Abstract
Marinating with calcium chloride had been employed to activate the endogenous proteolitic enzymatic system in muscle tissue. The activation of calpains leads to the disruption of major proteins responsible for myofilament structure. Nonetheless, intrinsic differences regarding enzymatic activity between different species need to be established, which concerns protein degradation and ultrastructural changes. In this study, four species—horse, chicken, rabbit and beef—were marinated in 150 mM CaCl2 solution. Calpain activity was determined by low and high molecular weight protein degradations (SDS-PAGE) and light microscopy, which was compared to a non-treated control. All the studied species presented an increase in the number of low molecular weight bands, corresponding to the 30 kDa polypeptide that resulted from tropomiosin degradation. High molecular weight protein degradation corresponds to the formation of breakdowns and amorphous regions in tissue micrographs. These results support the evidence of meat quality improvement by calcium marination.
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