GEN-MKT-18-7897-A
Dec 7, 2017 | Blogs, Food / Beverage | 0 comments
Browse the shelves of any grocery store, and you may get a false sense of security when it comes to ingredient lists. As much as consumers want to trust labels, the truth is, food products could contain mislabelled ingredients, such that they trigger an allergic reaction with serious detrimental effects including discomfort, pain sickness and in some instances, death. Manufacturers, however, do not want to risk their reputation and consumer safety over a false label. As such, there must be some sort of verification to support such an action.
Access the Screening Food for Allergen Toolkit >
How Can Food Manufacturers be Certain a Product is Free from an Allergen?There are several techniques which food testing laboratories use to screen for food allergens. PCR and ELISA are popular techniques. However, these workflows do not compare to the power of an LC-MS/MS assay. Therefore, the following application note, “Solution for Food Allergen Screening” a vMethod from SCIEX, takes allergen screening to a whole new level of detection. Unlike ELISA and PCR, this mass spectrometry-based workflow can screen 12 food allergens in one analysis and delivers high accuracy and selectivity while significantly reducing the amount of false negatives results which could trigger a product recall or worse.
The Take-Away: Reduced False-Positives When Screening Food for AllergensThis vMethod incorporates the standard operating procedure (SOP) for the extraction and analysis of specific allergens in baked and raw food products. The proprietary sample preparation protocol has been verified and tested by multiple independent laboratories. Chromatographic separation is achieved using a Phenomenex Kinetex C18 column (2.6 μm, 100 x 3 mm) column coupled with a QTRAP® 4500 Mass Spectrometer.
What you will find is that this workflow reduces false positive and false negative results through enhanced selectivity through peptide mass detection, reducing false results due to cross-reactivity or matrix effects. The performance of the method delivers a screening LOD 10 ppm in commodity.
Although food products usually label all potential allergens on the ingredients portion of the wrapper, in some cases the allergen hasn’t been declared or realized. For this reason, manufacturers take precautionary steps if they feel that there may be a risk of contamination or miss-labeling of their product1.
To discover more about this high throughput workflow, download the allergens toolkit >
Resources:1.https://www.cbsnews.com/news/clif-bar-recalls-protein-bars-after-nut-allergy-reports/2.http://www.syracuse.com/product-recalls/2017/09/wegmans_recalls_muffins_over_allergy_concerns.htmlDownload Now >
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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