GEN-MKT-18-7897-A
Jul 21, 2016 | Blogs, Food / Beverage | 0 comments
Food allergy is an immune-mediated, adverse reaction to an antigenic protein. Even limited exposure to an antigen can provoke a significant reaction in sensitive individuals, causing rashes, itching and swelling in the mouth, nausea, vomiting, and asthma. Additionally, food allergies are the leading cause of anaphylaxis, an acute, potentially deadly allergic reaction. The prevalence and severity of food allergies are rising, with approximately 150 million people suffering from food allergies worldwide.1, 2 Presently, there is no cure for food allergies, and sufferers must rely on the correct labeling of foods to avoid consuming allergens. Hence, the development of sensitive and accurate analytical methods to screen for the presence of allergens in food products is necessary for the prevention of potentially life-threatening health problems for allergy sufferers.
Enzyme-linked immunosorbent assays (ELISA) are the most commonly used tests for screening allergens. Although relatively quick and simple to perform, ELISA tests are limited in selectivity and susceptible to cross-reactivity, which can lead to false positive or false negative results. Additionally, most ELISA tests are capable of detecting only one allergen at a time, requiring multiple tests to screen for more than one allergen in a food sample. Therefore, a method that can unambiguously confirm and identify multiple allergens would be invaluable for food screening.
In our exciting solution to routine food allergen screening we have developed an LC-MS/MS method using the QTRAP® 4500 LC-MS/MS system that detects and screens 12 separate allergenic proteins simultaneously in a single injection.
The key benefits of why LC-MS/MS is the instrument of choice for food manufactures and testing facilities are:
Discover more about switching your allergen screening to LC-MS/MS >
In this toolkit you will access an overview brochure and a comprehensive technical note that details the method development steps and method performance in a variety of challenging natural and processed matrices.
References
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As an analytical strategy, middle-down mass spectrometry (MS) workflows characterize biotherapeutic proteins by analyzing large, digested protein fragments or defined subunits, rather than fully intact proteins (top-down) or digested peptides (bottom-up). A middle-down strategy combines the strengths of top-down and bottom-up approaches by delivering high sequence coverage and structural specificity while maintaining relatively simple sample preparation. In practice, middle-down analysis enables accurate mass measurement, rapid sequence confirmation, and localization of key post-translational modifications (PTMs) on protein subunits that are directly relevant to product quality.
In biopharmaceutical development, sequence variants (SV) are considered an inherent risk of producing complex proteins in living systems. Sequence variants are unintended changes to the amino acid sequence of a biotherapeutic and can be caused by errors in transcription or translation in the host cell, or cell culture and process conditions. Detailed analysis of SVs is important in process and product development to ensure the drug’s safety and efficacy. Even low‑level sequence variants can have significant implications for product quality, safety, and efficacy, making their accurate detection and characterization a critical requirement across development, process optimization, and regulatory submission.
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