Traditional cured meat-making process degrades the proteins of M. latissimus dorsi of bovine

This study investigated the changes in some properties of protein in cured meat product (Pastirma) made from the M. latissimus dorsi (LAT) muscle of cattle as a result of traditional process. As an effect of the salting and curing process, protein extractabilities were significantly increased in Pastirma muscles when compared to the fresh cuts (P 0.01). The analysis of fluorescent intensity showed that values of processed samples were higher than those of the control samples at all guanidine-Hydrochloride (Gu-HCl) concentrations. The increase in the hydrophobicity is a vital key of indication that new peptides were created during the traditional pastirma-making process. The metmyoglobin percentage was greatly increased to a great extent (by as much as 55%) in pastirma samples compared to the fresh samples. The coloured images of histological sections also exhibit the pastirma processing had no negative influence on the structure of the muscle but results in a firmer construction of the processed meat muscle. The SDS-PAGE patterns suggest that this traditionally type of process catalyzed indispensable enzymatic digestion on muscle proteins. Results also imply that during processing of pastirma products myosin heavy chain (MHC) degraded into polypeptides with a molecular weight in the range of lower than 20- kDa. The differences in the protein structure between the control and pastirma samples were thus likely to be contributable to protein digestion in which make it palatable and the most famous meat product throughout Turkey. Compounds identified in this study are important to pastirma flavor, and some compounds have been linked to specific flavors such as the fruity and spicy taste.