Effect of ionic strength of different salts on the binding of volatile compounds to porcine soluble protein extracts in model systems

Abstract

Abstract The effect of different salts on the binding ability of porcine soluble protein extracts was studied using solid-phase microextraction (SPME) and GC/MS analysis. Previously, the effect of the different salts (NaCl, KCl, MgCl2 and CaCl2) on the volatile compound headspace concentration in water solution was determined. KCl produced a similar salting out effect as NaCl increasing the volatile compound headspace concentration up to 5–10 times. However, MgCl2 and CaCl2 did not produce a salting out effect on the volatile compounds studied. Finally, NaCl and KCl produced a significant reduction on the binding ability of sarcoplasmic protein extracts to branched aldehydes, hexanal and methional while no effect was produced on octanal and 2-pentanone. On the other hand, the effect of MgCl2 and CaCl2 was much lower even at high ionic strength, except for the branched aldehydes where the presence of MgCl2 at 1.0 ionic strength produced the complete liberation of the volatile compound bound. Consequently, the partial NaCl substitution in meat products by other salts must be considered not only due to their salting out effect but also due to their effect on protein binding ability.