2024 Posters
Sustainable Protein
Tiffany Amat, MA/Food Science Ingineer (she/her/hers)
PhD Student
L'Institut Agro Dijon
Dijon, Bourgogne, France
Rémi Saurel (he/him/his)
Professor
L'Institut Agro Dijon
Dijon, France
Ali Assifaoui (he/him/his)
Professor
L'Institut Agro Dijon
Dijon, France
Christophe Schmitt, PhD (he/him/his)
Protein Senior Expert - Leader Plant Protein Strategic Network Research
Nestlé Research, Nestlé Institute of Food Sciences
Lausanne, Vaud, Switzerland
Juliana Valle Costa Silva (she/her/hers)
PhD
Nestlé Research, Nestlé Institute of Food Sciences
Lausanne, Switzerland
Johann Buczkowski (he/him/his)
Research Assistant
Nestlé Research, Nestlé Institute of Food Sciences
Lausanne, Switzerland
Recently, a raising interest for faba bean ingredients arose as valuable protein-rich alternative to other pulses. Besides, it contains significant amount of minerals (calcium) and phytic acid (PA) molecules which remain in food ingredients after processing [1]. Considered as antinutrient, PA forms complexes with proteins and calcium impairing their digestibility and bioavailability. The aim of this work is to compare the affinity of two globulin extracts, isolated by selective separation (E1) and isoelectric point precipitation (E2), to interact with calcium ions and PA. Firstly, globulin isolates were characterized in terms of protein composition (SEC-HPLC, µDSC, SDS-PAGE electrophoresis) and mineral contents. Calcium binding capacities were evaluated in globulin dispersions (2.5% proteins) at pHs: 4.5, 5.5, 6.5 and 7.5, by addition of CaCl2 (Fig. 1). Free calcium concentrations were assessed by calcium sensor. Results evidenced the pH influence on the ability of globulin systems to associate calcium. Close to their pI (~4.5), proteins are less charged and hardly bound calcium molecules. Neutral pHs (6.5 and 7.5) highlighted the significant calcium binding capacities of globulin systems by formation of insoluble complexes with protein precipitation. Also, globulin E2 extract appeared more denatured and contained more phytic acid. Modifications of conformation and charge accessibility induced better calcium chelation effects for globulin E2 systems (Fig. 1).