Food allergy is a major health problem in the Western countries, affecting 3-8% of the population. It has not yet been established what makes a dietary protein a food allergen. Several characteristics have been proposed to be shared by food allergens. One of these is resistance to digestion. This paper reviews data from digestibility studies on purified food allergens and evaluates the predictive value of digestibility tests on the allergenic potential. We point out that food allergens do not necessarily resist digestion. We discuss how the choice of in vitro digestibility assay condition and the method used for detection of residual intact protein as well as fragments hereof may greatly influence the outcome as well as the interpretation of results. The finding that digests from food allergens may retain allergenicity, stresses the importance of using immunological assays for evaluating the allergenic potential of food allergen digestion products. Studies assessing the allergenicity of digestion products, by either IgE-binding, elicitation or sensitizing capacity, shows that digestion may abolish, decrease, have no effect, or even increase the allergenicity of food allergens. Therefore, the predictive value of the pepsin resistance test for assessing the allergenic potential of novel proteins can be questioned.
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http://dx.doi.org/10.1080/10408398.2013.779569 | DOI Listing |
Food Chem
December 2024
Tianjin Key Laboratory of Food Science and Health, School of Medicine, Nankai University, Tianjin 300071, China. Electronic address:
Food allergy is increasingly prevalent and poses notable health risks, which underscores the urgent need to develop reliable and sensitive detection methods for effective identification of food allergens. This study aims to address the limitations of existing methods by developing an immunoassay utilizing bacteriophage/carbon dots (CDs)@silica core-shell nanospheres. Two CDs with different emission wavelengths (513 nm for Green CDs, 645 nm for Red CDs) were synthesized for signal development and amplification.
View Article and Find Full Text PDFPLoS One
December 2024
Department of Pharmacy Practice, Faculty of Pharmacy, Airlangga University, Surabaya, Indonesia.
Food allergies are a global health problem that continues to grow annually, with a prevalence of more than 10%. Shrimp allergy is the most common and life-threatening allergy. There is no cure for food allergies, but shrimp allergen extract (SAE) offers promise as a treatment through allergen-specific immunotherapy (AIT).
View Article and Find Full Text PDFJAMA Netw Open
December 2024
Division of Immunology, Department of Medicine, Boston Children's Hospital, Harvard Medical School, Boston, Massachusetts.
Biosensors (Basel)
December 2024
REQUIMTE/LAQV, Instituto Superior de Engenharia do Porto, Instituto Politécnico do Porto, Rua Dr. António Bernardino de Almeida 431, 4249-015 Porto, Portugal.
β-parvalbumin (β-PV) is the primary fish allergen responsible for most allergic reactions in individuals sensitive to fish. To ensure food safety, a sandwich-based magnetic immunoassay was developed using maleimide-functionalized magnetic beads (NH-MBs). Specific anti-β-PV antibodies were immobilized on these MBs, and a screen-printed carbon electrode was employed as the electrochemical transducer.
View Article and Find Full Text PDFBiosensors (Basel)
December 2024
Department of Food Science and Technology, Tokyo University of Marine Science and Technology, Tokyo 108-8477, Japan.
In recent years, in vitro skin sensitization assays have been recommended as animal-free alternatives for the safety assessment of cosmetics and topical drugs, and these methods have been adopted in OECD test guidelines. However, existing assays remain complex and costly. To address this, we recently developed a more efficient, cost-effective, and accurate method for evaluating skin sensitizers by using immune cell-derived THP-1 cells as a biosensor, coupled with an RT-PCR-based assay.
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