Sophie Beaubier
Verified @univ-lorraine.fr
University of Lorraine
Laboratoire Réaction et Génie des Procédés - LRGP (UMR CNRS 7274)
RESEARCH INTERESTS
Bioprocesses
Plant proteins
Enzymatic transformation
Modelization and optimization of bioprocesses
Scopus Publications
Scholar Citations
Scholar h-index
Scholar i10-index
Scopus Publications
Sophie Beaubier, Sara Albe-Slabi, Luna Beau, Olivier Galet, and Romain Kapel
Elsevier BV
Sara Albe-Slabi, Odile Mesieres, Sophie Beaubier, Luna Beau, Arnaud Aymes, Thibault Roques-Carmes, Véronique Sadtler, and Romain Kapel
Elsevier BV
Sophie Beaubier, Erwann Durand, Charles Lenclume, Frédéric Fine, Arnaud Aymes, Xavier Framboisier, Romain Kapel, and Pierre Villeneuve
Elsevier BV
Sophie Beaubier, Carlos Pineda-Vadillo, Odile Mesieres, Xavier Framboisier, Olivier Galet, and Romain Kapel
Elsevier BV
Nastassia Kaugarenia, Sophie Beaubier, Erwann Durand, Arnaud Aymes, Pierre Villeneuve, François Lesage, and Romain Kapel
MDPI AG
Preventing oxidation and microbial spoilage are both major concerns in food industries. In this context, this study aimed to valorize the total rapeseed meal proteins with controlled enzymatic proteolysis to generate potent mineral-chelating peptides from cruciferins while keeping intact the antimicrobial napins. Implementation of proteolysis of total rapeseed protein isolate with the Prolyve® enzyme highlighted an interesting selective hydrolysis of the cruciferins. Hence, the mechanism of this particular hydrolysis was investigated through a Design of Experiments method to obtain a model for the prediction of kinetics (cruciferin degradation and napin purity) according to the operating conditions applied. Then, multicriteria optimization was implemented to maximize the napin purity and yield while minimizing both enzymatic cost and reaction time. Antioxidant assays of the peptide fraction obtained under the optimal conditions proved the high metal-chelating activity preservation (EC50 = 247 ± 27 µg) for more than three times faster production. This fraction might counteract lipid oxidation or serve as preventing agents for micronutrient deficiencies, and the resulting purified napins may have applications in food safety against microbial contamination. These results can greatly help the development of rapeseed meal applications in food industries.
Sophie Beaubier, Claire Defaix, Sara Albe-Slabi, Arnaud Aymes, Olivier Galet, Frantz Fournier, and Romain Kapel
Elsevier BV
Juliane Calvez, Nadezda Khodorova, Sophie Beaubier, Alexandra Eymard, Daniel Tomé, and Claire Gaudichon
Springer Science and Business Media LLC
Sara Albe-Slabi, Claire Defaix, Sophie Beaubier, Olivier Galet, and Romain Kapel
Elsevier BV
Erwann Durand, Sophie Beaubier, Frederic Fine, Pierre Villeneuve, and Romain Kapel
Wiley
Sophie Beaubier, Sara Albe-Slabi, Arnaud Aymes, Marine Bianeis, Olivier Galet, and Romain Kapel
MDPI AG
Exploitation of plant proteins as an alternative to animal proteins currently presents an important challenge for food industries. In this contribution, total sunflower protein isolate from cold press meal was used as a starting material for the generation of highly soluble and functional hydrolysates that could be used in various food formulations. To do this, a rational and complete approach of controlled hydrolysis was implemented using the individual Alcalase and Prolyve enzymes. The method of stopping the hydrolysis reaction was also evaluated. The influence of operating conditions on hydrolysis kinetics and enzymatic mechanism was studied to identify the appropriate hydrolysis conditions. The gain of the solubility was then analyzed and compared to that of the initial proteins. Finally, the emulsifying and foaming properties (capacities and stabilities) of the resulting hydrolysates were also assessed. As a result, controlled enzymatic proteolysis significantly improved the sunflower protein solubility at neutral pH (twofold increase) and generated highly soluble hydrolysates. The limited proteolysis also maintained the good foam capacities and allowed an improvement in the initial foam stabilities and emulsifying capacities and stabilities of sunflower proteins. This contribution can greatly increase the value of sunflower meal and help in the development of sunflower protein products in the future.
Sophie Beaubier, Rémi Przybylski, Alice Bodin, Naïma Nedjar, Pascal Dhulster, and Romain Kapel
MDPI AG
Hydrolysis of bovine hemoglobin (bHb), the main constituent of bovine cruor by-product, releases a natural antimicrobial peptide (NKT) which could present a major interest for food safety. To enrich this, tangential ultrafiltration can be implemented, but ultrafiltration conditions are mainly empirically established. In this context, the application of a simulation method for predicting the NKT yield and enrichment was investigated. Ultrafiltration performances were studied for decolored bHb hydrolysates at different degrees of hydrolysis (DH; 3%, 5%, 10% and 18%) and colored hydrolysates (3% and 5% DH) with 1 and 3 kg·mol−1 regenerated cellulose membranes. The simulation method helped to identify the most promising hydrolysate (in terms of NKT enrichment, yield and productivity) as the 3% DH colored hydrolysate, and UF conditions (volumetric reduction factor of 5 and 3 with 1 and 3 kg·mol−1 membrane, respectively) for higher antimicrobial recovery. A maximal enrichment factor of about 29 and NKT purity of 70% in permeate were observed. The results showed that the antimicrobial activity was in relation with the process selectivity and NKT purity. Finally, this reliable method, applied for predicting the ultrafiltration performances to enrich peptides of interest, is part of a global approach to rationally valorize protein resources from various by-products.
Sophie Beaubier, Xavier Framboisier, Frantz Fournier, Olivier Galet, and Romain Kapel
Elsevier BV
Erwann Durand, Sophie Beaubier, Isidora Ilic, Frederic fine, Romain Kapel, and Pierre Villeneuve
Elsevier BV
Sophie Beaubier, Xavier Framboisier, Irina Ioannou, Olivier Galet, and Romain Kapel
Elsevier BV