Bioanalytical methods for the metalloproteomics study of bovine longissimus thoracis muscle tissue with different grades of meat tenderness in the Nellore breed (Bos indicus).

ABSTRACT

The work describes a metalloproteomics study of bovine muscle tissue with different grades of meat tenderness from animals of the Nellore breed (Bos indicus) based on protein separation by two-dimensional gel electrophoresis, the identification of calcium ions in protein spots by X-ray fluorescence (SR-XRF) and the characterisation of proteins by electrospray ionisation mass spectrometry. Forty (40) specimens were selected and divided into two experimental groups animals with tough meat (TO) and animals with tender meat (TE). A third group (P) of Piedmontese breed animals (Bos taurus) was included to serve as a comparative model for the level of meat tenderness. The procedures were efficient and preserved the metal-protein structure, enabling calcium detection in protein spots by SR-XRF at a given molecular weight range of 14-97kDa. Two proteins (pyruvate kinase and albumin) were inferred to be related to the phenotypical differences in animals from the different groups.