Interaction of soluble peptides and proteins from skeletal muscle with volatile compounds in model systems as affected by curing agents

The effect of curing agents (salt, glucose, nitrate, nitrite, and ascorbic acid) on the binding of skeletal peptides (camosine and anserine) and a sarcoplasmic protein (myoglobin) with key flavor compounds (hexanal, octanal, 2-pentanone, 2-methylbutanal, and 3-methylbutanal) has been studied by solidphase microextraction (SPME). Curing agents had an effect on the interaction process between camosine and volatile compounds, which was higher than the interactions observed with anserine and myoglobin. Sodium chloride decreased the interaction of volatiles with camosine except for octanal, which was increased, and 2-pentanone, which was unaltered. Ascorbic acid exerted the highest effect by decreasing the interaction of camosine with all of the volatile compounds except for octanal and 2-pentanone. The interaction with anserine was affected by sodium chloride, nitrate, and nitrite, producing a decrease in the interaction with hexanal, octanal, and methional. Finally, sodium chloride, glucose, and nitrite increased the interaction of myoglobin with hexanal, octanal, and methional. The effect of simulated stages of the curing process on the binding was also studied. A combined effect of the curing agents resulted in a change in the relative proportions of volatile compounds that can lead to different flavor perceptions of dry-cured meat products.