FLEISCHWIRTSCHAFT international 3/2018

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52 Fleischwirtschaft international 3_2018 Research & Development Microstructural and physicochemical properties of seekhkebabs Fig. 1: Scanning electron micrographs (SEM) of kebabs processed by (a) charcoal grilling (b) roasting and (c) smoking Results and discussion Cooking loss and proximate composition The physical properties of meat and eating quality have been largely affected by cooking temperature and time. The cooking loss and proximate composition of kebabs processed by grilling, roasting and smoking are presented in the Table. The cooking method had a significant (P
..................................................................................................................................................................... Fleischwirtschaft international 3_2018 53 Research & Development cant damage to the microstructure of muscle fibers was observed in smoked kebabs, which presented a dense protein matrix characteristic of heat induced protein gels. Remarkable structural changes in smoked kebabs might be due to cellular membrane destruction, transverse and longitudinal shrinkage of muscle fibers, aggregation and gel formation of sarcoplasmic proteins, and shrinkage and solubilisation of connective tissue (KONG et al., 2008). SDSPAGE profile The SDSPAGE profile of the total protein extract from different kebab samples is shown in Figure 2. The figure indicated multiple protein bands in the molecular weight range between 45.0 and 212 kDa. In our study, the protein profile assessed by SDSPAGE showed a marked difference in protein expression pattern under three different cooking conditions. The content of proteins (possibly actin) with a molecular weight of around 43–44 kDa distinctly decreased in the smoking process. In roasting, the content of proteins with molecular weight of 66 kDa increased significantly but became weak and even disappeared in grilling and smoking, respectively. It was found that the protein intensity with the molecular weight of 212 kDa (possibly myosin heavy chain) decreased when samples were subjected to smoking. Our results could be explained as that increased cooking time in smoking has resulted in fragmentation of muscle proteins with higher molecular weight. Myosin from white fibers has been reported to be less thermally stable, thus more susceptible to denaturation, than myosin from red fibers in both beef (EGELANDSDAL et al., 1994) and chicken (LIU et al., 2015). Greater denaturation of myofibrillar proteins in smoked samples might be the probable reason for its higher cooking loss and hardness values in comparison to grilling and roasting. Sensory analysis Mean sensory scores (Fig. 3) revealed significant (P
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FLEISCHWIRTSCHAFT international 3/2018

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