Proteins degradation value in cured meat product made from M-Cutaneous-omo brachialis muscle of bovine

We analyzed differences in some physicochemical parameters of proteins in shoulder rose (M. Cutaneous-omo brachialis) muscle as a result of beef processing to produce pastirma. Samples from processed muscles showed significantly increased concentrations of extracted proteins, especially of H2O P-ex and Guba-Straub-adenosine triphosphate solution (P < 0.01), as a result of the salting-curing process. The salt-curing process was likely to have an important effect on the extractability of muscle proteins such as myosin heavy chain (MHC) and water-soluble proteins, possibly as a result of releasing some proteins from each other and cleaving the structures between certain proteins. The fluorescence intensities of processed samples were higher than those of the control samples at all guanidine hydrochloride concentrations. The hydrophobicity also increased on account of new compounds that were created during the pastirma-making process. Since the process of making pastirma lasts about 4 weeks (drying), the metmyoglobin content was greatly increased in pastirma samples compared with the unprocessed samples (by as much as 57 %). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis results conceived that during processing of pastirma products, MHC and other muscle proteins degraded into polypeptides with smaller molecular weight lower than 15-kDa. The results of this study demonstrated that meat processing promoted the enzymatic digestion of some proteins, and the differences in composition between the control and pastirma samples were thus likely to be owing to protein degradation. The traditional pastirma-making process hence has no negative impact on the structure of the muscle and produces a firmer-textured.