In order to maximize use of lower value carcass meats, the food industry can use binders or food “glues” to bind trimmings into acceptable products for consumers. Traditionally these binders have included bovine or porcine thrombin, a blood-derived clotting agent that will clot around the meat ingredients to hold them together. In 2010, the European Parliament issued directives banning the use of binders derived from cows and pigs. In addition, US food safety legislation requires specific product labeling to inform consumers about the use of and species of origin for these binders. Testing for the presence and species of origin of blood-derived binders in food products is difficult; the binders are usually incorporated at very low concentrations in the final product. There is also the added complication of storage conditions, refrigeration and freezing, that might affect analysis. Grundy and co-workers1 report on the reliability and reproducibility of a liquid chromatography-mass spectrometry (LC-MS/MS) method they developed previously. Their method is based on the unique species-specific fibrinopeptide signatures released into the food product when a binder is used, and detects its presence and species of origin in finished product using selective reaction monitoring process of the triple stage quadrupole MS/MS. The study reviewed here involves monitoring performance of the protocol in five different food-testing laboratories worldwide, each using a different triple quadrupole mass spectrometer to complete the sample testing. Researchers created a standard operating procedure for their method and sent it, along with bovine and porcine fibrinopeptide standards spiked into prepared lamb meat, to participating laboratories. First, collaborating laboratories established standard calibration curves to optimise their individual instruments, including a Thermo Scientific TSQ Quantum Ultra, using commercial bovine and porcine fibronopeptide A and B standards. Once calibrated, each laboratory tested the spiked lamb samples and all correctly reported back the species of origin. Initial results showed that bovine fibrinopeptide was most difficult to detect in the LC-MS/MS chromatograms, so Grundy et al. decided to further test reproducibility among the participating laboratories using this species to spike samples. This next round of inter-laboratory testing used tuna as the matrix. Again, all laboratories correctly identified bovine fibronopeptide and reported the absence of the porcine peptide. With zero false positive and negative reporting rates in this collaborative study, the researchers confidently predict that their LC-MS/MS screening method is fully transferable to other food testing institutes. References
- Grundy, H.H., et al., (2013) “Selected reaction monitoring method to determine the species origin of blood-based binding agents in meats: A collaborative study,” Food Chemistry 141(4) (pp.3531–3536)4):3531-6. Epub ahead of publication doi: 10.1016/j.foodchem.2013.06.063.
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