Characterization of thermostable antigens of different species of meat animals

Abstract

Meat species adulteration is a universal problem, which violates food labeling laws, constitutes fraud, and raises ethical, religious and food-safety concerns. Mixing of different species followed by grinding and/or heat processing adds to the analytical techniques such as electrophoresis and chromatography. Immunological techniques using heat (thermo) stable muscle antigens (TMAs) prepared from tissue of meat animals have shown promise in the detection of adulteration. Therefore the present study was undertaken with an aim to characterize TMAs obtained from ox, buffalo, sheep and goat by SDS-PAGE and western blotting. TMAs, prepared from these species, were subjected to SDS-PAGE analysis which revealed number of proteins ranging from 7.9 to 166.5 kDa. The number and size of protein bands varied from species to species. The western blot analysis of ox and buffalo TMAs using anti-TMA serum raised in rabbits indicated number of species specific TMAs along with some cross reacting ones. Eliminating the cross reacting antigens and polypeptides of same molecular weight, it is concluded that the proteins of molecular weight 166.5, 124.6, 35.5 and 27.3 present in ox TMA can be suggested for species-specific ox antisera production, while in buffalo TMA the proteins of molecular weight 100.7, 36.7, 19.4 and 14.9 kDa which can be suggested for species-specific buffalo antisera production for the detection of adulteration of other meats with ox and buffalo meat.