Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7595058 | Food Chemistry | 2015 | 8 Pages |
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 14-97Â kDa. Two proteins (pyruvate kinase and albumin) were inferred to be related to the phenotypical differences in animals from the different groups.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Welder Angelo Baldassini, Camila Pereira Braga, Luis Artur Loyola Chardulo, Josineudson Augusto II Vasconcelos Silva, Jessica Moraes Malheiros, Lúcia Galvão de Albuquerque, Talita Tanaka Fernandes, Pedro de Magalhães Padilha,