GEN-MKT-18-7897-A
Apr 13, 2020 | Blogs, Food / Beverage, Life Science Research, Proteomics | 0 comments
About 220 million people worldwide live with a food allergy.1 These numbers, along with the complexity and severity of conditions, continue to rise. In America, there are about 32 million food allergy sufferers—5.6 million of those are children under the age of 18.2.2 That’s 1 out of every 13 children, or about 2 in every classroom. From a financial perspective, the cost of food allergy childcare for US families is up to $25 billion annually.
What is a food allergy?A food allergy is an adverse health effect resulting from a specific immune response that occurs reproducibly from exposure to a given food. Food allergens are proteins that can be tolerated by most people but, in some sensitive individuals, can cause a severe, even life-threatening, reaction known as anaphylaxis.
There is no cure for severe food allergy, so complete avoidance is required. Allergic consumers rely heavily on product labeling to help them do just that. There are more than 170 foods that are reported to cause allergenic reactions. In the US, the 8 major food allergens responsible for most of the severe reactions must be declared: eggs, fish, milk, peanuts, tree nuts, shellfish or crustacean, soy and wheat.2 In the UK this list also includes 6 additional food allergens: celery, lupin, mollusks, mustard, sesame seeds and sulfur dioxide and sulfites.3
Testing is critical to ensure food safetyA study led by Michelle Colgrave and James Broadbent of the Commonwealth Scientific and Industrial Research Organization (CSIRO) found that common methods, such as the antibody-based ELISA, are not always appropriate in complex food matrices. Drawing from their experience with gluten detection using liquid chromatography-mass spectrometry (LC-MS), they developed an alternative, complementary proteomics approach to detect allergenic proteins. This approach could be the first step toward the development of a routine food testing assay.
Colgrave and Broadbent’s study focused on seafood allergy for the following reasons:
From the target groups, 3 types of shrimp and prawns were chosen based on their production worldwide. (Whiteleg shrimp is one of the most commonly caught aquatic species.)
Detecting proteins by their piecesThe analysis followed these steps:
The generic workflow for protein detection and quantification using LC-MSBefore you watch the webinar, here’s a summary of the research approach.
To learn more about their work, watch their webinar by filling out the form on your right, where they describe their ongoing work on the proteome analysis of shellfish. They share data from the initial detection and identification of shellfish proteins by LC-QqTOF, and some early results of targeted allergen analysis using LC-QqQ mass spectrometry. They conclude with their goals for the second phase of the project.
Fill out the form on your right to watch the webinar.
RUO-MKT-18-10425-A
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.
CE‑SDS remains a cornerstone assay for characterizing fragmentation, aggregation, and product‑related impurities in therapeutic proteins. UV detection has been the long‑standing standard. However, it frequently struggles with baseline noise, limited sensitivity for minor fragments, and subjective integration.
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