Model studies on the efficacy of protein homogenates from raw pork muscle and dry-cured ham in binding selected flavor compounds.

The binding of sarcoplasmic and myofibrillar proteins extracted from postrigor pork muscle and from 7 and 12 months dry-cured hams with volatile compounds such as 3-methyl-butanal, 2-methyl-butanal, 2-pentanone, hexanal, methional, and octanal was studied using solid phase microextraction and gas chromatography analysis. The binding ability of sarcoplasmic proteins from pork muscle was higher than the ability shown by 7 and 12 months dry-cured ham sarcoplasmic homogenates and also higher than the binding ability of myofibrillar homogenates. The effect of the ionic strength on the binding was also studied. This effect was more important on myofibrillar proteins due to its ability to produce changes on the protein conformation that affect their binding ability. However, the sarcoplasmic protein binding ability was more related to the small compounds present in this homogenate than with the aqueous phase ionic strength.