Assessment of Functional Properties of Bovine Plasma Proteins Compared with Other Protein Concentrates, Application in a Hamburger Formulation

2011 ◽  
Vol 6 (9) ◽  
pp. 717-729 ◽  
Author(s):  
L.T. Rodriguez Furlan ◽  
A.N. Rinaldoni ◽  
A.P. Padilla ◽  
M.E. Campderros
Keyword(s):  
Functional Properties ◽  
Plasma Proteins ◽  
Protein Concentrates ◽  
Bovine Plasma

Enzymatic and extrusion pretreatments of defatted rice bran to improve functional properties of protein concentrates

2021 ◽  
Author(s):  
Francisco Henrique Pereira Neves Leal ◽  
Caroline de Almeida Senna ◽  
Larine Kupski ◽  
Gabriela da Rocha Lemos Mendes ◽  
Eliana Badiale‐Furlong
Keyword(s):  
Functional Properties ◽  
Rice Bran ◽  
Protein Concentrates ◽  
Defatted Rice Bran

scholarly journals Aggregation of Omic Data and Secretome Prediction Enable the Discovery of Candidate Plasma Biomarkers for Beef Tenderness

2020 ◽  
Vol 21 (2) ◽  
pp. 664 ◽  
Author(s):  
Sabrina Boudon ◽  
Joelle Henry-Berger ◽  
Isabelle Cassar-Malek
Keyword(s):  
Plasma Proteins ◽  
Biological Information ◽  
Plasma Proteome ◽  
Complex Phenotype ◽  
Beef Tenderness ◽  
Plasma Biomarkers ◽  
Bovine Plasma ◽  
Computational Reconstruction ◽  
Beef Sector ◽  
Omic Data

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.

scholarly journals Understanding the impact of moderate-intensity pulsed electric fields (MIPEF) on structural and functional characteristics of pea, rice and gluten concentrates

2020 ◽  
Vol 13 (12) ◽  
pp. 2145-2155
Author(s):  
Sofia Melchior ◽  
Sonia Calligaris ◽  
Giulia Bisson ◽  
Lara Manzocco
Keyword(s):  
Electric Fields ◽  
Functional Properties ◽  
Structural Changes ◽  
Pulsed Electric Fields ◽  
Moderate Intensity ◽  
Intramolecular Rearrangement ◽  
Structural Modifications ◽  
Protein Concentrates ◽  
Protein Nature ◽  
The Impact

Abstract Aim The effect of moderate-intensity pulsed electric fields (MIPEF) was evaluated on vegetable protein concentrates from pea, rice, and gluten. Methods Five percent (w/w) suspensions of protein concentrates (pH 5 and 6) were exposed to up to 60,000 MIPEF pulses at 1.65 kV/cm. Both structural modifications (absorbance at 280 nm, free sulfhydryl groups, FT-IR-spectra) and functional properties (solubility, water and oil holding capacity, foamability) were analyzed. Results MIPEF was able to modify protein structure by inducing unfolding, intramolecular rearrangement, and formation of aggregates. However, these effects were strongly dependent on protein nature and pH. In the case of rice and pea samples, structural changes were associated with negligible modifications in functional properties. By contrast, noticeable changes in these properties were observed for gluten samples, especially after exposure to 20,000 pulses. In particular, at pH 6, an increase in water and oil holding capacity of gluten was detected, while at pH 5, its solubility almost doubled. Conclusion These results suggest the potential of MIPEF to steer structure of proteins and enhance their technological functionality.

Functional properties of protein concentrates of KB6 kenaf (Hibiscus cannabinus) seed and its milky extract

LWT ◽  
2021 ◽  
Vol 135 ◽  
pp. 110234
Author(s):  
Shafa'atu Giwa Ibrahim ◽  
Wan Zunairah Wan Ibadullah ◽  
Nazamid Saari ◽  
Roselina Karim
Keyword(s):  
Functional Properties ◽  
Hibiscus Cannabinus ◽  
Protein Concentrates
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