Interactions of soluble peptides and proteins from skeletal muscle on the release of volatile compounds

The ability of skeletal dipeptides (carnosine and anserine) and a sarcoplasmic protein (myoglobin) to interact with key flavor compounds (hexanal, octanal, methional, 2-pentanone, 2-methylbutanal, and 3-methylbutanal) has been studied using the solid phase microextraction (SPME) technique. Conditions for SPME analysis (fiber coating, sampling time, and linearity of detection) were optimized. The effect of pH on the binding was also investigated. Thermodynamic models were applied to evaluate the binding parameters n (number of binding sites), K (affinity constant), and DeltaG (Gibb's free energy) to all of the flavor compounds studied, and they showed an absence of cooperative effect. Carnosine was the peptide with the highest affinity for all of the volatile compounds except 2-pentanone. Its interaction with hexanal and methional was significantly affected by pH. Anserine showed a lower level of interactions with hexanal, methional, 2-methylbutanal, and 3-methylbutanal, whereas myoglobin interacted with only hexanal and 2-methylbutanal. Differences in aroma retention can thus result in different sensory perceptions of muscle foods.