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

•2D-PAGE efficiently proteins with different grades of meat tenderness.•Total protein extraction procedures preserved the metal–protein structure.•Pyruvate kinase and albumin were inferred to be related to the phenotypical differences.•Those two proteins likely partly explain the variation in the te...

Full description

Saved in:
Bibliographic Details
Published in:Food chemistry Vol. 169; pp. 65 - 72
Main Authors: Baldassini, Welder Angelo, Braga, Camila Pereira, Chardulo, Luis Artur Loyola, Silva, Josineudson Augusto II Vasconcelos, Malheiros, Jessica Moraes, de Albuquerque, Lúcia Galvão, Fernandes, Talita Tanaka, Padilha, Pedro de Magalhães
Format: Journal Article
Language:English
Published: England Elsevier Ltd 15-02-2015
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:•2D-PAGE efficiently proteins with different grades of meat tenderness.•Total protein extraction procedures preserved the metal–protein structure.•Pyruvate kinase and albumin were inferred to be related to the phenotypical differences.•Those two proteins likely partly explain the variation in the tenderness of their meat. 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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2014.07.131