Improvement of gluten-free bread properties by the incorporation of bovine plasma proteins and different saccharides into the matrix

2015 ◽  
Vol 170 ◽  
pp. 257-264 ◽  
Author(s):  
Laura T. Rodriguez Furlán ◽  
Antonio Pérez Padilla ◽  
Mercedes E. Campderrós
2020 ◽  
Vol 21 (2) ◽  
pp. 664 ◽  
Author(s):  
Sabrina Boudon ◽  
Joelle Henry-Berger ◽  
Isabelle Cassar-Malek

Beef quality is a complex phenotype that can be evaluated only after animal slaughtering. Previous research has investigated the potential of genetic markers or muscle-derived proteins to assess beef tenderness. Thus, the use of low-invasive biomarkers in living animals is an issue for the beef sector. We hypothesized that publicly available data may help us discovering candidate plasma biomarkers. Thanks to a review of the literature, we built a corpus of articles on beef tenderness. Following data collection, aggregation, and computational reconstruction of the muscle secretome, the putative plasma proteins were searched by comparison with a bovine plasma proteome atlas and submitted to mining of biological information. Of the 44 publications included in the study, 469 unique gene names were extracted for aggregation. Seventy-one proteins putatively released in the plasma were revealed. Among them 13 proteins were predicted to be secreted in plasma, 44 proteins as hypothetically secreted in plasma, and 14 additional candidate proteins were detected thanks to network analysis. Among these 71 proteins, 24 were included in tenderness quantitative trait loci. The in-silico workflow enabled the discovery of candidate plasma biomarkers for beef tenderness from reconstruction of the secretome, to be examined in the cattle plasma proteome.


2010 ◽  
Vol 43 (3) ◽  
pp. 788-796 ◽  
Author(s):  
Laura T. Rodríguez Furlán ◽  
Antonio Pérez Padilla ◽  
Mercedes E. Campderrós

2016 ◽  
Vol 07 (08) ◽  
pp. 671-681 ◽  
Author(s):  
Carina Lorena Fernández ◽  
Ricardo Alejandro Fogar ◽  
Mirtha Marina Doval ◽  
Ana María Romero ◽  
María Alicia Judis

1958 ◽  
Vol 4 (6) ◽  
pp. 496-509 ◽  
Author(s):  
Herndon G Shepherd ◽  
Hugh J McDonald

Abstract A colorimetric method has been adapted to the quantitative determination of the oral hypoglycemic compound phenethylbiguanide. This method was useful in studying the binding affinity of purified bovine plasma albumin and gamma globulin for the hypoglycemic agent. Equilibrium dialysis studies, which measure the decrease in thermodynamic activity of the bound cation, reveal that there is no significant interaction between phenethylbiguanide and the two native proteins. Consequently, the two plasma proteins are assumed to exert no buffering action in controlling the plasma concentration of the drug. The adherence of phenethylbiguanide to Beer's Law indicates that the compound exists in the monomeric state in aqueous solution below 10-4 molar.


1997 ◽  
Vol 45 (8) ◽  
pp. 2919-2923 ◽  
Author(s):  
Thomas A. Seymour ◽  
Margo Y. Peters ◽  
Michael T. Morrissey ◽  
Haejung An

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