry (MS) and reversed-phase liquid chromatography (RPLC) coupled with high/low resolution MS to identify casein allergenic proteins. Our results clearly identified tryptic peptides corresponding to Alpha-S1, Alpha-S2, and Beta caseins such as sequence FFVAPFPEVFGK at m/z 692.8686 marker of Alpha-S1, sequence NAVPITPTLNR at m/z 598.3433 marker of Alpha-S2 or sequence AVPYPQR at m/z 415.7293 marker of Beta casein. Future studies will investigate the kinetics of protein release using various solvents to simulate different food compositions.

Acknowledgements: This work was supported by the project 2023-UNBACLE-0241869 - NOVAFIND, financed by Uniba ERC Seeds project.

Keywords: allergens, food packaging, mass spectrometry

References

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2. Sicherer S. H.  and Sampson H. A., Journal of Allergy and Clinical Immunology, 1 (2018), pag. 41-58. DOI: 10.1016/j.jaci.2017.11.003

3. Pali-Schöll I, Verhoeckx, K, et al., Trends in Food Science & Technology, February (2019), pag. 45-48. DOI: 10.1016/j.tifs.2018.03.007