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HPLC-MS/MS of Species Specific Fibrinogen Peptide as a Qualitative Method for Fibrin Based Meat Binder


In an attempt to make the maximum use of lower value meat or pieces of meat, the food industry has developed special binders, which can consolidate pieces of meat into whole portions. These binders not only increases yield but allow portion control for meat and fish cuts in catering. They also could permit misrepresentation of cheaper cuts and pieces as expensive cuts of meat and fish. <P>
While traditional meat binders have utilised salted-out soluble proteins from the meat to bind pieces of meat together, a more effective and rapid binding agent has been produced from either bovine or porcine blood. The binding agent is composed of blood plasma (fibrinogen) and the enzyme thrombin. These are two essential components of blood clotting, which work together to create fibrin, and bind the meat together. The process is done at room temperature or below and the resultant mix can be shaped in a mould to give the desired shape of cut. As these binders are both colourless and odourless they can be used in a variety of meat and fish products. <P>

The binder has been approved for use, but would require accurate labelling. A reliable method for use by enforcement officers is required for the detection of these agents and to speciate the source of blood proteins.

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Research Approach:<BR> Various peptides are released during the blood clotting process. Detection and identification of the peptides will indicate whether fibrin has been formed, and the amino acid sequence of the peptide will allow species identification. This project aimed at developing a HPLC-MS/MS method to separate and characterise bovine and porcine blood fibrinopeptides A and B. This approach will improve the selectivity and identification of the targeted peptides over the existing method (reverse phase-HPLC), which is not definitive, especially if the peptides are recovered from a complex food sample. <P>

Results and findings:<BR>A HPLC-MS/MS method was developed which detected the presence of both porcine and bovine fibrinopeptides from blood-based meat binding agents at the 5% (v/w) spiking level. The method was found to be effective for the detection of binders in beef, pork, lamb and fish matrices apart from cod. This method was not as sensitive for the detection of binders in both white fish (cod) and chicken matrix. This is believed to be due to the hydrolysis of the peptides by peptidases in the muscle tissues. Bovine fibrinopeptide A was also detected in meat samples post cooking, which indicates that the peptide is not lost in the drip liquor during cooking. Also a large range of commercial food ingredients were found not to interfere with the identification of meat based binding agents. Further research needs to be undertaken to determine the effects on results of different muscle tissues and storage of samples prior to analysis.

<p>Find more about this project and other FSA food safety-related projects at the <a href="; target="_blank">Food Standards Agency Research webpage</a>.

Central Science Laboratory
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